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Volumn 65, Issue , 2011, Pages 261-286

Ligand-binding PAS domains in a genomic, cellular, and structural context

Author keywords

Ligand binding; PAS; Sensor; Signal transduction

Indexed keywords

BACTERIAL PROTEIN; CYCLIC GMP DEPENDENT PROTEIN KINASE; HEME; HYDROLASE; PHOSPHODIESTERASE; PROTEIN HISTIDINE KINASE;

EID: 80053291460     PISSN: 00664227     EISSN: 15453251     Source Type: Book Series    
DOI: 10.1146/annurev-micro-121809-151631     Document Type: Review
Times cited : (309)

References (119)
  • 1
    • 0035141969 scopus 로고    scopus 로고
    • B of Bacillus subtilis
    • DOI 10.1128/JB.183.4.1329-1338.2001
    • Akbar S, Gaidenko TA, Kang CM, O'Reilly M, Devine KM, Price CW. 2001. New family of regulators in the environmental signaling pathway which activates the general stress transcription factor sigma(B) of Bacillus subtilis. J. Bacteriol. 183:1329-38 (Pubitemid 32107729)
    • (2001) Journal of Bacteriology , vol.183 , Issue.4 , pp. 1329-1338
    • Akbar, S.1    Gaidenko, T.A.2    Min Kang, C.3    O'Reilly, M.4    Devine, K.M.5    Price, C.W.6
  • 2
    • 0036774056 scopus 로고    scopus 로고
    • Structure and interactions of PAS Kinase N-terminal PAS domain: Model for intramolecular kinase regulation
    • DOI 10.1016/S0969-2126(02)00857-2, PII S0969212602008572
    • Amezcua CA, Harper SM, Rutter J, Gardner KH. 2002. Structure and interactions of PAS kinase Nterminal PAS domain: model for intramolecular kinase regulation. Structure 10:1349-61 (Pubitemid 35232384)
    • (2002) Structure , vol.10 , Issue.10 , pp. 1349-1361
    • Amezcua, C.A.1    Harper, S.M.2    Rutter, J.3    Gardner, K.H.4
  • 3
    • 0035853296 scopus 로고    scopus 로고
    • Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains
    • DOI 10.1006/jmbi.2001.4508
    • Anantharaman V, Koonin EV, Aravind L. 2001. Regulatory potential, phyletic distribution and evolution of ancient, intracellular small-molecule-binding domains. J. Mol. Biol. 307:1271-92 (Pubitemid 33027639)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.5 , pp. 1271-1292
    • Anantharaman, V.1    Koonin, E.V.2    Aravind, L.3
  • 5
    • 0030712081 scopus 로고    scopus 로고
    • The GAF domain: An evolutionary link between diverse phototransducing proteins
    • DOI 10.1016/S0968-0004(97)01148-1, PII S0968000497011481
    • Aravind L, Ponting CP. 1997. The GAF domain: an evolutionary link between diverse phototransducing proteins. Trends Biochem. Sci. 22:458-59 (Pubitemid 27515909)
    • (1997) Trends in Biochemical Sciences , vol.22 , Issue.12 , pp. 458-459
    • Aravind, L.1    Ponting, C.P.2
  • 6
    • 33749021097 scopus 로고    scopus 로고
    • B-dependent stress response of Bacillus subtilis via YtvA
    • DOI 10.1128/JB.00716-06
    • Avila-PerezM,Hellingwerf KJ, Kort R. 2006. Blue light activates the sigmaB-dependent stress response of Bacillus subtilis via YtvA. J. Bacteriol. 188:6411-14 (Pubitemid 44448584)
    • (2006) Journal of Bacteriology , vol.188 , Issue.17 , pp. 6411-6414
    • Avila-Perez, M.1    Hellingwerf, K.J.2    Kort, R.3
  • 7
    • 0028577744 scopus 로고
    • Complete chemical structure of photoactive yellow protein: Novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry
    • Baca M, Borgstahl GE, BoissinotM, Burke PM,Williams DR, et al. 1994. Complete chemical structure of photoactive yellow protein: novel thioester-linked 4-hydroxycinnamyl chromophore and photocycle chemistry. Biochemistry 33:14369-77
    • (1994) Biochemistry , vol.33 , pp. 14369-77
    • Baca, M.1    Borgstahl, G.E.2    Boissinot, M.3    Burke, P.M.4    Williams, D.R.5
  • 9
    • 4344671750 scopus 로고    scopus 로고
    • Hypercyst mutants in Rhodospirillum centenum identify regulatory loci involved in cyst cell differentiation
    • DOI 10.1128/JB.186.17.5834-5841.2004
    • Berleman JE, Hasselbring BM, Bauer CE. 2004. Hypercyst mutants in Rhodospirillum centenum identify regulatory loci involved in cyst cell differentiation. J. Bacteriol. 186:5834-41 (Pubitemid 39128657)
    • (2004) Journal of Bacteriology , vol.186 , Issue.17 , pp. 5834-5841
    • Berleman, J.E.1    Hasselbring, B.M.2    Bauer, C.E.3
  • 13
    • 0029110488 scopus 로고
    • 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: Unusual fold, active site, and chromophore
    • BorgstahlGE, WilliamsDR, Getzoff ED. 1995. 1.4 A structure of photoactive yellow protein, a cytosolic photoreceptor: unusual fold, active site, and chromophore. Biochemistry 34:6278-87
    • (1995) Biochemistry , vol.34 , pp. 6278-87
    • Borgstahl, G.E.1    Williams, D.R.2    Getzoff, E.D.3
  • 14
    • 0030893492 scopus 로고    scopus 로고
    • Anaerobic citrate metabolism and its regulation in enterobacteria
    • DOI 10.1007/s002030050419
    • Bott M. 1997. Anaerobic citrate metabolism and its regulation in enterobacteria. Arch.Microbiol. 167:78-88 (Pubitemid 27141756)
    • (1997) Archives of Microbiology , vol.167 , Issue.2-3 , pp. 78-88
    • Bott, M.1
  • 15
    • 77956090680 scopus 로고    scopus 로고
    • Probing the chemotaxis periplasmic sensor domains from Geobacter sulfurreducens by combined resonance Raman and molecular dynamic approaches: NO and CO sensing
    • Catarino T, Pessanha M, De Candia AG, Gouