메뉴 건너뛰기




Volumn 63, Issue , 2013, Pages 1-47

Haem-based sensors: A still growing old superfamily

Author keywords

Chimeric proteins; Gene regulating; Globin coupled sensors; Haem based sensors; Structure function relationship

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; C REACTIVE PROTEIN; CARBON MONOXIDE; CHIMERIC PROTEIN; DIMER; DNA; DNA BINDING PROTEIN; GLOBIN; HAEM BASED SENSOR; HEME; HISTIDINE; MEMBRANE PROTEIN; OXYGEN; PROTEIN HISTIDINE KINASE; RETINOIC ACID RECEPTOR GAMMA; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR BMAL1; TRANSCRIPTION FACTOR NPAS2; TRANSCRIPTION FACTOR PAS; UNCLASSIFIED DRUG;

EID: 84884182583     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-407693-8.00001-7     Document Type: Chapter
Times cited : (14)

References (206)
  • 1
    • 80051726238 scopus 로고    scopus 로고
    • Regulatory cohesion of cell cycle and cell differentiation through interlinked phosphorylation and second messenger networks
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]
    • Abel S., Chien P., Wassmann P., Schirmer T., Kaever V., Laub M.T., et al. Regulatory cohesion of cell cycle and cell differentiation through interlinked phosphorylation and second messenger networks. Molecular Cell 2011, 43(4):550-560. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]. 10.1016/j.molcel.2011.07.018.
    • (2011) Molecular Cell , vol.43 , Issue.4 , pp. 550-560
    • Abel, S.1    Chien, P.2    Wassmann, P.3    Schirmer, T.4    Kaever, V.5    Laub, M.T.6
  • 2
    • 0037466485 scopus 로고    scopus 로고
    • O2-specific regulation of the ferrous heme-based sensor kinase FixL from Sinorhizobium meliloti and its aberrant inactivation in the ferric form
    • [Research Support, Non-U.S. Gov't]
    • Akimoto S., Tanaka A., Nakamura K., Shiro Y., Nakamura H. O2-specific regulation of the ferrous heme-based sensor kinase FixL from Sinorhizobium meliloti and its aberrant inactivation in the ferric form. Biochemical and Biophysical Research Communications 2003, 304(1):136-142. [Research Support, Non-U.S. Gov't].
    • (2003) Biochemical and Biophysical Research Communications , vol.304 , Issue.1 , pp. 136-142
    • Akimoto, S.1    Tanaka, A.2    Nakamura, K.3    Shiro, Y.4    Nakamura, H.5
  • 3
    • 4344573215 scopus 로고    scopus 로고
    • Activation mechanisms of transcriptional regulator CooA revealed by small-angle X-ray scattering
    • [Research Support, Non-U.S. Gov't]
    • Akiyama S., Fujisawa T., Ishimori K., Morishima I., Aono S. Activation mechanisms of transcriptional regulator CooA revealed by small-angle X-ray scattering. Journal of Molecular Biology 2004, 341(3):651-668. [Research Support, Non-U.S. Gov't]. 10.1016/j.jmb.2004.06.040.
    • (2004) Journal of Molecular Biology , vol.341 , Issue.3 , pp. 651-668
    • Akiyama, S.1    Fujisawa, T.2    Ishimori, K.3    Morishima, I.4    Aono, S.5
  • 4
    • 84874772938 scopus 로고    scopus 로고
    • Proteins involved in electron transfer to Fe(III) and Mn(IV) oxides by Geobacter sulfurreducens and Geobacter uraniireducens
    • Aklujkar M., Coppi M.V., Leang C., Kim B.C., Chavan M.A., Perpetua L.A., et al. Proteins involved in electron transfer to Fe(III) and Mn(IV) oxides by Geobacter sulfurreducens and Geobacter uraniireducens. Microbiology 2013, 159(Pt 3):515-535. 10.1099/mic.0.064089-0.
    • (2013) Microbiology , vol.159 , Issue.PART 3 , pp. 515-535
    • Aklujkar, M.1    Coppi, M.V.2    Leang, C.3    Kim, B.C.4    Chavan, M.A.5    Perpetua, L.A.6
  • 5
    • 34248164348 scopus 로고    scopus 로고
    • Microarray analysis of oxidative stress regulated genes in mesencephalic dopaminergic neuronal cells: Relevance to oxidative damage in Parkinson's disease
    • [Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural]
    • Anantharam V., Lehrmann E., Kanthasamy A., Yang Y., Banerjee P., Becker K.G., et al. Microarray analysis of oxidative stress regulated genes in mesencephalic dopaminergic neuronal cells: Relevance to oxidative damage in Parkinson's disease. Neurochemistry International 2007, 50(6):834-847. [Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural]. 10.1016/j.neuint.2007.02.003.
    • (2007) Neurochemistry International , vol.50 , Issue.6 , pp. 834-847
    • Anantharam, V.1    Lehrmann, E.2    Kanthasamy, A.3    Yang, Y.4    Banerjee, P.5    Becker, K.G.6
  • 6
    • 0025969319 scopus 로고
    • The regulatory status of the fixL- and fixJ-like genes in Bradyrhizobium japonicum may be different from that in Rhizobium meliloti
    • [Research Support, Non-U.S. Gov't]
    • Anthamatten D., Hennecke H. The regulatory status of the fixL- and fixJ-like genes in Bradyrhizobium japonicum may be different from that in Rhizobium meliloti. Molecular and General Genetics 1991, 225(1):38-48. [Research Support, Non-U.S. Gov't].
    • (1991) Molecular and General Genetics , vol.225 , Issue.1 , pp. 38-48
    • Anthamatten, D.1    Hennecke, H.2
  • 7
    • 0026573942 scopus 로고
    • Characterization of a fixLJ-regulated Bradyrhizobium japonicum gene sharing similarity with the Escherichia coli fnr and Rhizobium meliloti fixK genes
    • [Comparative Study. Research Support, Non-U.S. Gov't]
    • Anthamatten D., Scherb B., Hennecke H. Characterization of a fixLJ-regulated Bradyrhizobium japonicum gene sharing similarity with the Escherichia coli fnr and Rhizobium meliloti fixK genes. Journal of Bacteriology 1992, 174(7):2111-2120. [Comparative Study. Research Support, Non-U.S. Gov't].
    • (1992) Journal of Bacteriology , vol.174 , Issue.7 , pp. 2111-2120
    • Anthamatten, D.1    Scherb, B.2    Hennecke, H.3
  • 8
    • 0037134550 scopus 로고    scopus 로고
    • Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis
    • [Research Support, Non-U.S. Gov't]
    • Aono S., Kato T., Matsuki M., Nakajima H., Ohta T., Uchida T., et al. Resonance Raman and ligand binding studies of the oxygen-sensing signal transducer protein HemAT from Bacillus subtilis. Journal of Biological Chemistry 2002, 277(16):13528-13538. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M112256200.
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.16 , pp. 13528-13538
    • Aono, S.1    Kato, T.2    Matsuki, M.3    Nakajima, H.4    Ohta, T.5    Uchida, T.6
  • 9
    • 0030597287 scopus 로고    scopus 로고
    • A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum
    • [Research Support, Non-U.S. Gov't]
    • Aono S., Nakajima H., Saito K., Okada M. A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum. Biochemical and Biophysical Research Communications 1996, 228(3):752-756. [Research Support, Non-U.S. Gov't]. 10.1006/bbrc.1996.1727.
    • (1996) Biochemical and Biophysical Research Communications , vol.228 , Issue.3 , pp. 752-756
    • Aono, S.1    Nakajima, H.2    Saito, K.3    Okada, M.4
  • 10
    • 0033516892 scopus 로고    scopus 로고
    • Recognition of target DNA and transcription activation by the CO-sensing transcriptional activator CooA
    • [Research Support, Non-U.S. Gov't]
    • Aono S., Takasaki H., Unno H., Kamiya T., Nakajima H. Recognition of target DNA and transcription activation by the CO-sensing transcriptional activator CooA. Biochemical and Biophysical Research Communications 1999, 261(2):270-275. [Research Support, Non-U.S. Gov't]. 10.1006/bbrc.1999.1046.
    • (1999) Biochemical and Biophysical Research Communications , vol.261 , Issue.2 , pp. 270-275
    • Aono, S.1    Takasaki, H.2    Unno, H.3    Kamiya, T.4    Nakajima, H.5
  • 11
    • 0035899964 scopus 로고    scopus 로고
    • Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity
    • [Research Support, Non-U.S. Gov't]
    • Ausmees N., Mayer R., Weinhouse H., Volman G., Amikam D., Benziman M., et al. Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity. FEMS Microbiology Letters 2001, 204(1):163-167. [Research Support, Non-U.S. Gov't].
    • (2001) FEMS Microbiology Letters , vol.204 , Issue.1 , pp. 163-167
    • Ausmees, N.1    Mayer, R.2    Weinhouse, H.3    Volman, G.4    Amikam, D.5    Benziman, M.6
  • 12
    • 56249132984 scopus 로고    scopus 로고
    • Changes in quaternary structure in the signaling mechanisms of PAS domains
    • [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.]
    • Ayers R.A., Moffat K. Changes in quaternary structure in the signaling mechanisms of PAS domains. Biochemistry 2008, 47(46):12078-12086. [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.]. 10.1021/bi801254c.
    • (2008) Biochemistry , vol.47 , Issue.46 , pp. 12078-12086
    • Ayers, R.A.1    Moffat, K.2
  • 13
    • 33144485743 scopus 로고    scopus 로고
    • Functional implications of the propionate 7-arginine 220 interaction in the FixLH oxygen sensor from Bradyrhizobium japonicum
    • [Research Support, Non-U.S. Gov't]
    • Balland V., Bouzhir-Sima L., Anxolabehere-Mallart E., Boussac A., Vos M.H., Liebl U., et al. Functional implications of the propionate 7-arginine 220 interaction in the FixLH oxygen sensor from Bradyrhizobium japonicum. Biochemistry 2006, 45(7):2072-2084. [Research Support, Non-U.S. Gov't]. 10.1021/bi051696h.
    • (2006) Biochemistry , vol.45 , Issue.7 , pp. 2072-2084
    • Balland, V.1    Bouzhir-Sima, L.2    Anxolabehere-Mallart, E.3    Boussac, A.4    Vos, M.H.5    Liebl, U.6
  • 14
    • 17644380996 scopus 로고    scopus 로고
    • Role of arginine 220 in the oxygen sensor FixL from Bradyrhizobium japonicum
    • [Research Support, Non-U.S. Gov't]
    • Balland V., Bouzhir-Sima L., Kiger L., Marden M.C., Vos M.H., Liebl U., et al. Role of arginine 220 in the oxygen sensor FixL from Bradyrhizobium japonicum. Journal of Biological Chemistry 2005, 280(15):15279-15288. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M413928200.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 15279-15288
    • Balland, V.1    Bouzhir-Sima, L.2    Kiger, L.3    Marden, M.C.4    Vos, M.H.5    Liebl, U.6
  • 15
    • 0025995658 scopus 로고
    • In vitro activity of the nitrogen fixation regulatory protein FIXJ from Rhizobium meliloti
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Batut J., Santero E., Kustu S. In vitro activity of the nitrogen fixation regulatory protein FIXJ from Rhizobium meliloti. Journal of Bacteriology 1991, 173(18):5914-5917. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (1991) Journal of Bacteriology , vol.173 , Issue.18 , pp. 5914-5917
    • Batut, J.1    Santero, E.2    Kustu, S.3
  • 16
    • 84862676513 scopus 로고    scopus 로고
    • Effect of DNA binding on geminate CO recombination kinetics in CO-sensing transcription factor CooA
    • [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.]
    • Benabbas A., Karunakaran V., Youn H., Poulos T.L., Champion P.M. Effect of DNA binding on geminate CO recombination kinetics in CO-sensing transcription factor CooA. Journal of Biological Chemistry 2012, 287(26):21729-21740. [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.]. 10.1074/jbc.M112.345090.
    • (2012) Journal of Biological Chemistry , vol.287 , Issue.26 , pp. 21729-21740
    • Benabbas, A.1    Karunakaran, V.2    Youn, H.3    Poulos, T.L.4    Champion, P.M.5
  • 17
    • 84867830765 scopus 로고    scopus 로고
    • Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor
    • Blank M., Burmester T. Widespread occurrence of N-terminal acylation in animal globins and possible origin of respiratory globins from a membrane-bound ancestor. Molecular and Biological Evolution 2012, 29(11):3553-3561. 10.1093/molbev/mss164.
    • (2012) Molecular and Biological Evolution , vol.29 , Issue.11 , pp. 3553-3561
    • Blank, M.1    Burmester, T.2
  • 18
    • 15444350252 scopus 로고    scopus 로고
    • The complete genome sequence of Escherichia coli K-12
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Blattner F.R., Plunkett G., Bloch C.A., Perna N.T., Burland V., Riley M., et al. The complete genome sequence of Escherichia coli K-12. Science 1997, 277(5331):1453-1462. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (1997) Science , vol.277 , Issue.5331 , pp. 1453-1462
    • Blattner, F.R.1    Plunkett, G.2    Bloch, C.A.3    Perna, N.T.4    Burland, V.5    Riley, M.6
  • 19
    • 78651109050 scopus 로고    scopus 로고
    • Systematic analysis of cyclic di-GMP signalling enzymes and their role in biofilm formation and virulence in Yersinia pestis
    • [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.]
    • Bobrov A.G., Kirillina O., Ryjenkov D.A., Waters C.M., Price P.A., Fetherston J.D., et al. Systematic analysis of cyclic di-GMP signalling enzymes and their role in biofilm formation and virulence in Yersinia pestis. Molecular Microbiology 2011, 79(2):533-551. [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.]. 10.1111/j.1365-2958.2010.07470.x.
    • (2011) Molecular Microbiology , vol.79 , Issue.2 , pp. 533-551
    • Bobrov, A.G.1    Kirillina, O.2    Ryjenkov, D.A.3    Waters, C.M.4    Price, P.A.5    Fetherston, J.D.6
  • 20
    • 34447537731 scopus 로고    scopus 로고
    • A novel chimera: The "truncated hemoglobin-antibiotic monooxygenase" from Streptomyces avermitilis
    • [Research Support, Non-U.S. Gov't]
    • Bonamore A., Attili A., Arenghi F., Catacchio B., Chiancone E., Morea V., et al. A novel chimera: The "truncated hemoglobin-antibiotic monooxygenase" from Streptomyces avermitilis. Gene 2007, 398(1-2):52-61. [Research Support, Non-U.S. Gov't]. 10.1016/j.gene.2007.01.038.
    • (2007) Gene , vol.398 , Issue.1-2 , pp. 52-61
    • Bonamore, A.1    Attili, A.2    Arenghi, F.3    Catacchio, B.4    Chiancone, E.5    Morea, V.6
  • 21
    • 33947313309 scopus 로고    scopus 로고
    • Structure-based hypothesis on the activation of the CO-sensing transcription factor CooA
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Borjigin M., Li H., Lanz N.D., Kerby R.L., Roberts G.P., Poulos T.L. Structure-based hypothesis on the activation of the CO-sensing transcription factor CooA. Acta Crystallographica. Section D, Biological Crystallography 2007, 63(Pt 3):282-287. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1107/S0907444906051638.
    • (2007) Acta Crystallographica. Section D, Biological Crystallography , vol.63 , Issue.PART 3 , pp. 282-287
    • Borjigin, M.1    Li, H.2    Lanz, N.D.3    Kerby, R.L.4    Roberts, G.P.5    Poulos, T.L.6
  • 22
    • 42049122814 scopus 로고    scopus 로고
    • Regulation of bacterial RNA polymerase sigma factor activity: A structural perspective
    • [Research Support, N.I.H., Extramural Review]
    • Campbell E.A., Westblade L.F., Darst S.A. Regulation of bacterial RNA polymerase sigma factor activity: A structural perspective. Current Opinion in Microbiology 2008, 11(2):121-127. [Research Support, N.I.H., Extramural Review]. 10.1016/j.mib.2008.02.016.
    • (2008) Current Opinion in Microbiology , vol.11 , Issue.2 , pp. 121-127
    • Campbell, E.A.1    Westblade, L.F.2    Darst, S.A.3
  • 23
    • 79959338646 scopus 로고    scopus 로고
    • Cellular stoichiometry of the chemotaxis proteins in Bacillus subtilis
    • [Comparative Study Research Support, N.I.H., Extramural]
    • Cannistraro V.J., Glekas G.D., Rao C.V., Ordal G.W. Cellular stoichiometry of the chemotaxis proteins in Bacillus subtilis. Journal of Bacteriology 2011, 193(13):3220-3227. [Comparative Study Research Support, N.I.H., Extramural]. 10.1128/JB.01255-10.
    • (2011) Journal of Bacteriology , vol.193 , Issue.13 , pp. 3220-3227
    • Cannistraro, V.J.1    Glekas, G.D.2    Rao, C.V.3    Ordal, G.W.4
  • 24
    • 0035957226 scopus 로고    scopus 로고
    • Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter xylinum, is a heme-based sensor
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Chang A.L., Tuckerman J.R., Gonzalez G., Mayer R., Weinhouse H., Volman G., et al. Phosphodiesterase A1, a regulator of cellulose synthesis in Acetobacter xylinum, is a heme-based sensor. Biochemistry 2001, 40(12):3420-3426. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (2001) Biochemistry , vol.40 , Issue.12 , pp. 3420-3426
    • Chang, A.L.1    Tuckerman, J.R.2    Gonzalez, G.3    Mayer, R.4    Weinhouse, H.5    Volman, G.6
  • 25
    • 0141677745 scopus 로고    scopus 로고
    • A supramolecular complex in the environmental stress signalling pathway of Bacillus subtilis
    • [Research Support, Non-U.S. Gov't]
    • Chen C.C., Lewis R.J., Harris R., Yudkin M.D., Delumeau O. A supramolecular complex in the environmental stress signalling pathway of Bacillus subtilis. Molecular Microbiology 2003, 49(6):1657-1669. [Research Support, Non-U.S. Gov't].
    • (2003) Molecular Microbiology , vol.49 , Issue.6 , pp. 1657-1669
    • Chen, C.C.1    Lewis, R.J.2    Harris, R.3    Yudkin, M.D.4    Delumeau, O.5
  • 27
    • 8344231645 scopus 로고    scopus 로고
    • Investigation of the role of the N-terminal proline, the distal heme ligand in the CO sensor CooA
    • [Research Support, U.S. Gov't, P.H.S.]
    • Clark R.W., Youn H., Parks R.B., Cherney M.M., Roberts G.P., Burstyn J.N. Investigation of the role of the N-terminal proline, the distal heme ligand in the CO sensor CooA. Biochemistry 2004, 43(44):14149-14160. [Research Support, U.S. Gov't, P.H.S.]. 10.1021/bi0487948.
    • (2004) Biochemistry , vol.43 , Issue.44 , pp. 14149-14160
    • Clark, R.W.1    Youn, H.2    Parks, R.B.3    Cherney, M.M.4    Roberts, G.P.5    Burstyn, J.N.6
  • 28
    • 20344374161 scopus 로고    scopus 로고
    • Conserved modular design of an oxygen sensory/signaling network with species-specific output
    • [Comparative Study Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Crosson S., McGrath P.T., Stephens C., McAdams H.H., Shapiro L. Conserved modular design of an oxygen sensory/signaling network with species-specific output. Proceedings of the National Academy of Sciences of the United States of America 2005, 102(22):8018-8023. [Comparative Study Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]. 10.1073/pnas.0503022102.
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.22 , pp. 8018-8023
    • Crosson, S.1    McGrath, P.T.2    Stephens, C.3    McAdams, H.H.4    Shapiro, L.5
  • 30
    • 33947193633 scopus 로고    scopus 로고
    • Cryptochromes impair phosphorylation of transcriptional activators in the clock: A general mechanism for circadian repression
    • [Research Support, Non-U.S. Gov't]
    • Dardente H., Fortier E.E., Martineau V., Cermakian N. Cryptochromes impair phosphorylation of transcriptional activators in the clock: A general mechanism for circadian repression. Biochemical Journal 2007, 402(3):525-536. [Research Support, Non-U.S. Gov't]. 10.1042/BJ20060827.
    • (2007) Biochemical Journal , vol.402 , Issue.3 , pp. 525-536
    • Dardente, H.1    Fortier, E.E.2    Martineau, V.3    Cermakian, N.4
  • 31
    • 0023731837 scopus 로고
    • Cascade regulation of nif gene expression in Rhizobium meliloti
    • [Research Support, Non-U.S. Gov't]
    • David M., Daveran M.L., Batut J., Dedieu A., Domergue O., Ghai J., et al. Cascade regulation of nif gene expression in Rhizobium meliloti. Cell 1988, 54(5):671-683. [Research Support, Non-U.S. Gov't].
    • (1988) Cell , vol.54 , Issue.5 , pp. 671-683
    • David, M.1    Daveran, M.L.2    Batut, J.3    Dedieu, A.4    Domergue, O.5    Ghai, J.6
  • 32
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • [Research Support, U.S. Gov't, Non-P.H.S.]
    • Delgado-Nixon V.M., Gonzalez G., Gilles-Gonzalez M.A. Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor. Biochemistry 2000, 39(10):2685-2691. [Research Support, U.S. Gov't, Non-P.H.S.].
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 33
    • 84866556174 scopus 로고    scopus 로고
    • Cis-2-dodecenoic acid receptor RpfR links quorum-sensing signal perception with regulation of virulence through cyclic dimeric guanosine monophosphate turnover
    • [Research Support, Non-U.S. Gov't]
    • Deng Y., Schmid N., Wang C., Wang J., Pessi G., Wu D., et al. Cis-2-dodecenoic acid receptor RpfR links quorum-sensing signal perception with regulation of virulence through cyclic dimeric guanosine monophosphate turnover. Proceedings of the National Academy of Sciences of the United States of America 2012, 109(38):15479-15484. [Research Support, Non-U.S. Gov't]. 10.1073/pnas.1205037109.
    • (2012) Proceedings of the National Academy of Sciences of the United States of America , vol.109 , Issue.38 , pp. 15479-15484
    • Deng, Y.1    Schmid, N.2    Wang, C.3    Wang, J.4    Pessi, G.5    Wu, D.6
  • 34
    • 0025196088 scopus 로고
    • Rhizobium meliloti Fix L is an oxygen sensor and regulates R. meliloti nifA and fixK genes differently in Escherichia coli
    • [Research Support, Non-U.S. Gov't]
    • de Philip P., Batut J., Boistard P. Rhizobium meliloti Fix L is an oxygen sensor and regulates R. meliloti nifA and fixK genes differently in Escherichia coli. Journal of Bacteriology 1990, 172(8):4255-4262. [Research Support, Non-U.S. Gov't].
    • (1990) Journal of Bacteriology , vol.172 , Issue.8 , pp. 4255-4262
    • de Philip, P.1    Batut, J.2    Boistard, P.3
  • 35
    • 77955664479 scopus 로고    scopus 로고
    • The heme pocket of the globin domain of the globin-coupled sensor of Geobacter sulfurreducens-An EPR study
    • Desmet F., Thijs L., El Mkami H., Dewilde S., Moens L., Smith G., et al. The heme pocket of the globin domain of the globin-coupled sensor of Geobacter sulfurreducens-An EPR study. Journal of Inorganic Biochemistry 2010, 104(10):1022-1028. 10.1016/j.jinorgbio.2010.05.009.
    • (2010) Journal of Inorganic Biochemistry , vol.104 , Issue.10 , pp. 1022-1028
    • Desmet, F.1    Thijs, L.2    El Mkami, H.3    Dewilde, S.4    Moens, L.5    Smith, G.6
  • 36
    • 0031970498 scopus 로고    scopus 로고
    • The Rhizobium etli FixL protein differs in structure from other known FixL proteins
    • [Research Support, Non-U.S. Gov't]
    • D'Hooghe I., Michiels J., Vanderleyden J. The Rhizobium etli FixL protein differs in structure from other known FixL proteins. Molecular and General Genetics 1998, 257(5):576-580. [Research Support, Non-U.S. Gov't].
    • (1998) Molecular and General Genetics , vol.257 , Issue.5 , pp. 576-580
    • D'Hooghe, I.1    Michiels, J.2    Vanderleyden, J.3
  • 37
    • 0028851773 scopus 로고
    • Structural and functional analysis of the fixLJ genes of Rhizobium leguminosarum biovar phaseoli CNPAF512
    • [Comparative Study Research Support, Non-U.S. Gov't]
    • D'Hooghe I., Michiels J., Vlassak K., Verreth C., Waelkens F., Vanderleyden J. Structural and functional analysis of the fixLJ genes of Rhizobium leguminosarum biovar phaseoli CNPAF512. Molecular and General Genetics 1995, 249(1):117-126. [Comparative Study Research Support, Non-U.S. Gov't].
    • (1995) Molecular and General Genetics , vol.249 , Issue.1 , pp. 117-126
    • D'Hooghe, I.1    Michiels, J.2    Vlassak, K.3    Verreth, C.4    Waelkens, F.5    Vanderleyden, J.6
  • 38
    • 33746072949 scopus 로고    scopus 로고
    • The proteome of dissimilatory metal-reducing microorganism Geobacter sulfurreducens under various growth conditions
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Ding Y.H., Hixson K.K., Giometti C.S., Stanley A., Esteve-Nunez A., Khare T., et al. The proteome of dissimilatory metal-reducing microorganism Geobacter sulfurreducens under various growth conditions. Biochimica et Biophysica Acta 2006, 1764(7):1198-1206. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1016/j.bbapap.2006.04.017.
    • (2006) Biochimica et Biophysica Acta , vol.1764 , Issue.7 , pp. 1198-1206
    • Ding, Y.H.1    Hixson, K.K.2    Giometti, C.S.3    Stanley, A.4    Esteve-Nunez, A.5    Khare, T.6
  • 39
    • 0346668332 scopus 로고    scopus 로고
    • NPAS2: A gas-responsive transcription factor
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Dioum E.M., Rutter J., Tuckerman J.R., Gonzalez G., Gilles-Gonzalez M.A., McKnight S.L. NPAS2: A gas-responsive transcription factor. Science 2002, 298(5602):2385-2387. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]. 10.1126/science.1078456.
    • (2002) Science , vol.298 , Issue.5602 , pp. 2385-2387
    • Dioum, E.M.1    Rutter, J.2    Tuckerman, J.R.3    Gonzalez, G.4    Gilles-Gonzalez, M.A.5    McKnight, S.L.6
  • 40
    • 0023259464 scopus 로고
    • The nifA gene of Rhizobium meliloti is oxygen regulated
    • [Research Support, U.S. Gov't, Non-P.H.S.]
    • Ditta G., Virts E., Palomares A., Kim C.H. The nifA gene of Rhizobium meliloti is oxygen regulated. Journal of Bacteriology 1987, 169(7):3217-3223. [Research Support, U.S. Gov't, Non-P.H.S.].
    • (1987) Journal of Bacteriology , vol.169 , Issue.7 , pp. 3217-3223
    • Ditta, G.1    Virts, E.2    Palomares, A.3    Kim, C.H.4
  • 41
    • 0038454431 scopus 로고    scopus 로고
    • Altered patterns of sleep and behavioral adaptability in NPAS2-deficient mice
    • [Research Support, U.S. Gov't, P.H.S.]
    • Dudley C.A., Erbel-Sieler C., Estill S.J., Reick M., Franken P., Pitts S., et al. Altered patterns of sleep and behavioral adaptability in NPAS2-deficient mice. Science 2003, 301(5631):379-383. [Research Support, U.S. Gov't, P.H.S.]. 10.1126/science.1082795.
    • (2003) Science , vol.301 , Issue.5631 , pp. 379-383
    • Dudley, C.A.1    Erbel-Sieler, C.2    Estill, S.J.3    Reick, M.4    Franken, P.5    Pitts, S.6
  • 42
    • 58149485506 scopus 로고    scopus 로고
    • Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression
    • [Research Support, Non-U.S. Gov't]
    • Duerig A., Abel S., Folcher M., Nicollier M., Schwede T., Amiot N., et al. Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression. Genes & Development 2009, 23(1):93-104. [Research Support, Non-U.S. Gov't]. 10.1101/gad.502409.
    • (2009) Genes & Development , vol.23 , Issue.1 , pp. 93-104
    • Duerig, A.1    Abel, S.2    Folcher, M.3    Nicollier, M.4    Schwede, T.5    Amiot, N.6
  • 43
    • 0037663697 scopus 로고    scopus 로고
    • A distal arginine in oxygen-sensing heme-PAS domains is essential to ligand binding, signal transduction, and structure
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Dunham C.M., Dioum E.M., Tuckerman J.R., Gonzalez G., Scott W.G., Gilles-Gonzalez M.A. A distal arginine in oxygen-sensing heme-PAS domains is essential to ligand binding, signal transduction, and structure. Biochemistry 2003, 42(25):7701-7708. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]. 10.1021/bi0343370.
    • (2003) Biochemistry , vol.42 , Issue.25 , pp. 7701-7708
    • Dunham, C.M.1    Dioum, E.M.2    Tuckerman, J.R.3    Gonzalez, G.4    Scott, W.G.5    Gilles-Gonzalez, M.A.6
  • 44
    • 43749094347 scopus 로고    scopus 로고
    • Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy
    • [Research Support, Non-U.S. Gov't]
    • El-Mashtoly S.F., Gu Y., Yoshimura H., Yoshioka S., Aono S., Kitagawa T. Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy. Journal of Biological Chemistry 2008, 283(11):6942-6949. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M709209200.
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.11 , pp. 6942-6949
    • El-Mashtoly, S.F.1    Gu, Y.2    Yoshimura, H.3    Yoshioka, S.4    Aono, S.5    Kitagawa, T.6
  • 45
    • 84862001732 scopus 로고    scopus 로고
    • Site-specific protein dynamics in communication pathway from sensor to signaling domain of oxygen sensor protein, HemAT-Bs: Time-resolved Ultraviolet Resonance Raman Study
    • [Research Support, Non-U.S. Gov't]
    • El-Mashtoly S.F., Kubo M., Gu Y., Sawai H., Nakashima S., Ogura T., et al. Site-specific protein dynamics in communication pathway from sensor to signaling domain of oxygen sensor protein, HemAT-Bs: Time-resolved Ultraviolet Resonance Raman Study. Journal of Biological Chemistry 2012, 287(24):19973-19984. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M112.357855.
    • (2012) Journal of Biological Chemistry , vol.287 , Issue.24 , pp. 19973-19984
    • El-Mashtoly, S.F.1    Kubo, M.2    Gu, Y.3    Sawai, H.4    Nakashima, S.5    Ogura, T.6
  • 46
    • 49649105751 scopus 로고    scopus 로고
    • Roles of Arg-97 and Phe-113 in regulation of distal ligand binding to heme in the sensor domain of Ec DOS protein. Resonance Raman and mutation study
    • [Research Support, Non-U.S. Gov't]
    • El-Mashtoly S.F., Nakashima S., Tanaka A., Shimizu T., Kitagawa T. Roles of Arg-97 and Phe-113 in regulation of distal ligand binding to heme in the sensor domain of Ec DOS protein. Resonance Raman and mutation study. Journal of Biological Chemistry 2008, 283(27):19000-19010. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M801262200.
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.27 , pp. 19000-19010
    • El-Mashtoly, S.F.1    Nakashima, S.2    Tanaka, A.3    Shimizu, T.4    Kitagawa, T.5
  • 47
    • 33947665446 scopus 로고    scopus 로고
    • Ultraviolet resonance Raman evidence for utilization of the heme 6-propionate hydrogen-bond network in signal transmission from heme to protein in Ec DOS protein
    • [Research Support, Non-U.S. Gov't]
    • El-Mashtoly S.F., Takahashi H., Shimizu T., Kitagawa T. Ultraviolet resonance Raman evidence for utilization of the heme 6-propionate hydrogen-bond network in signal transmission from heme to protein in Ec DOS protein. Journal of the American Chemical Society 2007, 129(12):3556-3563. [Research Support, Non-U.S. Gov't]. 10.1021/ja0669777.
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.12 , pp. 3556-3563
    • El-Mashtoly, S.F.1    Takahashi, H.2    Shimizu, T.3    Kitagawa, T.4
  • 48
    • 84874641033 scopus 로고    scopus 로고
    • Common genetic variants in ARNTL and NPAS2 and at chromosome 12p13 are associated with objectively measured sleep traits in the elderly
    • Evans D.S., Parimi N., Nievergelt C.M., Blackwell T., Redline S., Ancoli-Israel S., et al. Common genetic variants in ARNTL and NPAS2 and at chromosome 12p13 are associated with objectively measured sleep traits in the elderly. Sleep 2013, 36(3):431-446. 10.5665/sleep.2466.
    • (2013) Sleep , vol.36 , Issue.3 , pp. 431-446
    • Evans, D.S.1    Parimi, N.2    Nievergelt, C.M.3    Blackwell, T.4    Redline, S.5    Ancoli-Israel, S.6
  • 49
    • 0141761124 scopus 로고    scopus 로고
    • The diversity of globin-coupled sensors
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review]
    • Freitas T.A., Hou S., Alam M. The diversity of globin-coupled sensors. FEBS Letters 2003, 552(2-3):99-104. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review].
    • (2003) FEBS Letters , vol.552 , Issue.2-3 , pp. 99-104
    • Freitas, T.A.1    Hou, S.2    Alam, M.3
  • 51
    • 10444268100 scopus 로고    scopus 로고
    • Globin-coupled sensors, protoglobins, and the last universal common ancestor
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review]
    • Freitas T.A., Saito J.A., Hou S., Alam M. Globin-coupled sensors, protoglobins, and the last universal common ancestor. Journal of Inorganic Biochemistry 2005, 99(1):23-33. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review]. 10.1016/j.jinorgbio.2004.10.024.
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 23-33
    • Freitas, T.A.1    Saito, J.A.2    Hou, S.3    Alam, M.4
  • 52
    • 84866330711 scopus 로고    scopus 로고
    • Two surfaces of a conserved interdomain linker differentially affect output from the RST sensing module of the Bacillus subtilis stressosome
    • [Research Support, N.I.H., Extramural]
    • Gaidenko T.A., Bie X., Baldwin E.P., Price C.W. Two surfaces of a conserved interdomain linker differentially affect output from the RST sensing module of the Bacillus subtilis stressosome. Journal of Bacteriology 2012, 194(15):3913-3921. [Research Support, N.I.H., Extramural]. 10.1128/JB.00583-12.
    • (2012) Journal of Bacteriology , vol.194 , Issue.15 , pp. 3913-3921
    • Gaidenko, T.A.1    Bie, X.2    Baldwin, E.P.3    Price, C.W.4
  • 53
    • 0034705398 scopus 로고    scopus 로고
    • Impaired cued and contextual memory in NPAS2-deficient mice
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Garcia J.A., Zhang D., Estill S.J., Michnoff C., Rutter J., Reick M., et al. Impaired cued and contextual memory in NPAS2-deficient mice. Science 2000, 288(5474):2226-2230. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (2000) Science , vol.288 , Issue.5474 , pp. 2226-2230
    • Garcia, J.A.1    Zhang, D.2    Estill, S.J.3    Michnoff, C.4    Rutter, J.5    Reick, M.6
  • 54
    • 0032486330 scopus 로고    scopus 로고
    • Role of the CLOCK protein in the mammalian circadian mechanism
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Gekakis N., Staknis D., Nguyen H.B., Davis F.C., Wilsbacher L.D., King D.P., et al. Role of the CLOCK protein in the mammalian circadian mechanism. Science 1998, 280(5369):1564-1569. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (1998) Science , vol.280 , Issue.5369 , pp. 1564-1569
    • Gekakis, N.1    Staknis, D.2    Nguyen, H.B.3    Davis, F.C.4    Wilsbacher, L.D.5    King, D.P.6
  • 55
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Gilles-Gonzalez M.A., Ditta G.S., Helinski D.R. A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature 1991, 350(6314):170-172. [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]. 10.1038/350170a0.
    • (1991) Nature , vol.350 , Issue.6314 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 56
    • 0027219226 scopus 로고
    • Regulation of the kinase activity of heme protein FixL from the two-component system FixL/FixJ of Rhizobium meliloti
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Gilles-Gonzalez M.A., Gonzalez G. Regulation of the kinase activity of heme protein FixL from the two-component system FixL/FixJ of Rhizobium meliloti. Journal of Biological Chemistry 1993, 268(22):16293-16297. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.22 , pp. 16293-16297
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 57
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review]
    • Gilles-Gonzalez M.A., Gonzalez G. Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses. Journal of Inorganic Biochemistry 2005, 99(1):1-22. [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review]. 10.1016/j.jinorgbio.2004.11.006.
    • (2005) Journal of Inorganic Biochemistry , vol.99 , Issue.1 , pp. 1-22
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 58
    • 0028949951 scopus 로고
    • Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Gilles-Gonzalez M.A., Gonzalez G., Perutz M.F. Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron. Biochemistry 1995, 34(1):232-236. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (1995) Biochemistry , vol.34 , Issue.1 , pp. 232-236
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3
  • 59
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation
    • [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Gilles-Gonzalez M.A., Gonzalez G., Perutz M.F., Kiger L., Marden M.C., Poyart C. Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation. Biochemistry 1994, 33(26):8067-8073. [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (1994) Biochemistry , vol.33 , Issue.26 , pp. 8067-8073
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3    Kiger, L.4    Marden, M.C.5    Poyart, C.6
  • 60
    • 0033676586 scopus 로고    scopus 로고
    • Differential regulation of fixN-reiterated genes in Rhizobium etli by a novel fixL-fixK cascade
    • [Research Support, Non-U.S. Gov't]
    • Girard L., Brom S., Davalos A., Lopez O., Soberon M., Romero D. Differential regulation of fixN-reiterated genes in Rhizobium etli by a novel fixL-fixK cascade. Molecular Plant-Microbe Interactions 2000, 13(12):1283-1292. [Research Support, Non-U.S. Gov't]. 10.1094/MPMI.2000.13.12.1283.
    • (2000) Molecular Plant-Microbe Interactions , vol.13 , Issue.12 , pp. 1283-1292
    • Girard, L.1    Brom, S.2    Davalos, A.3    Lopez, O.4    Soberon, M.5    Romero, D.6
  • 61
    • 0034636144 scopus 로고    scopus 로고
    • New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Gong W., Hao B., Chan M.K. New mechanistic insights from structural studies of the oxygen-sensing domain of Bradyrhizobium japonicum FixL. Biochemistry 2000, 39(14):3955-3962. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (2000) Biochemistry , vol.39 , Issue.14 , pp. 3955-3962
    • Gong, W.1    Hao, B.2    Chan, M.K.3
  • 62
    • 0032438105 scopus 로고    scopus 로고
    • Structure of a biological oxygen sensor: A new mechanism for heme-driven signal transduction
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Gong W., Hao B., Mansy S.S., Gonzalez G., Gilles-Gonzalez M.A., Chan M.K. Structure of a biological oxygen sensor: A new mechanism for heme-driven signal transduction. Proceedings of the National Academy of Sciences of the United States of America 1998, 95(26):15177-15182. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.26 , pp. 15177-15182
    • Gong, W.1    Hao, B.2    Mansy, S.S.3    Gonzalez, G.4    Gilles-Gonzalez, M.A.5    Chan, M.K.6
  • 63
    • 0037008046 scopus 로고    scopus 로고
    • Nature of the displaceable heme-axial residue in the EcDos protein, a heme-based sensor from Escherichia coli
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Gonzalez G., Dioum E.M., Bertolucci C.M., Tomita T., Ikeda-Saito M., Cheesman M.R., et al. Nature of the displaceable heme-axial residue in the EcDos protein, a heme-based sensor from Escherichia coli. Biochemistry 2002, 41(26):8414-8421. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (2002) Biochemistry , vol.41 , Issue.26 , pp. 8414-8421
    • Gonzalez, G.1    Dioum, E.M.2    Bertolucci, C.M.3    Tomita, T.4    Ikeda-Saito, M.5    Cheesman, M.R.6
  • 64
    • 0033572771 scopus 로고    scopus 로고
    • Structural transitions in the FixJ receiver domain
    • [Research Support, Non-U.S. Gov't]
    • Gouet P., Fabry B., Guillet V., Birck C., Mourey L., Kahn D., et al. Structural transitions in the FixJ receiver domain. Structure 1999, 7(12):1517-1526. [Research Support, Non-U.S. Gov't].
    • (1999) Structure , vol.7 , Issue.12 , pp. 1517-1526
    • Gouet, P.1    Fabry, B.2    Guillet, V.3    Birck, C.4    Mourey, L.5    Kahn, D.6
  • 65
    • 0034116376 scopus 로고    scopus 로고
    • The PAS superfamily: Sensors of environmental and developmental signals
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review]
    • Gu Y.Z., Hogenesch J.B., Bradfield C.A. The PAS superfamily: Sensors of environmental and developmental signals. Annual Review of Pharmacology and Toxicology 2000, 40:519-561. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review]. 10.1146/annurev.pharmtox.40.1.519.
    • (2000) Annual Review of Pharmacology and Toxicology , vol.40 , pp. 519-561
    • Gu, Y.Z.1    Hogenesch, J.B.2    Bradfield, C.A.3
  • 66
    • 0037195260 scopus 로고    scopus 로고
    • Structure-based mechanism of O2 sensing and ligand discrimination by the FixL heme domain of Bradyrhizobium japonicum
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Hao B., Isaza C., Arndt J., Soltis M., Chan M.K. Structure-based mechanism of O2 sensing and ligand discrimination by the FixL heme domain of Bradyrhizobium japonicum. Biochemistry 2002, 41(43):12952-12958. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (2002) Biochemistry , vol.41 , Issue.43 , pp. 12952-12958
    • Hao, B.1    Isaza, C.2    Arndt, J.3    Soltis, M.4    Chan, M.K.5
  • 67
    • 79251600033 scopus 로고    scopus 로고
    • Heme-binding characteristics of the isolated PAS-B domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms
    • [In Vitro Research Support, Non-U.S. Gov't]
    • Hayasaka K., Kitanishi K., Igarashi J., Shimizu T. Heme-binding characteristics of the isolated PAS-B domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms. Biochimica et Biophysica Acta 2011, 1814(2):326-333. [In Vitro Research Support, Non-U.S. Gov't]. 10.1016/j.bbapap.2010.09.007.
    • (2011) Biochimica et Biophysica Acta , vol.1814 , Issue.2 , pp. 326-333
    • Hayasaka, K.1    Kitanishi, K.2    Igarashi, J.3    Shimizu, T.4
  • 68
    • 0033574410 scopus 로고    scopus 로고
    • Transcription activation by CooA, the CO-sensing factor from Rhodospirillum rubrum. The interaction between CooA and the C-terminal domain of the alpha subunit of RNA polymerase
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • He Y., Gaal T., Karls R., Donohue T.J., Gourse R.L., Roberts G.P. Transcription activation by CooA, the CO-sensing factor from Rhodospirillum rubrum. The interaction between CooA and the C-terminal domain of the alpha subunit of RNA polymerase. Journal of Biological Chemistry 1999, 274(16):10840-10845. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.16 , pp. 10840-10845
    • He, Y.1    Gaal, T.2    Karls, R.3    Donohue, T.J.4    Gourse, R.L.5    Roberts, G.P.6
  • 69
    • 0030051489 scopus 로고    scopus 로고
    • Characterization of a CO-responsive transcriptional activator from Rhodospirillum rubrum
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • He Y., Shelver D., Kerby R.L., Roberts G.P. Characterization of a CO-responsive transcriptional activator from Rhodospirillum rubrum. Journal of Biological Chemistry 1996, 271(1):120-123. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.1 , pp. 120-123
    • He, Y.1    Shelver, D.2    Kerby, R.L.3    Roberts, G.P.4
  • 70
    • 80053291460 scopus 로고    scopus 로고
    • Ligand-binding PAS domains in a genomic, cellular, and structural context
    • [Review]
    • Henry J.T., Crosson S. Ligand-binding PAS domains in a genomic, cellular, and structural context. Annual Review of Microbiology 2011, 65:261-286. [Review]. 10.1146/annurev-micro-121809-151631.
    • (2011) Annual Review of Microbiology , vol.65 , pp. 261-286
    • Henry, J.T.1    Crosson, S.2
  • 71
    • 34249081123 scopus 로고    scopus 로고
    • Resonance Raman observation of the structural dynamics of FixL on signal transduction and ligand discrimination
    • [Comparative Study Research Support, Non-U.S. Gov't]
    • Hiruma Y., Kikuchi A., Tanaka A., Shiro Y., Mizutani Y. Resonance Raman observation of the structural dynamics of FixL on signal transduction and ligand discrimination. Biochemistry 2007, 46(20):6086-6096. [Comparative Study Research Support, Non-U.S. Gov't]. 10.1021/bi062083n.
    • (2007) Biochemistry , vol.46 , Issue.20 , pp. 6086-6096
    • Hiruma, Y.1    Kikuchi, A.2    Tanaka, A.3    Shiro, Y.4    Mizutani, Y.5
  • 72
    • 0034676026 scopus 로고    scopus 로고
    • Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor
    • Ho Y.S., Burden L.M., Hurley J.H. Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor. EMBO Journal 2000, 19(20):5288-5299. 10.1093/emboj/19.20.5288.
    • (2000) EMBO Journal , vol.19 , Issue.20 , pp. 5288-5299
    • Ho, Y.S.1    Burden, L.M.2    Hurley, J.H.3
  • 73
    • 53349145764 scopus 로고    scopus 로고
    • The circadian gene NPAS2, a putative tumor suppressor, is involved in DNA damage response
    • [Research Support, N.I.H., Extramural]
    • Hoffman A.E., Zheng T., Ba Y., Zhu Y. The circadian gene NPAS2, a putative tumor suppressor, is involved in DNA damage response. Molecular Cancer Research 2008, 6(9):1461-1468. [Research Support, N.I.H., Extramural]. 10.1158/1541-7786.MCR-07-2094.
    • (2008) Molecular Cancer Research , vol.6 , Issue.9 , pp. 1461-1468
    • Hoffman, A.E.1    Zheng, T.2    Ba, Y.3    Zhu, Y.4
  • 74
    • 0032510778 scopus 로고    scopus 로고
    • The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Hogenesch J.B., Gu Y.Z., Jain S., Bradfield C.A. The basic-helix-loop-helix-PAS orphan MOP3 forms transcriptionally active complexes with circadian and hypoxia factors. Proceedings of the National Academy of Sciences of the United States of America 1998, 95(10):5474-5479. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.10 , pp. 5474-5479
    • Hogenesch, J.B.1    Gu, Y.Z.2    Jain, S.3    Bradfield, C.A.4
  • 75
    • 0035486999 scopus 로고    scopus 로고
    • A globin-coupled oxygen sensor from the facultatively alkaliphilic Bacillus halodurans C-125
    • [Research Support, U.S. Gov't, Non-P.H.S.]
    • Hou S., Belisle C., Lam S., Piatibratov M., Sivozhelezov V., Takami H., et al. A globin-coupled oxygen sensor from the facultatively alkaliphilic Bacillus halodurans C-125. Extremophiles 2001, 5(5):351-354. [Research Support, U.S. Gov't, Non-P.H.S.].
    • (2001) Extremophiles , vol.5 , Issue.5 , pp. 351-354
    • Hou, S.1    Belisle, C.2    Lam, S.3    Piatibratov, M.4    Sivozhelezov, V.5    Takami, H.6
  • 77
    • 0034598826 scopus 로고    scopus 로고
    • Myoglobin-like aerotaxis transducers in Archaea and Bacteria
    • [Research Support, U.S. Gov't, Non-P.H.S.]
    • Hou S., Larsen R.W., Boudko D., Riley C.W., Karatan E., Zimmer M., et al. Myoglobin-like aerotaxis transducers in Archaea and Bacteria. Nature 2000, 403(6769):540-544. [Research Support, U.S. Gov't, Non-P.H.S.]. 10.1038/35000570.
    • (2000) Nature , vol.403 , Issue.6769 , pp. 540-544
    • Hou, S.1    Larsen, R.W.2    Boudko, D.3    Riley, C.W.4    Karatan, E.5    Zimmer, M.6
  • 78
    • 13644262078 scopus 로고    scopus 로고
    • Spectroscopic and redox properties of a CooA homologue from Carboxydothermus hydrogenoformans
    • [Research Support, Non-U.S. Gov't]
    • Inagaki S., Masuda C., Akaishi T., Nakajima H., Yoshioka S., Ohta T., et al. Spectroscopic and redox properties of a CooA homologue from Carboxydothermus hydrogenoformans. Journal of Biological Chemistry 2005, 280(5):3269-3274. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M409884200.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.5 , pp. 3269-3274
    • Inagaki, S.1    Masuda, C.2    Akaishi, T.3    Nakajima, H.4    Yoshioka, S.5    Ohta, T.6
  • 79
    • 77951029841 scopus 로고    scopus 로고
    • Cell pole-specific activation of a critical bacterial cell cycle kinase
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Iniesta A.A., Hillson N.J., Shapiro L. Cell pole-specific activation of a critical bacterial cell cycle kinase. Proceedings of the National Academy of Sciences of the United States of America 2010, 107(15):7012-7017. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1073/pnas.1001767107.
    • (2010) Proceedings of the National Academy of Sciences of the United States of America , vol.107 , Issue.15 , pp. 7012-7017
    • Iniesta, A.A.1    Hillson, N.J.2    Shapiro, L.3
  • 80
    • 39549117367 scopus 로고    scopus 로고
    • Effects of mutations in the heme domain on the transcriptional activity and DNA-binding activity of NPAS2
    • [Research Support, Non-U.S. Gov't]
    • Ishida M., Ueha T., Sagami I. Effects of mutations in the heme domain on the transcriptional activity and DNA-binding activity of NPAS2. Biochemical and Biophysical Research Communications 2008, 368(2):292-297. [Research Support, Non-U.S. Gov't]. 10.1016/j.bbrc.2008.01.053.
    • (2008) Biochemical and Biophysical Research Communications , vol.368 , Issue.2 , pp. 292-297
    • Ishida, M.1    Ueha, T.2    Sagami, I.3
  • 81
    • 67449161546 scopus 로고    scopus 로고
    • Role of Phe113 at the distal side of the heme domain of an oxygen-sensor (Ec DOS) in the characterization of the heme environment
    • [Research Support, Non-U.S. Gov't]
    • Ito S., Araki Y., Tanaka A., Igarashi J., Wada T., Shimizu T. Role of Phe113 at the distal side of the heme domain of an oxygen-sensor (Ec DOS) in the characterization of the heme environment. Journal of Inorganic Biochemistry 2009, 103(7):989-996. [Research Support, Non-U.S. Gov't]. 10.1016/j.jinorgbio.2009.04.009.
    • (2009) Journal of Inorganic Biochemistry , vol.103 , Issue.7 , pp. 989-996
    • Ito, S.1    Araki, Y.2    Tanaka, A.3    Igarashi, J.4    Wada, T.5    Shimizu, T.6
  • 82
    • 70349429628 scopus 로고    scopus 로고
    • The FG loop of a heme-based gas sensor enzyme, Ec DOS, functions in heme binding, autoxidation and catalysis
    • [Research Support, Non-U.S. Gov't]
    • Ito S., Igarashi J., Shimizu T. The FG loop of a heme-based gas sensor enzyme, Ec DOS, functions in heme binding, autoxidation and catalysis. Journal of Inorganic Biochemistry 2009, 103(10):1380-1385. [Research Support, Non-U.S. Gov't]. 10.1016/j.jinorgbio.2009.07.012.
    • (2009) Journal of Inorganic Biochemistry , vol.103 , Issue.10 , pp. 1380-1385
    • Ito, S.1    Igarashi, J.2    Shimizu, T.3
  • 83
    • 9144261238 scopus 로고    scopus 로고
    • Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins
    • Iyer L.M., Anantharaman V., Aravind L. Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins. BMC Genomics 2003, 4(1):5.
    • (2003) BMC Genomics , vol.4 , Issue.1 , pp. 5
    • Iyer, L.M.1    Anantharaman, V.2    Aravind, L.3
  • 84
    • 0038727151 scopus 로고    scopus 로고
    • Circadian clock-related polymorphisms in seasonal affective disorder and their relevance to diurnal preference
    • [Comparative Study Research Support, Non-U.S. Gov't]
    • Johansson C., Willeit M., Smedh C., Ekholm J., Paunio T., Kieseppa T., et al. Circadian clock-related polymorphisms in seasonal affective disorder and their relevance to diurnal preference. Neuropsychopharmacology 2003, 28(4):734-739. [Comparative Study Research Support, Non-U.S. Gov't]. 10.1038/sj.npp.1300121.
    • (2003) Neuropsychopharmacology , vol.28 , Issue.4 , pp. 734-739
    • Johansson, C.1    Willeit, M.2    Smedh, C.3    Ekholm, J.4    Paunio, T.5    Kieseppa, T.6
  • 85
    • 3343024625 scopus 로고    scopus 로고
    • Reciprocal regulation of haem biosynthesis and the circadian clock in mammals
    • [Research Support, U.S. Gov't, P.H.S.]
    • Kaasik K., Lee C.C. Reciprocal regulation of haem biosynthesis and the circadian clock in mammals. Nature 2004, 430(6998):467-471. [Research Support, U.S. Gov't, P.H.S.]. 10.1038/nature02724.
    • (2004) Nature , vol.430 , Issue.6998 , pp. 467-471
    • Kaasik, K.1    Lee, C.C.2
  • 86
    • 0026019387 scopus 로고
    • Involvement of fixLJ in the regulation of nitrogen fixation in Azorhizobium caulinodans
    • Kaminski P.A., Elmerich C. Involvement of fixLJ in the regulation of nitrogen fixation in Azorhizobium caulinodans. Molecular Microbiology 1991, 5(3):665-673.
    • (1991) Molecular Microbiology , vol.5 , Issue.3 , pp. 665-673
    • Kaminski, P.A.1    Elmerich, C.2
  • 87
    • 13844262033 scopus 로고    scopus 로고
    • C-di-GMP (3'-5'-cyclic diguanylic acid) inhibits Staphylococcus aureus cell-cell interactions and biofilm formation
    • Karaolis D.K., Rashid M.H., Chythanya R., Luo W., Hyodo M., Hayakawa Y. c-di-GMP (3'-5'-cyclic diguanylic acid) inhibits Staphylococcus aureus cell-cell interactions and biofilm formation. Antimicrobial Agents and Chemotherapy 2005, 49(3):1029-1038. 10.1128/AAC.49.3.1029-1038.2005.
    • (2005) Antimicrobial Agents and Chemotherapy , vol.49 , Issue.3 , pp. 1029-1038
    • Karaolis, D.K.1    Rashid, M.H.2    Chythanya, R.3    Luo, W.4    Hyodo, M.5    Hayakawa, Y.6
  • 88
    • 42549120776 scopus 로고    scopus 로고
    • RcoM: A new single-component transcriptional regulator of CO metabolism in bacteria
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]
    • Kerby R.L., Youn H., Roberts G.P. RcoM: A new single-component transcriptional regulator of CO metabolism in bacteria. Journal of Bacteriology 2008, 190(9):3336-3343. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]. 10.1128/JB.00033-08.
    • (2008) Journal of Bacteriology , vol.190 , Issue.9 , pp. 3336-3343
    • Kerby, R.L.1    Youn, H.2    Roberts, G.P.3
  • 89
    • 0037462976 scopus 로고    scopus 로고
    • Repositioning about the dimer interface of the transcription regulator CooA: A major signal transduction pathway between the effector and DNA-binding domains
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Kerby R.L., Youn H., Thorsteinsson M.V., Roberts G.P. Repositioning about the dimer interface of the transcription regulator CooA: A major signal transduction pathway between the effector and DNA-binding domains. Journal of Molecular Biology 2003, 325(4):809-823. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (2003) Journal of Molecular Biology , vol.325 , Issue.4 , pp. 809-823
    • Kerby, R.L.1    Youn, H.2    Thorsteinsson, M.V.3    Roberts, G.P.4
  • 90
    • 15444362702 scopus 로고    scopus 로고
    • Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling
    • [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, P.H.S.]
    • Key J., Moffat K. Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling. Biochemistry 2005, 44(12):4627-4635. [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, P.H.S.]. 10.1021/bi047942r.
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4627-4635
    • Key, J.1    Moffat, K.2
  • 91
    • 34247550744 scopus 로고    scopus 로고
    • Time-resolved crystallographic studies of the heme domain of the oxygen sensor FixL: Structural dynamics of ligand rebinding and their relation to signal transduction
    • [Research Support, N.I.H., Extramural]
    • Key J., Srajer V., Pahl R., Moffat K. Time-resolved crystallographic studies of the heme domain of the oxygen sensor FixL: Structural dynamics of ligand rebinding and their relation to signal transduction. Biochemistry 2007, 46(16):4706-4715. [Research Support, N.I.H., Extramural]. 10.1021/bi700043c.
    • (2007) Biochemistry , vol.46 , Issue.16 , pp. 4706-4715
    • Key, J.1    Srajer, V.2    Pahl, R.3    Moffat, K.4
  • 92
    • 44949200347 scopus 로고    scopus 로고
    • Heme-binding characteristics of the isolated PAS-A domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms
    • Kitanishi K., Igarashi J., Hayasaka K., Hikage N., Saiful I., Yamauchi S., et al. Heme-binding characteristics of the isolated PAS-A domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms. Biochemistry 2008, 47(23):6157-6168. 10.1021/bi7023892.
    • (2008) Biochemistry , vol.47 , Issue.23 , pp. 6157-6168
    • Kitanishi, K.1    Igarashi, J.2    Hayasaka, K.3    Hikage, N.4    Saiful, I.5    Yamauchi, S.6
  • 93
    • 78650152432 scopus 로고    scopus 로고
    • Important roles of Tyr43 at the putative heme distal side in the oxygen recognition and stability of the Fe(II)-O2 complex of YddV, a globin-coupled heme-based oxygen sensor diguanylate cyclase
    • [Comparative Study Research Support, Non-U.S. Gov't]
    • Kitanishi K., Kobayashi K., Kawamura Y., Ishigami I., Ogura T., Nakajima K., et al. Important roles of Tyr43 at the putative heme distal side in the oxygen recognition and stability of the Fe(II)-O2 complex of YddV, a globin-coupled heme-based oxygen sensor diguanylate cyclase. Biochemistry 2010, 49(49):10381-10393. [Comparative Study Research Support, Non-U.S. Gov't]. 10.1021/bi100733q.
    • (2010) Biochemistry , vol.49 , Issue.49 , pp. 10381-10393
    • Kitanishi, K.1    Kobayashi, K.2    Kawamura, Y.3    Ishigami, I.4    Ogura, T.5    Nakajima, K.6
  • 94
    • 80053896156 scopus 로고    scopus 로고
    • Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5
    • [Research Support, Non-U.S. Gov't]
    • Kitanishi K., Kobayashi K., Uchida T., Ishimori K., Igarashi J., Shimizu T. Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5. Journal of Biological Chemistry 2011, 286(41):35522-35534. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M111.274811.
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.41 , pp. 35522-35534
    • Kitanishi, K.1    Kobayashi, K.2    Uchida, T.3    Ishimori, K.4    Igarashi, J.5    Shimizu, T.6
  • 95
    • 78649912237 scopus 로고    scopus 로고
    • Catalysis and oxygen binding of Ec DOS: A haem-based oxygen-sensor enzyme from Escherichia coli
    • [Research Support, Non-U.S. Gov't]
    • Kobayashi K., Tanaka A., Takahashi H., Igarashi J., Ishitsuka Y., Yokota N., et al. Catalysis and oxygen binding of Ec DOS: A haem-based oxygen-sensor enzyme from Escherichia coli. Journal of Biochemistry 2010, 148(6):693-703. [Research Support, Non-U.S. Gov't]. 10.1093/jb/mvq103.
    • (2010) Journal of Biochemistry , vol.148 , Issue.6 , pp. 693-703
    • Kobayashi, K.1    Tanaka, A.2    Takahashi, H.3    Igarashi, J.4    Ishitsuka, Y.5    Yokota, N.6
  • 96
    • 33847298449 scopus 로고    scopus 로고
    • Crystal structure of CO-sensing transcription activator CooA bound to exogenous ligand imidazole
    • [Research Support, Non-U.S. Gov't]
    • Komori H., Inagaki S., Yoshioka S., Aono S., Higuchi Y. Crystal structure of CO-sensing transcription activator CooA bound to exogenous ligand imidazole. Journal of Molecular Biology 2007, 367(3):864-871. [Research Support, Non-U.S. Gov't]. 10.1016/j.jmb.2007.01.043.
    • (2007) Journal of Molecular Biology , vol.367 , Issue.3 , pp. 864-871
    • Komori, H.1    Inagaki, S.2    Yoshioka, S.3    Aono, S.4    Higuchi, Y.5
  • 97
    • 23844468462 scopus 로고    scopus 로고
    • Spectroscopic characterization of the isolated heme-bound PAS-B domain of neuronal PAS domain protein 2 associated with circadian rhythms
    • [Research Support, Non-U.S. Gov't]
    • Koudo R., Kurokawa H., Sato E., Igarashi J., Uchida T., Sagami I., et al. Spectroscopic characterization of the isolated heme-bound PAS-B domain of neuronal PAS domain protein 2 associated with circadian rhythms. FEBS Journal 2005, 272(16):4153-4162. [Research Support, Non-U.S. Gov't]. 10.1111/j.1742-4658.2005.04828.x.
    • (2005) FEBS Journal , vol.272 , Issue.16 , pp. 4153-4162
    • Koudo, R.1    Kurokawa, H.2    Sato, E.3    Igarashi, J.4    Uchida, T.5    Sagami, I.6
  • 98
    • 77956304750 scopus 로고    scopus 로고
    • ARNTL (BMAL1) and NPAS2 gene variants contribute to fertility and seasonality
    • [Research Support, Non-U.S. Gov't]
    • Kovanen L., Saarikoski S.T., Aromaa A., Lonnqvist J., Partonen T. ARNTL (BMAL1) and NPAS2 gene variants contribute to fertility and seasonality. PLoS One 2010, 5(4):e10007. [Research Support, Non-U.S. Gov't]. 10.1371/journal.pone.0010007.
    • (2010) PLoS One , vol.5 , Issue.4
    • Kovanen, L.1    Saarikoski, S.T.2    Aromaa, A.3    Lonnqvist, J.4    Partonen, T.5
  • 99
    • 34250681839 scopus 로고    scopus 로고
    • Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopy
    • [Research Support, Non-U.S. Gov't]
    • Kruglik S.G., Jasaitis A., Hola K., Yamashita T., Liebl U., Martin J.L., et al. Subpicosecond oxygen trapping in the heme pocket of the oxygen sensor FixL observed by time-resolved resonance Raman spectroscopy. Proceedings of the National Academy of Sciences of the United States of America 2007, 104(18):7408-7413. [Research Support, Non-U.S. Gov't]. 10.1073/pnas.0700445104.
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.18 , pp. 7408-7413
    • Kruglik, S.G.1    Jasaitis, A.2    Hola, K.3    Yamashita, T.4    Liebl, U.5    Martin, J.L.6
  • 100
    • 33644516891 scopus 로고    scopus 로고
    • Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3'-5')-cyclic-GMP in virulence
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]
    • Kulasakara H., Lee V., Brencic A., Liberati N., Urbach J., Miyata S., et al. Analysis of Pseudomonas aeruginosa diguanylate cyclases and phosphodiesterases reveals a role for bis-(3'-5')-cyclic-GMP in virulence. Proceedings of the National Academy of Sciences of the United States of America 2006, 103(8):2839-2844. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]. 10.1073/pnas.0511090103.
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.8 , pp. 2839-2844
    • Kulasakara, H.1    Lee, V.2    Brencic, A.3    Liberati, N.4    Urbach, J.5    Miyata, S.6
  • 101
    • 0033784540 scopus 로고    scopus 로고
    • Structure of the CO sensing transcription activator CooA
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Lanzilotta W.N., Schuller D.J., Thorsteinsson M.V., Kerby R.L., Roberts G.P., Poulos T.L. Structure of the CO sensing transcription activator CooA. Natural Structural Biology 2000, 7(10):876-880. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]. 10.1038/82820.
    • (2000) Natural Structural Biology , vol.7 , Issue.10 , pp. 876-880
    • Lanzilotta, W.N.1    Schuller, D.J.2    Thorsteinsson, M.V.3    Kerby, R.L.4    Roberts, G.P.5    Poulos, T.L.6
  • 103
    • 73649124591 scopus 로고    scopus 로고
    • Heme ligand binding properties and intradimer interactions in the full-length sensor protein dos from Escherichia coli and its isolated heme domain
    • [Research Support, Non-U.S. Gov't]
    • Lechauve C., Bouzhir-Sima L., Yamashita T., Marden M.C., Vos M.H., Liebl U., et al. Heme ligand binding properties and intradimer interactions in the full-length sensor protein dos from Escherichia coli and its isolated heme domain. Journal of Biological Chemistry 2009, 284(52):36146-36159. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M109.066811.
    • (2009) Journal of Biological Chemistry , vol.284 , Issue.52 , pp. 36146-36159
    • Lechauve, C.1    Bouzhir-Sima, L.2    Yamashita, T.3    Marden, M.C.4    Vos, M.H.5    Liebl, U.6
  • 104
    • 3843070019 scopus 로고    scopus 로고
    • Geobacter sulfurreducens can grow with oxygen as a terminal electron acceptor
    • [Research Support, Non-U.S. Gov't]
    • Lin W.C., Coppi M.V., Lovley D.R. Geobacter sulfurreducens can grow with oxygen as a terminal electron acceptor. Applied and Environmental Microbiology 2004, 70(4):2525-2528. [Research Support, Non-U.S. Gov't].
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.4 , pp. 2525-2528
    • Lin, W.C.1    Coppi, M.V.2    Lovley, D.R.3
  • 105
    • 0027403425 scopus 로고
    • The oxygen sensor FixL of Rhizobium meliloti is a membrane protein containing four possible transmembrane segments
    • [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Lois A.F., Ditta G.S., Helinski D.R. The oxygen sensor FixL of Rhizobium meliloti is a membrane protein containing four possible transmembrane segments. Journal of Bacteriology 1993, 175(4):1103-1109. [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (1993) Journal of Bacteriology , vol.175 , Issue.4 , pp. 1103-1109
    • Lois, A.F.1    Ditta, G.S.2    Helinski, D.R.3
  • 106
    • 0027523571 scopus 로고
    • Geobacter metallireducens gen. nov. sp. nov., a microorganism capable of coupling the complete oxidation of organic compounds to the reduction of iron and other metals
    • [Research Support, U.S. Gov't, Non-P.H.S.]
    • Lovley D.R., Giovannoni S.J., White D.C., Champine J.E., Phillips E.J., Gorby Y.A., et al. Geobacter metallireducens gen. nov. sp. nov., a microorganism capable of coupling the complete oxidation of organic compounds to the reduction of iron and other metals. Archives of Microbiology 1993, 159(4):336-344. [Research Support, U.S. Gov't, Non-P.H.S.].
    • (1993) Archives of Microbiology , vol.159 , Issue.4 , pp. 336-344
    • Lovley, D.R.1    Giovannoni, S.J.2    White, D.C.3    Champine, J.E.4    Phillips, E.J.5    Gorby, Y.A.6
  • 107
    • 53349176566 scopus 로고    scopus 로고
    • Molecular architecture of the "stressosome," a signal integration and transduction hub
    • [Research Support, Non-U.S. Gov't]
    • Marles-Wright J., Grant T., Delumeau O., van Duinen G., Firbank S.J., Lewis P.J., et al. Molecular architecture of the "stressosome," a signal integration and transduction hub. Science 2008, 322(5898):92-96. [Research Support, Non-U.S. Gov't]. 10.1126/science.1159572.
    • (2008) Science , vol.322 , Issue.5898 , pp. 92-96
    • Marles-Wright, J.1    Grant, T.2    Delumeau, O.3    van Duinen, G.4    Firbank, S.J.5    Lewis, P.J.6
  • 108
    • 50249155967 scopus 로고    scopus 로고
    • The transcription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch
    • [Research Support, N.I.H., Extramural]
    • Marvin K.A., Kerby R.L., Youn H., Roberts G.P., Burstyn J.N. The transcription regulator RcoM-2 from Burkholderia xenovorans is a cysteine-ligated hemoprotein that undergoes a redox-mediated ligand switch. Biochemistry 2008, 47(34):9016-9028. [Research Support, N.I.H., Extramural]. 10.1021/bi800486x.
    • (2008) Biochemistry , vol.47 , Issue.34 , pp. 9016-9028
    • Marvin, K.A.1    Kerby, R.L.2    Youn, H.3    Roberts, G.P.4    Burstyn, J.N.5
  • 109
    • 79959813633 scopus 로고    scopus 로고
    • Cyclic diguanylate turnover mediated by the sole GGDEF/EAL response regulator in Pseudomonas putida: Its role in the rhizosphere and an analysis of its target processes
    • [Research Support, Non-U.S. Gov't]
    • Matilla M.A., Travieso M.L., Ramos J.L., Ramos-Gonzalez M.I. Cyclic diguanylate turnover mediated by the sole GGDEF/EAL response regulator in Pseudomonas putida: Its role in the rhizosphere and an analysis of its target processes. Environmental Microbiology 2011, 13(7):1745-1766. [Research Support, Non-U.S. Gov't]. 10.1111/j.1462-2920.2011.02499.x.
    • (2011) Environmental Microbiology , vol.13 , Issue.7 , pp. 1745-1766
    • Matilla, M.A.1    Travieso, M.L.2    Ramos, J.L.3    Ramos-Gonzalez, M.I.4
  • 110
    • 0141868933 scopus 로고    scopus 로고
    • A bacterial cell-cycle regulatory network operating in time and space
    • [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review]
    • McAdams H.H., Shapiro L. A bacterial cell-cycle regulatory network operating in time and space. Science 2003, 301(5641):1874-1877. [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review]. 10.1126/science.1087694.
    • (2003) Science , vol.301 , Issue.5641 , pp. 1874-1877
    • McAdams, H.H.1    Shapiro, L.2
  • 111
    • 0037701427 scopus 로고    scopus 로고
    • Bradyrhizobium japonicum NnrR, a denitrification regulator, expands the FixLJ-FixK2 regulatory cascade
    • [Research Support, Non-U.S. Gov't]
    • Mesa S., Bedmar E.J., Chanfon A., Hennecke H., Fischer H.M. Bradyrhizobium japonicum NnrR, a denitrification regulator, expands the FixLJ-FixK2 regulatory cascade. Journal of Bacteriology 2003, 185(13):3978-3982. [Research Support, Non-U.S. Gov't].
    • (2003) Journal of Bacteriology , vol.185 , Issue.13 , pp. 3978-3982
    • Mesa, S.1    Bedmar, E.J.2    Chanfon, A.3    Hennecke, H.4    Fischer, H.M.5
  • 112
    • 0346243803 scopus 로고    scopus 로고
    • Genome of Geobacter sulfurreducens: Metal reduction in subsurface environments
    • [Research Support, U.S. Gov't, Non-P.H.S.]
    • Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W., Heidelberg J.F., et al. Genome of Geobacter sulfurreducens: Metal reduction in subsurface environments. Science 2003, 302(5652):1967-1969. [Research Support, U.S. Gov't, Non-P.H.S.]. 10.1126/science.1088727.
    • (2003) Science , vol.302 , Issue.5652 , pp. 1967-1969
    • Methe, B.A.1    Nelson, K.E.2    Eisen, J.A.3    Paulsen, I.T.4    Nelson, W.5    Heidelberg, J.F.6
  • 113
    • 0033551768 scopus 로고    scopus 로고
    • Iron coordination structures of oxygen sensor FixL characterized by Fe K-edge extended x-ray absorption fine structure and resonance raman spectroscopy
    • Miyatake H., Mukai M., Adachi S., Nakamura H., Tamura K., Iizuka T., et al. Iron coordination structures of oxygen sensor FixL characterized by Fe K-edge extended x-ray absorption fine structure and resonance raman spectroscopy. Journal of Biological Chemistry 1999, 274(33):23176-23184.
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.33 , pp. 23176-23184
    • Miyatake, H.1    Mukai, M.2    Adachi, S.3    Nakamura, H.4    Tamura, K.5    Iizuka, T.6
  • 114
    • 0034636982 scopus 로고    scopus 로고
    • Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: Crystallographic, mutagenesis and resonance Raman spectroscopic studies
    • [Research Support, Non-U.S. Gov't]
    • Miyatake H., Mukai M., Park S.Y., Adachi S., Tamura K., Nakamura H., et al. Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: Crystallographic, mutagenesis and resonance Raman spectroscopic studies. Journal of Molecular Biology 2000, 301(2):415-431. [Research Support, Non-U.S. Gov't]. 10.1006/jmbi.2000.3954.
    • (2000) Journal of Molecular Biology , vol.301 , Issue.2 , pp. 415-431
    • Miyatake, H.1    Mukai, M.2    Park, S.Y.3    Adachi, S.4    Tamura, K.5    Nakamura, H.6
  • 115
    • 0030027631 scopus 로고    scopus 로고
    • Globins in nonvertebrate species: Dispersal by horizontal gene transfer and evolution of the structure-function relationships
    • [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Moens L., Vanfleteren J., Van de Peer Y., Peeters K., Kapp O., Czeluzniak J., et al. Globins in nonvertebrate species: Dispersal by horizontal gene transfer and evolution of the structure-function relationships. Molecular and Biological Evolution 1996, 13(2):324-333. [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (1996) Molecular and Biological Evolution , vol.13 , Issue.2 , pp. 324-333
    • Moens, L.1    Vanfleteren, J.2    Van de Peer, Y.3    Peeters, K.4    Kapp, O.5    Czeluzniak, J.6
  • 116
    • 0026511245 scopus 로고
    • The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain
    • [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Monson E.K., Weinstein M., Ditta G.S., Helinski D.R. The FixL protein of Rhizobium meliloti can be separated into a heme-binding oxygen-sensing domain and a functional C-terminal kinase domain. Proceedings of the National Academy of Sciences of the United States of America 1992, 89(10):4280-4284. [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (1992) Proceedings of the National Academy of Sciences of the United States of America , vol.89 , Issue.10 , pp. 4280-4284
    • Monson, E.K.1    Weinstein, M.2    Ditta, G.S.3    Helinski, D.R.4
  • 118
    • 0034649398 scopus 로고    scopus 로고
    • Roles of Ile209 and Ile210 on the heme pocket structure and regulation of histidine kinase activity of oxygen sensor FixL from Rhizobium meliloti
    • [Research Support, Non-U.S. Gov't]
    • Mukai M., Nakamura K., Nakamura H., Iizuka T., Shiro Y. Roles of Ile209 and Ile210 on the heme pocket structure and regulation of histidine kinase activity of oxygen sensor FixL from Rhizobium meliloti. Biochemistry 2000, 39(45):13810-13816. [Research Support, Non-U.S. Gov't].
    • (2000) Biochemistry , vol.39 , Issue.45 , pp. 13810-13816
    • Mukai, M.1    Nakamura, K.2    Nakamura, H.3    Iizuka, T.4    Shiro, Y.5
  • 119
    • 33646682128 scopus 로고    scopus 로고
    • Spectroscopic and DNA-binding characterization of the isolated heme-bound basic helix-loop-helix-PAS-A domain of neuronal PAS protein 2 (NPAS2), a transcription activator protein associated with circadian rhythms
    • [Research Support, Non-U.S. Gov't]
    • Mukaiyama Y., Uchida T., Sato E., Sasaki A., Sato Y., Igarashi J., et al. Spectroscopic and DNA-binding characterization of the isolated heme-bound basic helix-loop-helix-PAS-A domain of neuronal PAS protein 2 (NPAS2), a transcription activator protein associated with circadian rhythms. FEBS Journal 2006, 273(11):2528-2539. [Research Support, Non-U.S. Gov't]. 10.1111/j.1742-4658.2006.05259.x.
    • (2006) FEBS Journal , vol.273 , Issue.11 , pp. 2528-2539
    • Mukaiyama, Y.1    Uchida, T.2    Sato, E.3    Sasaki, A.4    Sato, Y.5    Igarashi, J.6
  • 120
    • 27944452772 scopus 로고    scopus 로고
    • Structure of a nonheme globin in environmental stress signaling
    • [Comparative Study Research Support, Non-U.S. Gov't]
    • Murray J.W., Delumeau O., Lewis R.J. Structure of a nonheme globin in environmental stress signaling. Proceedings of the National Academy of Sciences of the United States of America 2005, 102(48):17320-17325. [Comparative Study Research Support, Non-U.S. Gov't]. 10.1073/pnas.0506599102.
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.48 , pp. 17320-17325
    • Murray, J.W.1    Delumeau, O.2    Lewis, R.J.3
  • 121
    • 84858447333 scopus 로고    scopus 로고
    • Leu65 in the heme distal side is critical for the stability of the Fe(II)-O2 complex of YddV, a globin-coupled oxygen sensor diguanylate cyclase
    • [Research Support, Non-U.S. Gov't]
    • Nakajima K., Kitanishi K., Kobayashi K., Kobayashi N., Igarashi J., Shimizu T. Leu65 in the heme distal side is critical for the stability of the Fe(II)-O2 complex of YddV, a globin-coupled oxygen sensor diguanylate cyclase. Journal of Inorganic Biochemistry 2012, 108:163-170. [Research Support, Non-U.S. Gov't]. 10.1016/j.jinorgbio.2011.09.019.
    • (2012) Journal of Inorganic Biochemistry , vol.108 , pp. 163-170
    • Nakajima, K.1    Kitanishi, K.2    Kobayashi, K.3    Kobayashi, N.4    Igarashi, J.5    Shimizu, T.6
  • 122
    • 0031595076 scopus 로고    scopus 로고
    • Bradyrhizobium japonicum FixK2, a crucial distributor in the FixLJ-dependent regulatory cascade for control of genes inducible by low oxygen levels
    • [Research Support, Non-U.S. Gov't]
    • Nellen-Anthamatten D., Rossi P., Preisig O., Kullik I., Babst M., Fischer H.M., et al. Bradyrhizobium japonicum FixK2, a crucial distributor in the FixLJ-dependent regulatory cascade for control of genes inducible by low oxygen levels. Journal of Bacteriology 1998, 180(19):5251-5255. [Research Support, Non-U.S. Gov't].
    • (1998) Journal of Bacteriology , vol.180 , Issue.19 , pp. 5251-5255
    • Nellen-Anthamatten, D.1    Rossi, P.2    Preisig, O.3    Kullik, I.4    Babst, M.5    Fischer, H.M.6
  • 123
    • 34249317295 scopus 로고    scopus 로고
    • Association of Per1 and Npas2 with autistic disorder: Support for the clock genes/social timing hypothesis
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]
    • Nicholas B., Rudrasingham V., Nash S., Kirov G., Owen M.J., Wimpory D.C. Association of Per1 and Npas2 with autistic disorder: Support for the clock genes/social timing hypothesis. Molecular Psychiatry 2007, 12(6):581-592. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]. 10.1038/sj.mp.4001953.
    • (2007) Molecular Psychiatry , vol.12 , Issue.6 , pp. 581-592
    • Nicholas, B.1    Rudrasingham, V.2    Nash, S.3    Kirov, G.4    Owen, M.J.5    Wimpory, D.C.6
  • 124
    • 0029020772 scopus 로고
    • Oxygen control of the Bradyrhizobium japonicum hemA gene
    • [Research Support, U.S. Gov't, Non-P.H.S.]
    • Page K.M., Guerinot M.L. Oxygen control of the Bradyrhizobium japonicum hemA gene. Journal of Bacteriology 1995, 177(14):3979-3984. [Research Support, U.S. Gov't, Non-P.H.S.].
    • (1995) Journal of Bacteriology , vol.177 , Issue.14 , pp. 3979-3984
    • Page, K.M.1    Guerinot, M.L.2
  • 125
    • 8544223537 scopus 로고    scopus 로고
    • Hierarchical thinking in network biology: The unbiased modularization of biochemical networks
    • [Research Support, Non-U.S. Gov't Review]
    • Papin J.A., Reed J.L., Palsson B.O. Hierarchical thinking in network biology: The unbiased modularization of biochemical networks. Trends in Biochemical Sciences 2004, 29(12):641-647. [Research Support, Non-U.S. Gov't Review]. 10.1016/j.tibs.2004.10.001.
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.12 , pp. 641-647
    • Papin, J.A.1    Reed, J.L.2    Palsson, B.O.3
  • 126
    • 1542327658 scopus 로고    scopus 로고
    • Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH)
    • [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Park H., Suquet C., Satterlee J.D., Kang C. Insights into signal transduction involving PAS domain oxygen-sensing heme proteins from the X-ray crystal structure of Escherichia coli Dos heme domain (Ec DosH). Biochemistry 2004, 43(10):2738-2746. [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]. 10.1021/bi035980p.
    • (2004) Biochemistry , vol.43 , Issue.10 , pp. 2738-2746
    • Park, H.1    Suquet, C.2    Satterlee, J.D.3    Kang, C.4
  • 127
    • 34247634564 scopus 로고    scopus 로고
    • Three circadian clock genes Per2, Arntl, and Npas2 contribute to winter depression
    • [Research Support, Non-U.S. Gov't]
    • Partonen T., Treutlein J., Alpman A., Frank J., Johansson C., Depner M., et al. Three circadian clock genes Per2, Arntl, and Npas2 contribute to winter depression. Annals of Medicine 2007, 39(3):229-238. [Research Support, Non-U.S. Gov't]. 10.1080/07853890701278795.
    • (2007) Annals of Medicine , vol.39 , Issue.3 , pp. 229-238
    • Partonen, T.1    Treutlein, J.2    Alpman, A.3    Frank, J.4    Johansson, C.5    Depner, M.6
  • 128
    • 58549113376 scopus 로고    scopus 로고
    • HisE11 and HisF8 provide bis-histidyl heme hexa-coordination in the globin domain of Geobacter sulfurreducens globin-coupled sensor
    • [Research Support, Non-U.S. Gov't]
    • Pesce A., Thijs L., Nardini M., Desmet F., Sisinni L., Gourlay L., et al. HisE11 and HisF8 provide bis-histidyl heme hexa-coordination in the globin domain of Geobacter sulfurreducens globin-coupled sensor. Journal of Molecular Biology 2009, 386(1):246-260. [Research Support, Non-U.S. Gov't]. 10.1016/j.jmb.2008.12.023.
    • (2009) Journal of Molecular Biology , vol.386 , Issue.1 , pp. 246-260
    • Pesce, A.1    Thijs, L.2    Nardini, M.3    Desmet, F.4    Sisinni, L.5    Gourlay, L.6
  • 129
    • 33749504737 scopus 로고    scopus 로고
    • Two ligand-binding sites in the O2-sensing signal transducer HemAT: Implications for ligand recognition/discrimination and signaling
    • [Research Support, Non-U.S. Gov't]
    • Pinakoulaki E., Yoshimura H., Daskalakis V., Yoshioka S., Aono S., Varotsis C. Two ligand-binding sites in the O2-sensing signal transducer HemAT: Implications for ligand recognition/discrimination and signaling. Proceedings of the National Academy of Sciences of the United States of America 2006, 103(40):14796-14801. [Research Support, Non-U.S. Gov't]. 10.1073/pnas.0604248103.
    • (2006) Proceedings of the National Academy of Sciences of the United States of America , vol.103 , Issue.40 , pp. 14796-14801
    • Pinakoulaki, E.1    Yoshimura, H.2    Daskalakis, V.3    Yoshioka, S.4    Aono, S.5    Varotsis, C.6
  • 130
    • 14644387541 scopus 로고    scopus 로고
    • Nitric oxide and nitrosative stress tolerance in bacteria
    • [Research Support, Non-U.S. Gov't Review]
    • Poole R.K. Nitric oxide and nitrosative stress tolerance in bacteria. Biochemical Society Transactions 2005, 33(Pt 1):176-180. [Research Support, Non-U.S. Gov't Review]. 10.1042/BST0330176.
    • (2005) Biochemical Society Transactions , vol.33 , Issue.PART 1 , pp. 176-180
    • Poole, R.K.1
  • 131
    • 0034072208 scopus 로고    scopus 로고
    • New functions for the ancient globin family: Bacterial responses to nitric oxide and nitrosative stress
    • [Research Support, Non-U.S. Gov't Review]
    • Poole R.K., Hughes M.N. New functions for the ancient globin family: Bacterial responses to nitric oxide and nitrosative stress. Molecular Microbiology 2000, 36(4):775-783. [Research Support, Non-U.S. Gov't Review].
    • (2000) Molecular Microbiology , vol.36 , Issue.4 , pp. 775-783
    • Poole, R.K.1    Hughes, M.N.2
  • 132
    • 2442647919 scopus 로고    scopus 로고
    • Dynamics of carbon monoxide binding to CooA
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Puranik M., Nielsen S.B., Youn H., Hvitved A.N., Bourassa J.L., Case M.A., et al. Dynamics of carbon monoxide binding to CooA. Journal of Biological Chemistry 2004, 279(20):21096-21108. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]. 10.1074/jbc.M400613200.
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.20 , pp. 21096-21108
    • Puranik, M.1    Nielsen, S.B.2    Youn, H.3    Hvitved, A.N.4    Bourassa, J.L.5    Case, M.A.6
  • 133
    • 70350501347 scopus 로고    scopus 로고
    • A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 from Acetobacter xylinum
    • [Research Support, Non-U.S. Gov't]
    • Qi Y., Rao F., Luo Z., Liang Z.X. A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 from Acetobacter xylinum. Biochemistry 2009, 48(43):10275-10285. [Research Support, Non-U.S. Gov't]. 10.1021/bi901121w.
    • (2009) Biochemistry , vol.48 , Issue.43 , pp. 10275-10285
    • Qi, Y.1    Rao, F.2    Luo, Z.3    Liang, Z.X.4
  • 134
    • 84856747039 scopus 로고    scopus 로고
    • The bacterial stressosome: A modular system that has been adapted to control secondary messenger signaling
    • [Research Support, Non-U.S. Gov't]
    • Quin M.B., Berrisford J.M., Newman J.A., Basle A., Lewis R.J., Marles-Wright J. The bacterial stressosome: A modular system that has been adapted to control secondary messenger signaling. Structure 2012, 20(2):350-363. [Research Support, Non-U.S. Gov't]. 10.1016/j.str.2012.01.003.
    • (2012) Structure , vol.20 , Issue.2 , pp. 350-363
    • Quin, M.B.1    Berrisford, J.M.2    Newman, J.A.3    Basle, A.4    Lewis, R.J.5    Marles-Wright, J.6
  • 135
    • 84868624316 scopus 로고    scopus 로고
    • Deletion of the Desulfovibrio vulgaris carbon monoxide sensor invokes global changes in transcription
    • [Research Support, U.S. Gov't, Non-P.H.S.]
    • Rajeev L., Hillesland K.L., Zane G.M., Zhou A., Joachimiak M.P., He Z., et al. Deletion of the Desulfovibrio vulgaris carbon monoxide sensor invokes global changes in transcription. Journal of Bacteriology 2012, 194(21):5783-5793. [Research Support, U.S. Gov't, Non-P.H.S.]. 10.1128/JB.00749-12.
    • (2012) Journal of Bacteriology , vol.194 , Issue.21 , pp. 5783-5793
    • Rajeev, L.1    Hillesland, K.L.2    Zane, G.M.3    Zhou, A.4    Joachimiak, M.P.5    He, Z.6
  • 137
    • 0035919618 scopus 로고    scopus 로고
    • NPAS2: An analog of clock operative in the mammalian forebrain
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Reick M., Garcia J.A., Dudley C., McKnight S.L. NPAS2: An analog of clock operative in the mammalian forebrain. Science 2001, 293(5529):506-509. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]. 10.1126/science.1060699.
    • (2001) Science , vol.293 , Issue.5529 , pp. 506-509
    • Reick, M.1    Garcia, J.A.2    Dudley, C.3    McKnight, S.L.4
  • 138
    • 67349147094 scopus 로고    scopus 로고
    • Role of conserved F(alpha)-helix residues in the native fold and stability of the kinase-inhibited oxy state of the oxygen-sensing FixL protein from Sinorhizobium meliloti
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Reynolds M.F., Ackley L., Blizman A., Lutz Z., Manoff D., Miles M., et al. Role of conserved F(alpha)-helix residues in the native fold and stability of the kinase-inhibited oxy state of the oxygen-sensing FixL protein from Sinorhizobium meliloti. Archives of Biochemistry and Biophysics 2009, 485(2):150-159. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1016/j.abb.2009.02.011.
    • (2009) Archives of Biochemistry and Biophysics , vol.485 , Issue.2 , pp. 150-159
    • Reynolds, M.F.1    Ackley, L.2    Blizman, A.3    Lutz, Z.4    Manoff, D.5    Miles, M.6
  • 139
    • 0034681189 scopus 로고    scopus 로고
    • Electronic absorption, EPR, and resonance raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme
    • [Comparative Study Research Support, U.S. Gov't, P.H.S.]
    • Reynolds M.F., Parks R.B., Burstyn J.N., Shelver D., Thorsteinsson M.V., Kerby R.L., et al. Electronic absorption, EPR, and resonance raman spectroscopy of CooA, a CO-sensing transcription activator from R. rubrum, reveals a five-coordinate NO-heme. Biochemistry 2000, 39(2):388-396. [Comparative Study Research Support, U.S. Gov't, P.H.S.].
    • (2000) Biochemistry , vol.39 , Issue.2 , pp. 388-396
    • Reynolds, M.F.1    Parks, R.B.2    Burstyn, J.N.3    Shelver, D.4    Thorsteinsson, M.V.5    Kerby, R.L.6
  • 140
    • 0035223846 scopus 로고    scopus 로고
    • CooA: A heme-containing regulatory protein that serves as a specific sensor of both carbon monoxide and redox state
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review]
    • Roberts G.P., Thorsteinsson M.V., Kerby R.L., Lanzilotta W.N., Poulos T. CooA: A heme-containing regulatory protein that serves as a specific sensor of both carbon monoxide and redox state. Progress in Nucleic Acid Research and Molecular Biology 2001, 67:35-63. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Review].
    • (2001) Progress in Nucleic Acid Research and Molecular Biology , vol.67 , pp. 35-63
    • Roberts, G.P.1    Thorsteinsson, M.V.2    Kerby, R.L.3    Lanzilotta, W.N.4    Poulos, T.5
  • 141
    • 32544440049 scopus 로고    scopus 로고
    • The Bradyrhizobium japonicum napEDABC genes are controlled by the FixLJ-FixK(2)-NnrR regulatory cascade
    • [Research Support, Non-U.S. Gov't]
    • Robles E.F., Sanchez C., Bonnard N., Delgado M.J., Bedmar E.J. The Bradyrhizobium japonicum napEDABC genes are controlled by the FixLJ-FixK(2)-NnrR regulatory cascade. Biochemical Society Transactions 2006, 34(Pt 1):108-110. [Research Support, Non-U.S. Gov't]. 10.1042/BST0340108.
    • (2006) Biochemical Society Transactions , vol.34 , Issue.PART 1 , pp. 108-110
    • Robles, E.F.1    Sanchez, C.2    Bonnard, N.3    Delgado, M.J.4    Bedmar, E.J.5
  • 142
    • 0029782887 scopus 로고    scopus 로고
    • Structural basis for ligand discrimination and response initiation in the heme-based oxygen sensor FixL
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Rodgers K.R., Lukat-Rodgers G.S., Barron J.A. Structural basis for ligand discrimination and response initiation in the heme-based oxygen sensor FixL. Biochemistry 1996, 35(29):9539-9548. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1021/bi9530853.
    • (1996) Biochemistry , vol.35 , Issue.29 , pp. 9539-9548
    • Rodgers, K.R.1    Lukat-Rodgers, G.S.2    Barron, J.A.3
  • 143
    • 0033784706 scopus 로고    scopus 로고
    • Nitrosyl adducts of FixL as probes of heme environment
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Rodgers K.R., Lukat-Rodgers G.S., Tang L. Nitrosyl adducts of FixL as probes of heme environment. Journal of Biological Inorganic Chemistry 2000, 5(5):642-654. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (2000) Journal of Biological Inorganic Chemistry , vol.5 , Issue.5 , pp. 642-654
    • Rodgers, K.R.1    Lukat-Rodgers, G.S.2    Tang, L.3
  • 144
    • 0023090935 scopus 로고
    • Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid
    • Ross P., Weinhouse H., Aloni Y., Michaeli D., Weinberger-Ohana P., Mayer R., et al. Regulation of cellulose synthesis in Acetobacter xylinum by cyclic diguanylic acid. Nature 1987, 325(6101):279-281.
    • (1987) Nature , vol.325 , Issue.6101 , pp. 279-281
    • Ross, P.1    Weinhouse, H.2    Aloni, Y.3    Michaeli, D.4    Weinberger-Ohana, P.5    Mayer, R.6
  • 145
    • 0035919479 scopus 로고    scopus 로고
    • Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Rutter J., Reick M., Wu L.C., McKnight S.L. Regulation of clock and NPAS2 DNA binding by the redox state of NAD cofactors. Science 2001, 293(5529):510-514. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]. 10.1126/science.1060698.
    • (2001) Science , vol.293 , Issue.5529 , pp. 510-514
    • Rutter, J.1    Reick, M.2    Wu, L.C.3    McKnight, S.L.4
  • 146
    • 33846078828 scopus 로고    scopus 로고
    • Cyclic di-GMP signalling in the virulence and environmental adaptation of Xanthomonas campestris
    • [Research Support, Non-U.S. Gov't]
    • Ryan R.P., Fouhy Y., Lucey J.F., Jiang B.L., He Y.Q., Feng J.X., et al. Cyclic di-GMP signalling in the virulence and environmental adaptation of Xanthomonas campestris. Molecular Microbiology 2007, 63(2):429-442. [Research Support, Non-U.S. Gov't]. 10.1111/j.1365-2958.2006.05531.x.
    • (2007) Molecular Microbiology , vol.63 , Issue.2 , pp. 429-442
    • Ryan, R.P.1    Fouhy, Y.2    Lucey, J.F.3    Jiang, B.L.4    He, Y.Q.5    Feng, J.X.6
  • 147
    • 77950547731 scopus 로고    scopus 로고
    • Cell-cell signal-dependent dynamic interactions between HD-GYP and GGDEF domain proteins mediate virulence in Xanthomonas campestris
    • [Research Support, Non-U.S. Gov't]
    • Ryan R.P., McCarthy Y., Andrade M., Farah C.S., Armitage J.P., Dow J.M. Cell-cell signal-dependent dynamic interactions between HD-GYP and GGDEF domain proteins mediate virulence in Xanthomonas campestris. Proceedings of the National Academy of Sciences of the United States of America 2010, 107(13):5989-5994. [Research Support, Non-U.S. Gov't]. 10.1073/pnas.0912839107.
    • (2010) Proceedings of the National Academy of Sciences of the United States of America , vol.107 , Issue.13 , pp. 5989-5994
    • Ryan, R.P.1    McCarthy, Y.2    Andrade, M.3    Farah, C.S.4    Armitage, J.P.5    Dow, J.M.6
  • 148
    • 0037189552 scopus 로고    scopus 로고
    • Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding site on catalysis and structure
    • Sasakura Y., Hirata S., Sugiyama S., Suzuki S., Taguchi S., Watanabe M., et al. Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding site on catalysis and structure. Journal of Biological Chemistry 2002, 277(26):23821-23827. 10.1074/jbc.M202738200.
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23821-23827
    • Sasakura, Y.1    Hirata, S.2    Sugiyama, S.3    Suzuki, S.4    Taguchi, S.5    Watanabe, M.6
  • 149
    • 0037031927 scopus 로고    scopus 로고
    • Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli
    • [Research Support, Non-U.S. Gov't]
    • Sato A., Sasakura Y., Sugiyama S., Sagami I., Shimizu T., Mizutani Y., et al. Stationary and time-resolved resonance Raman spectra of His77 and Met95 mutants of the isolated heme domain of a direct oxygen sensor from Escherichia coli. Journal of Biological Chemistry 2002, 277(36):32650-32658. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M204559200.
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.36 , pp. 32650-32658
    • Sato, A.1    Sasakura, Y.2    Sugiyama, S.3    Sagami, I.4    Shimizu, T.5    Mizutani, Y.6
  • 150
    • 71649089775 scopus 로고    scopus 로고
    • Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP
    • [Research Support, Non-U.S. Gov't]
    • Sawai H., Yoshioka S., Uchida T., Hyodo M., Hayakawa Y., Ishimori K., et al. Molecular oxygen regulates the enzymatic activity of a heme-containing diguanylate cyclase (HemDGC) for the synthesis of cyclic di-GMP. Biochimica et Biophysica Acta 2010, 1804(1):166-172. [Research Support, Non-U.S. Gov't]. 10.1016/j.bbapap.2009.09.028.
    • (2010) Biochimica et Biophysica Acta , vol.1804 , Issue.1 , pp. 166-172
    • Sawai, H.1    Yoshioka, S.2    Uchida, T.3    Hyodo, M.4    Hayakawa, Y.5    Ishimori, K.6
  • 151
    • 84868144315 scopus 로고    scopus 로고
    • A bacterial hemerythrin domain regulates the activity of a Vibrio cholerae diguanylate cyclase
    • [Research Support, N.I.H., Extramural]
    • Schaller R.A., Ali S.K., Klose K.E., Kurtz D.M. A bacterial hemerythrin domain regulates the activity of a Vibrio cholerae diguanylate cyclase. Biochemistry 2012, 51(43):8563-8570. [Research Support, N.I.H., Extramural]. 10.1021/bi3011797.
    • (2012) Biochemistry , vol.51 , Issue.43 , pp. 8563-8570
    • Schaller, R.A.1    Ali, S.K.2    Klose, K.E.3    Kurtz, D.M.4
  • 152
    • 0041335297 scopus 로고    scopus 로고
    • Disparate oxygen responsiveness of two regulatory cascades that control expression of symbiotic genes in Bradyrhizobium japonicum
    • [Research Support, Non-U.S. Gov't]
    • Sciotti M.A., Chanfon A., Hennecke H., Fischer H.M. Disparate oxygen responsiveness of two regulatory cascades that control expression of symbiotic genes in Bradyrhizobium japonicum. Journal of Bacteriology 2003, 185(18):5639-5642. [Research Support, Non-U.S. Gov't].
    • (2003) Journal of Bacteriology , vol.185 , Issue.18 , pp. 5639-5642
    • Sciotti, M.A.1    Chanfon, A.2    Hennecke, H.3    Fischer, H.M.4
  • 153
    • 0028963922 scopus 로고
    • Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators
    • [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Shelver D., Kerby R.L., He Y., Roberts G.P. Carbon monoxide-induced activation of gene expression in Rhodospirillum rubrum requires the product of cooA, a member of the cyclic AMP receptor protein family of transcriptional regulators. Journal of Bacteriology 1995, 177(8):2157-2163. [Comparative Study Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (1995) Journal of Bacteriology , vol.177 , Issue.8 , pp. 2157-2163
    • Shelver, D.1    Kerby, R.L.2    He, Y.3    Roberts, G.P.4
  • 154
    • 0030856066 scopus 로고    scopus 로고
    • CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Shelver D., Kerby R.L., He Y., Roberts G.P. CooA, a CO-sensing transcription factor from Rhodospirillum rubrum, is a CO-binding heme protein. Proceedings of the National Academy of Sciences of the United States of America 1997, 94(21):11216-11220. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.21 , pp. 11216-11220
    • Shelver, D.1    Kerby, R.L.2    He, Y.3    Roberts, G.P.4
  • 155
    • 0033514973 scopus 로고    scopus 로고
    • Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Shelver D., Thorsteinsson M.V., Kerby R.L., Chung S.Y., Roberts G.P., Reynolds M.F., et al. Identification of two important heme site residues (cysteine 75 and histidine 77) in CooA, the CO-sensing transcription factor of Rhodospirillum rubrum. Biochemistry 1999, 38(9):2669-2678. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]. 10.1021/bi982658j.
    • (1999) Biochemistry , vol.38 , Issue.9 , pp. 2669-2678
    • Shelver, D.1    Thorsteinsson, M.V.2    Kerby, R.L.3    Chung, S.Y.4    Roberts, G.P.5    Reynolds, M.F.6
  • 156
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility
    • [Research Support, Non-U.S. Gov't]
    • Simm R., Morr M., Kader A., Nimtz M., Romling U. GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. Molecular Microbiology 2004, 53(4):1123-1134. [Research Support, Non-U.S. Gov't]. 10.1111/j.1365-2958.2004.04206.x.
    • (2004) Molecular Microbiology , vol.53 , Issue.4 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Romling, U.5
  • 157
    • 80052773225 scopus 로고    scopus 로고
    • Convergent genomic studies identify association of GRIK2 and NPAS2 with chronic fatigue syndrome
    • [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Smith A.K., Fang H., Whistler T., Unger E.R., Rajeevan M.S. Convergent genomic studies identify association of GRIK2 and NPAS2 with chronic fatigue syndrome. Neuropsychobiology 2011, 64(4):183-194. [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]. 10.1159/000326692.
    • (2011) Neuropsychobiology , vol.64 , Issue.4 , pp. 183-194
    • Smith, A.K.1    Fang, H.2    Whistler, T.3    Unger, E.R.4    Rajeevan, M.S.5
  • 158
    • 84868158218 scopus 로고    scopus 로고
    • Identification of Cys94 as the distal ligand to the Fe(III) heme in the transcriptional regulator RcoM-2 from Burkholderia xenovorans
    • [Research Support, N.I.H., Extramural]
    • Smith A.T., Marvin K.A., Freeman K.M., Kerby R.L., Roberts G.P., Burstyn J.N. Identification of Cys94 as the distal ligand to the Fe(III) heme in the transcriptional regulator RcoM-2 from Burkholderia xenovorans. Journal of Biological Inorganic Chemistry 2012, 17(7):1071-1082. [Research Support, N.I.H., Extramural]. 10.1007/s00775-012-0920-1.
    • (2012) Journal of Biological Inorganic Chemistry , vol.17 , Issue.7 , pp. 1071-1082
    • Smith, A.T.1    Marvin, K.A.2    Freeman, K.M.3    Kerby, R.L.4    Roberts, G.P.5    Burstyn, J.N.6
  • 159
    • 61449200221 scopus 로고    scopus 로고
    • Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli
    • [Research Support, Non-U.S. Gov't]
    • Sommerfeldt N., Possling A., Becker G., Pesavento C., Tschowri N., Hengge R. Gene expression patterns and differential input into curli fimbriae regulation of all GGDEF/EAL domain proteins in Escherichia coli. Microbiology 2009, 155(Pt 4):1318-1331. [Research Support, Non-U.S. Gov't]. 10.1099/mic.0.024257-0.
    • (2009) Microbiology , vol.155 , Issue.PART 4 , pp. 1318-1331
    • Sommerfeldt, N.1    Possling, A.2    Becker, G.3    Pesavento, C.4    Tschowri, N.5    Hengge, R.6
  • 160
    • 84872817053 scopus 로고    scopus 로고
    • Signal transduction and phosphoryl transfer by a FixL hybrid kinase with low oxygen affinity: Importance of the vicinal PAS domain and receiver aspartate
    • [Research Support, Non-U.S. Gov't]
    • Sousa E.H., Tuckerman J.R., Gondim A.C., Gonzalez G., Gilles-Gonzalez M.A. Signal transduction and phosphoryl transfer by a FixL hybrid kinase with low oxygen affinity: Importance of the vicinal PAS domain and receiver aspartate. Biochemistry 2013, 52(3):456-465. [Research Support, Non-U.S. Gov't]. 10.1021/bi300991r.
    • (2013) Biochemistry , vol.52 , Issue.3 , pp. 456-465
    • Sousa, E.H.1    Tuckerman, J.R.2    Gondim, A.C.3    Gonzalez, G.4    Gilles-Gonzalez, M.A.5
  • 161
    • 34249720952 scopus 로고    scopus 로고
    • A memory of oxygen binding explains the dose response of the heme-based sensor FixL
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Sousa E.H., Tuckerman J.R., Gonzalez G., Gilles-Gonzalez M.A. A memory of oxygen binding explains the dose response of the heme-based sensor FixL. Biochemistry 2007, 46(21):6249-6257. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1021/bi7003334.
    • (2007) Biochemistry , vol.46 , Issue.21 , pp. 6249-6257
    • Sousa, E.H.1    Tuckerman, J.R.2    Gonzalez, G.3    Gilles-Gonzalez, M.A.4
  • 162
    • 79953150407 scopus 로고    scopus 로고
    • Structural insights into inhibition of Bacillus anthracis sporulation by a novel class of non-heme globin sensor domains
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Stranzl G.R., Santelli E., Bankston L.A., La Clair C., Bobkov A., Schwarzenbacher R., et al. Structural insights into inhibition of Bacillus anthracis sporulation by a novel class of non-heme globin sensor domains. Journal of Biological Chemistry 2011, 286(10):8448-8458. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1074/jbc.M110.207126.
    • (2011) Journal of Biological Chemistry , vol.286 , Issue.10 , pp. 8448-8458
    • Stranzl, G.R.1    Santelli, E.2    Bankston, L.A.3    La Clair, C.4    Bobkov, A.5    Schwarzenbacher, R.6
  • 163
    • 77957862775 scopus 로고    scopus 로고
    • The diguanylate cyclase YddV controls production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through regulation of the PNAG biosynthetic pgaABCD operon
    • [Research Support, Non-U.S. Gov't]
    • Tagliabue L., Antoniani D., Maciag A., Bocci P., Raffaelli N., Landini P. The diguanylate cyclase YddV controls production of the exopolysaccharide poly-N-acetylglucosamine (PNAG) through regulation of the PNAG biosynthetic pgaABCD operon. Microbiology 2010, 156(Pt 10):2901-2911. [Research Support, Non-U.S. Gov't]. 10.1099/mic.0.041350-0.
    • (2010) Microbiology , vol.156 , Issue.PART 10 , pp. 2901-2911
    • Tagliabue, L.1    Antoniani, D.2    Maciag, A.3    Bocci, P.4    Raffaelli, N.5    Landini, P.6
  • 164
    • 77954639898 scopus 로고    scopus 로고
    • The yddV-dos operon controls biofilm formation through the regulation of genes encoding curli fibers' subunits in aerobically growing Escherichia coli
    • Tagliabue L., Maciag A., Antoniani D., Landini P. The yddV-dos operon controls biofilm formation through the regulation of genes encoding curli fibers' subunits in aerobically growing Escherichia coli. FEMS Immunology and Medical Microbiology 2010, 59(3):477-484. 10.1111/j.1574-695X.2010.00702.x.
    • (2010) FEMS Immunology and Medical Microbiology , vol.59 , Issue.3 , pp. 477-484
    • Tagliabue, L.1    Maciag, A.2    Antoniani, D.3    Landini, P.4
  • 165
    • 0942276394 scopus 로고    scopus 로고
    • Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli. Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met-95 mutants
    • Taguchi S., Matsui T., Igarashi J., Sasakura Y., Araki Y., Ito O., et al. Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli. Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met-95 mutants. Journal of Biological Chemistry 2004, 279(5):3340-3347. 10.1074/jbc.M301013200.
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3340-3347
    • Taguchi, S.1    Matsui, T.2    Igarashi, J.3    Sasakura, Y.4    Araki, Y.5    Ito, O.6
  • 166
    • 79959401969 scopus 로고    scopus 로고
    • Retinoic acid-related orphan receptor gamma directly regulates neuronal PAS domain protein 2 transcription in vivo
    • [Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural]
    • Takeda Y., Kang H.S., Angers M., Jetten A.M. Retinoic acid-related orphan receptor gamma directly regulates neuronal PAS domain protein 2 transcription in vivo. Nucleic Acids Research 2011, 39(11):4769-4782. [Research Support, N.I.H., Extramural Research Support, N.I.H., Intramural]. 10.1093/nar/gkq1335.
    • (2011) Nucleic Acids Research , vol.39 , Issue.11 , pp. 4769-4782
    • Takeda, Y.1    Kang, H.S.2    Angers, M.3    Jetten, A.M.4
  • 167
    • 0031783181 scopus 로고    scopus 로고
    • Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: Genetic organization and occurrence of conserved domains in isoenzymes
    • [Research Support, Non-U.S. Gov't]
    • Tal R., Wong H.C., Calhoon R., Gelfand D., Fear A.L., Volman G., et al. Three cdg operons control cellular turnover of cyclic di-GMP in Acetobacter xylinum: Genetic organization and occurrence of conserved domains in isoenzymes. Journal of Bacteriology 1998, 180(17):4416-4425. [Research Support, Non-U.S. Gov't].
    • (1998) Journal of Bacteriology , vol.180 , Issue.17 , pp. 4416-4425
    • Tal, R.1    Wong, H.C.2    Calhoon, R.3    Gelfand, D.4    Fear, A.L.5    Volman, G.6
  • 168
    • 35848951876 scopus 로고    scopus 로고
    • Roles of cyclic diguanylate in the regulation of bacterial pathogenesis
    • [Research Support, N.I.H., Extramural Review]
    • Tamayo R., Pratt J.T., Camilli A. Roles of cyclic diguanylate in the regulation of bacterial pathogenesis. Annual Review of Microbiology 2007, 61:131-148. [Research Support, N.I.H., Extramural Review]. 10.1146/annurev.micro.61.080706.093426.
    • (2007) Annual Review of Microbiology , vol.61 , pp. 131-148
    • Tamayo, R.1    Pratt, J.T.2    Camilli, A.3
  • 169
    • 33644537046 scopus 로고    scopus 로고
    • Roles of the heme distal residues of FixL in O2 sensing: A single convergent structure of the heme moiety is relevant to the downregulation of kinase activity
    • [Research Support, Non-U.S. Gov't]
    • Tanaka A., Nakamura H., Shiro Y., Fujii H. Roles of the heme distal residues of FixL in O2 sensing: A single convergent structure of the heme moiety is relevant to the downregulation of kinase activity. Biochemistry 2006, 45(8):2515-2523. [Research Support, Non-U.S. Gov't]. 10.1021/bi051989a.
    • (2006) Biochemistry , vol.45 , Issue.8 , pp. 2515-2523
    • Tanaka, A.1    Nakamura, H.2    Shiro, Y.3    Fujii, H.4
  • 170
    • 57649114078 scopus 로고    scopus 로고
    • Ligand binding to the Fe(III)-protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: Roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand binding
    • [Comparative Study Research Support, Non-U.S. Gov't]
    • Tanaka A., Shimizu T. Ligand binding to the Fe(III)-protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: Roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand binding. Biochemistry 2008, 47(50):13438-13446. [Comparative Study Research Support, Non-U.S. Gov't]. 10.1021/bi8012017.
    • (2008) Biochemistry , vol.47 , Issue.50 , pp. 13438-13446
    • Tanaka, A.1    Shimizu, T.2
  • 171
    • 34547137430 scopus 로고    scopus 로고
    • Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward Cyclic diGMP
    • [Research Support, Non-U.S. Gov't]
    • Tanaka A., Takahashi H., Shimizu T. Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward Cyclic diGMP. Journal of Biological Chemistry 2007, 282(29):21301-21307. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M701920200.
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.29 , pp. 21301-21307
    • Tanaka, A.1    Takahashi, H.2    Shimizu, T.3
  • 172
    • 38049105509 scopus 로고    scopus 로고
    • Characterization of a globin-coupled oxygen sensor with a gene-regulating function
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Thijs L., Vinck E., Bolli A., Trandafir F., Wan X., Hoogewijs D., et al. Characterization of a globin-coupled oxygen sensor with a gene-regulating function. Journal of Biological Chemistry 2007, 282(52):37325-37340. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1074/jbc.M705541200.
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.52 , pp. 37325-37340
    • Thijs, L.1    Vinck, E.2    Bolli, A.3    Trandafir, F.4    Wan, X.5    Hoogewijs, D.6
  • 173
    • 3843069972 scopus 로고    scopus 로고
    • Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation
    • [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Tischler A.D., Camilli A. Cyclic diguanylate (c-di-GMP) regulates Vibrio cholerae biofilm formation. Molecular Microbiology 2004, 53(3):857-869. [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]. 10.1111/j.1365-2958.2004.04155.x.
    • (2004) Molecular Microbiology , vol.53 , Issue.3 , pp. 857-869
    • Tischler, A.D.1    Camilli, A.2
  • 174
    • 70350047301 scopus 로고    scopus 로고
    • An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Tuckerman J.R., Gonzalez G., Sousa E.H., Wan X., Saito J.A., Alam M., et al. An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control. Biochemistry 2009, 48(41):9764-9774. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1021/bi901409g.
    • (2009) Biochemistry , vol.48 , Issue.41 , pp. 9764-9774
    • Tuckerman, J.R.1    Gonzalez, G.2    Sousa, E.H.3    Wan, X.4    Saito, J.A.5    Alam, M.6
  • 175
    • 0040182564 scopus 로고    scopus 로고
    • Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy
    • [Research Support, Non-U.S. Gov't]
    • Uchida T., Ishikawa H., Ishimori K., Morishima I., Nakajima H., Aono S., et al. Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy. Biochemistry 2000, 39(42):12747-12752. [Research Support, Non-U.S. Gov't].
    • (2000) Biochemistry , vol.39 , Issue.42 , pp. 12747-12752
    • Uchida, T.1    Ishikawa, H.2    Ishimori, K.3    Morishima, I.4    Nakajima, H.5    Aono, S.6
  • 176
    • 0032493819 scopus 로고    scopus 로고
    • Heme environmental structure of CooA is modulated by the target DNA binding. Evidence from resonance Raman spectroscopy and CO rebinding kinetics
    • [Research Support, Non-U.S. Gov't]
    • Uchida T., Ishikawa H., Takahashi S., Ishimori K., Morishima I., Ohkubo K., et al. Heme environmental structure of CooA is modulated by the target DNA binding. Evidence from resonance Raman spectroscopy and CO rebinding kinetics. Journal of Biological Chemistry 1998, 273(32):19988-19992. [Research Support, Non-U.S. Gov't].
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 19988-19992
    • Uchida, T.1    Ishikawa, H.2    Takahashi, S.3    Ishimori, K.4    Morishima, I.5    Ohkubo, K.6
  • 177
    • 84863407362 scopus 로고    scopus 로고
    • Effects of the bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): Conversion from His119/Cys170 coordination to His119/His171 coordination
    • [Research Support, Non-U.S. Gov't]
    • Uchida T., Sagami I., Shimizu T., Ishimori K., Kitagawa T. Effects of the bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): Conversion from His119/Cys170 coordination to His119/His171 coordination. Journal of Inorganic Biochemistry 2012, 108:188-195. [Research Support, Non-U.S. Gov't]. 10.1016/j.jinorgbio.2011.12.005.
    • (2012) Journal of Inorganic Biochemistry , vol.108 , pp. 188-195
    • Uchida, T.1    Sagami, I.2    Shimizu, T.3    Ishimori, K.4    Kitagawa, T.5
  • 178
    • 20444374458 scopus 로고    scopus 로고
    • CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2
    • [Research Support, Non-U.S. Gov't]
    • Uchida T., Sato E., Sato A., Sagami I., Shimizu T., Kitagawa T. CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2. Journal of Biological Chemistry 2005, 280(22):21358-21368. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M412350200.
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.22 , pp. 21358-21368
    • Uchida, T.1    Sato, E.2    Sato, A.3    Sagami, I.4    Shimizu, T.5    Kitagawa, T.6
  • 182
    • 34447526069 scopus 로고    scopus 로고
    • A model of globin evolution
    • [Research Support, Non-U.S. Gov't]
    • Vinogradov S.N., Hoogewijs D., Bailly X., Mizuguchi K., Dewilde S., Moens L., et al. A model of globin evolution. Gene 2007, 398(1-2):132-142. [Research Support, Non-U.S. Gov't]. 10.1016/j.gene.2007.02.041.
    • (2007) Gene , vol.398 , Issue.1-2 , pp. 132-142
    • Vinogradov, S.N.1    Hoogewijs, D.2    Bailly, X.3    Mizuguchi, K.4    Dewilde, S.5    Moens, L.6
  • 183
    • 44049108195 scopus 로고    scopus 로고
    • Diversity of globin function: Enzymatic, transport, storage, and sensing
    • [Review]
    • Vinogradov S.N., Moens L. Diversity of globin function: Enzymatic, transport, storage, and sensing. Journal of Biological Chemistry 2008, 283(14):8773-8777. [Review]. 10.1074/jbc.R700029200.
    • (2008) Journal of Biological Chemistry , vol.283 , Issue.14 , pp. 8773-8777
    • Vinogradov, S.N.1    Moens, L.2
  • 185
    • 0024006507 scopus 로고
    • Common regulatory elements control symbiotic and microaerobic induction of nifA in Rhizobium meliloti
    • [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.]
    • Virts E.L., Stanfield S.W., Helinski D.R., Ditta G.S. Common regulatory elements control symbiotic and microaerobic induction of nifA in Rhizobium meliloti. Proceedings of the National Academy of Sciences of the United States of America 1988, 85(9):3062-3065. [Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.].
    • (1988) Proceedings of the National Academy of Sciences of the United States of America , vol.85 , Issue.9 , pp. 3062-3065
    • Virts, E.L.1    Stanfield, S.W.2    Helinski, D.R.3    Ditta, G.S.4
  • 186
    • 0033515050 scopus 로고    scopus 로고
    • Resonance Raman evidence for a novel charge relay activation mechanism of the CO-dependent heme protein transcription factor CooA
    • [Research Support, U.S. Gov't, P.H.S.]
    • Vogel K.M., Spiro T.G., Shelver D., Thorsteinsson M.V., Roberts G.P. Resonance Raman evidence for a novel charge relay activation mechanism of the CO-dependent heme protein transcription factor CooA. Biochemistry 1999, 38(9):2679-2687. [Research Support, U.S. Gov't, P.H.S.]. 10.1021/bi982375r.
    • (1999) Biochemistry , vol.38 , Issue.9 , pp. 2679-2687
    • Vogel, K.M.1    Spiro, T.G.2    Shelver, D.3    Thorsteinsson, M.V.4    Roberts, G.P.5
  • 187
    • 64449088389 scopus 로고    scopus 로고
    • Globins synthesize the second messenger bis-(3'-5')-cyclic diguanosine monophosphate in bacteria
    • [Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]
    • Wan X., Tuckerman J.R., Saito J.A., Freitas T.A., Newhouse J.S., Denery J.R., et al. Globins synthesize the second messenger bis-(3'-5')-cyclic diguanosine monophosphate in bacteria. Journal of Molecular Biology 2009, 388(2):262-270. [Research Support, N.I.H., Intramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.]. 10.1016/j.jmb.2009.03.015.
    • (2009) Journal of Molecular Biology , vol.388 , Issue.2 , pp. 262-270
    • Wan, X.1    Tuckerman, J.R.2    Saito, J.A.3    Freitas, T.A.4    Newhouse, J.S.5    Denery, J.R.6
  • 188
    • 79958278160 scopus 로고    scopus 로고
    • A variant affecting miRNAs binding in the circadian gene Neuronal PAS domain protein 2 (NPAS2) is not associated with breast cancer risk
    • [Research Support, Non-U.S. Gov't]
    • Wang F., Hu Z., Yang R., Tang J., Liu Y., Hemminki K., et al. A variant affecting miRNAs binding in the circadian gene Neuronal PAS domain protein 2 (NPAS2) is not associated with breast cancer risk. Breast Cancer Research and Treatment 2011, 127(3):769-775. [Research Support, Non-U.S. Gov't]. 10.1007/s10549-010-1157-8.
    • (2011) Breast Cancer Research and Treatment , vol.127 , Issue.3 , pp. 769-775
    • Wang, F.1    Hu, Z.2    Yang, R.3    Tang, J.4    Liu, Y.5    Hemminki, K.6
  • 189
    • 0030734277 scopus 로고    scopus 로고
    • C-di-GMP-binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum
    • [Research Support, Non-U.S. Gov't]
    • Weinhouse H., Sapir S., Amikam D., Shilo Y., Volman G., Ohana P., et al. c-di-GMP-binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum. FEBS Letters 1997, 416(2):207-211. [Research Support, Non-U.S. Gov't].
    • (1997) FEBS Letters , vol.416 , Issue.2 , pp. 207-211
    • Weinhouse, H.1    Sapir, S.2    Amikam, D.3    Shilo, Y.4    Volman, G.5    Ohana, P.6
  • 190
    • 42449107875 scopus 로고    scopus 로고
    • Genetic components of the circadian clock regulate thrombogenesis in vivo
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]
    • Westgate E.J., Cheng Y., Reilly D.F., Price T.S., Walisser J.A., Bradfield C.A., et al. Genetic components of the circadian clock regulate thrombogenesis in vivo. Circulation 2008, 117(16):2087-2095. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]. 10.1161/CIRCULATIONAHA.107.739227.
    • (2008) Circulation , vol.117 , Issue.16 , pp. 2087-2095
    • Westgate, E.J.1    Cheng, Y.2    Reilly, D.F.3    Price, T.S.4    Walisser, J.A.5    Bradfield, C.A.6
  • 191
    • 49049110545 scopus 로고    scopus 로고
    • Sleep deprivation effects on circadian clock gene expression in the cerebral cortex parallel electroencephalographic differences among mouse strains
    • [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.]
    • Wisor J.P., Pasumarthi R.K., Gerashchenko D., Thompson C.L., Pathak S., Sancar A., et al. Sleep deprivation effects on circadian clock gene expression in the cerebral cortex parallel electroencephalographic differences among mouse strains. Journal of Neuroscience 2008, 28(28):7193-7201. [Research Support, N.I.H., Extramural Research Support, U.S. Gov't, Non-P.H.S.]. 10.1523/JNEUROSCI.1150-08.2008.
    • (2008) Journal of Neuroscience , vol.28 , Issue.28 , pp. 7193-7201
    • Wisor, J.P.1    Pasumarthi, R.K.2    Gerashchenko, D.3    Thompson, C.L.4    Pathak, S.5    Sancar, A.6
  • 192
    • 0035853755 scopus 로고    scopus 로고
    • Binding of CO at the Pro2 side is crucial for the activation of CO-sensing transcriptional activator CooA. (1)H NMR spectroscopic studies
    • [Research Support, Non-U.S. Gov't]
    • Yamamoto K., Ishikawa H., Takahashi S., Ishimori K., Morishima I., Nakajima H., et al. Binding of CO at the Pro2 side is crucial for the activation of CO-sensing transcriptional activator CooA. (1)H NMR spectroscopic studies. Journal of Biological Chemistry 2001, 276(15):11473-11476. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.C100047200.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.15 , pp. 11473-11476
    • Yamamoto, K.1    Ishikawa, H.2    Takahashi, S.3    Ishimori, K.4    Morishima, I.5    Nakajima, H.6
  • 193
    • 8744264927 scopus 로고    scopus 로고
    • The C-helix in CooA rolls upon CO binding to ferrous heme
    • [Research Support, Non-U.S. Gov't]
    • Yamashita T., Hoashi Y., Tomisugi Y., Ishikawa Y., Uno T. The C-helix in CooA rolls upon CO binding to ferrous heme. Journal of Biological Chemistry 2004, 279(45):47320-47325. [Research Support, Non-U.S. Gov't]. 10.1074/jbc.M407766200.
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.45 , pp. 47320-47325
    • Yamashita, T.1    Hoashi, Y.2    Tomisugi, Y.3    Ishikawa, Y.4    Uno, T.5
  • 194
    • 77950867308 scopus 로고    scopus 로고
    • The circadian gene NPAS2 is a novel prognostic biomarker for breast cancer
    • [Research Support, N.I.H., Extramural]
    • Yi C., Mu L., de la Longrais I.A., Sochirca O., Arisio R., Yu H., et al. The circadian gene NPAS2 is a novel prognostic biomarker for breast cancer. Breast Cancer Research and Treatment 2010, 120(3):663-669. [Research Support, N.I.H., Extramural]. 10.1007/s10549-009-0484-0.
    • (2010) Breast Cancer Research and Treatment , vol.120 , Issue.3 , pp. 663-669
    • Yi, C.1    Mu, L.2    de la Longrais, I.A.3    Sochirca, O.4    Arisio, R.5    Yu, H.6
  • 195
    • 69549127974 scopus 로고    scopus 로고
    • Cancer-related transcriptional targets of the circadian gene NPAS2 identified by genome-wide ChIP-on-chip analysis
    • [Research Support, N.I.H., Extramural]
    • Yi C.H., Zheng T., Leaderer D., Hoffman A., Zhu Y. Cancer-related transcriptional targets of the circadian gene NPAS2 identified by genome-wide ChIP-on-chip analysis. Cancer Letters 2009, 284(2):149-156. [Research Support, N.I.H., Extramural]. 10.1016/j.canlet.2009.04.017.
    • (2009) Cancer Letters , vol.284 , Issue.2 , pp. 149-156
    • Yi, C.H.1    Zheng, T.2    Leaderer, D.3    Hoffman, A.4    Zhu, Y.5
  • 196
    • 84861566182 scopus 로고    scopus 로고
    • Structural dynamics of proximal heme pocket in HemAT-Bs associated with oxygen dissociation
    • [Research Support, Non-U.S. Gov't]
    • Yoshida Y., Ishikawa H., Aono S., Mizutani Y. Structural dynamics of proximal heme pocket in HemAT-Bs associated with oxygen dissociation. Biochimica et Biophysica Acta 2012, 1824(7):866-872. [Research Support, Non-U.S. Gov't]. 10.1016/j.bbapap.2012.04.007.
    • (2012) Biochimica et Biophysica Acta , vol.1824 , Issue.7 , pp. 866-872
    • Yoshida, Y.1    Ishikawa, H.2    Aono, S.3    Mizutani, Y.4
  • 197
    • 33745814412 scopus 로고    scopus 로고
    • Specific hydrogen-bonding networks responsible for selective O2 sensing of the oxygen sensor protein HemAT from Bacillus subtilis
    • [Research Support, Non-U.S. Gov't]
    • Yoshimura H., Yoshioka S., Kobayashi K., Ohta T., Uchida T., Kubo M., et al. Specific hydrogen-bonding networks responsible for selective O2 sensing of the oxygen sensor protein HemAT from Bacillus subtilis. Biochemistry 2006, 45(27):8301-8307. [Research Support, Non-U.S. Gov't]. 10.1021/bi060315c.
    • (2006) Biochemistry , vol.45 , Issue.27 , pp. 8301-8307
    • Yoshimura, H.1    Yoshioka, S.2    Kobayashi, K.3    Ohta, T.4    Uchida, T.5    Kubo, M.6
  • 198
    • 34247877483 scopus 로고    scopus 로고
    • The formation of hydrogen bond in the proximal heme pocket of HemAT-Bs upon ligand binding
    • [Research Support, Non-U.S. Gov't]
    • Yoshimura H., Yoshioka S., Mizutani Y., Aono S. The formation of hydrogen bond in the proximal heme pocket of HemAT-Bs upon ligand binding. Biochemical and Biophysical Research Communications 2007, 357(4):1053-1057. [Research Support, Non-U.S. Gov't]. 10.1016/j.bbrc.2007.04.041.
    • (2007) Biochemical and Biophysical Research Communications , vol.357 , Issue.4 , pp. 1053-1057
    • Yoshimura, H.1    Yoshioka, S.2    Mizutani, Y.3    Aono, S.4
  • 199
    • 0347623828 scopus 로고    scopus 로고
    • The heme pocket afforded by Gly117 is crucial for proper heme ligation and activity of CooA
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Youn H., Kerby R.L., Thorsteinsson M.V., Conrad M., Staples C.R., Serate J., et al. The heme pocket afforded by Gly117 is crucial for proper heme ligation and activity of CooA. Journal of Biological Chemistry 2001, 276(45):41603-41610. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]. 10.1074/jbc.M106165200.
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.45 , pp. 41603-41610
    • Youn, H.1    Kerby, R.L.2    Thorsteinsson, M.V.3    Conrad, M.4    Staples, C.R.5    Serate, J.6
  • 200
    • 16844375556 scopus 로고    scopus 로고
    • Dual roles of an E-helix residue, Glu167, in the transcriptional activator function of CooA
    • [Research Support, Non-U.S. Gov't]
    • Youn H., Thorsteinsson M.V., Conrad M., Kerby R.L., Roberts G.P. Dual roles of an E-helix residue, Glu167, in the transcriptional activator function of CooA. Journal of Bacteriology 2005, 187(8):2573-2581. [Research Support, Non-U.S. Gov't]. 10.1128/JB.187.8.2573-2581.2005.
    • (2005) Journal of Bacteriology , vol.187 , Issue.8 , pp. 2573-2581
    • Youn, H.1    Thorsteinsson, M.V.2    Conrad, M.3    Kerby, R.L.4    Roberts, G.P.5
  • 201
    • 0042334880 scopus 로고    scopus 로고
    • Structure of the oxygen sensor in Bacillus subtilis: Signal transduction of chemotaxis by control of symmetry
    • [Comparative Study Research Support, Non-U.S. Gov't]
    • Zhang W., Phillips G.N. Structure of the oxygen sensor in Bacillus subtilis: Signal transduction of chemotaxis by control of symmetry. Structure 2003, 11(9):1097-1110. [Comparative Study Research Support, Non-U.S. Gov't].
    • (2003) Structure , vol.11 , Issue.9 , pp. 1097-1110
    • Zhang, W.1    Phillips, G.N.2
  • 202
  • 203
    • 12644279862 scopus 로고    scopus 로고
    • Molecular characterization of two mammalian bHLH-PAS domain proteins selectively expressed in the central nervous system
    • [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.]
    • Zhou Y.D., Barnard M., Tian H., Li X., Ring H.Z., Francke U., et al. Molecular characterization of two mammalian bHLH-PAS domain proteins selectively expressed in the central nervous system. Proceedings of the National Academy of Sciences of the United States of America 1997, 94(2):713-718. [Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.].
    • (1997) Proceedings of the National Academy of Sciences of the United States of America , vol.94 , Issue.2 , pp. 713-718
    • Zhou, Y.D.1    Barnard, M.2    Tian, H.3    Li, X.4    Ring, H.Z.5    Francke, U.6
  • 204
    • 33845646398 scopus 로고    scopus 로고
    • Ala394Thr polymorphism in the clock gene NPAS2: A circadian modifier for the risk of non-Hodgkin's lymphoma
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]
    • Zhu Y., Leaderer D., Guss C., Brown H.N., Zhang Y., Boyle P., et al. Ala394Thr polymorphism in the clock gene NPAS2: A circadian modifier for the risk of non-Hodgkin's lymphoma. International Journal of Cancer 2007, 120(2):432-435. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]. 10.1002/ijc.22321.
    • (2007) International Journal of Cancer , vol.120 , Issue.2 , pp. 432-435
    • Zhu, Y.1    Leaderer, D.2    Guss, C.3    Brown, H.N.4    Zhang, Y.5    Boyle, P.6
  • 205
    • 73649083745 scopus 로고    scopus 로고
    • Testing the circadian gene hypothesis in prostate cancer: A population-based case-control study
    • [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]
    • Zhu Y., Stevens R.G., Hoffman A.E., Fitzgerald L.M., Kwon E.M., Ostrander E.A., et al. Testing the circadian gene hypothesis in prostate cancer: A population-based case-control study. Cancer Research 2009, 69(24):9315-9322. [Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't]. 10.1158/0008-5472.CAN-09-0648.
    • (2009) Cancer Research , vol.69 , Issue.24 , pp. 9315-9322
    • Zhu, Y.1    Stevens, R.G.2    Hoffman, A.E.3    Fitzgerald, L.M.4    Kwon, E.M.5    Ostrander, E.A.6
  • 206
    • 38649085338 scopus 로고    scopus 로고
    • Non-synonymous polymorphisms in the circadian gene NPAS2 and breast cancer risk
    • [Research Support, N.I.H., Extramural]
    • Zhu Y., Stevens R.G., Leaderer D., Hoffman A., Holford T., Zhang Y., et al. Non-synonymous polymorphisms in the circadian gene NPAS2 and breast cancer risk. Breast Cancer Research and Treatment 2008, 107(3):421-425. [Research Support, N.I.H., Extramural]. 10.1007/s10549-007-9565-0.
    • (2008) Breast Cancer Research and Treatment , vol.107 , Issue.3 , pp. 421-425
    • Zhu, Y.1    Stevens, R.G.2    Leaderer, D.3    Hoffman, A.4    Holford, T.5    Zhang, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.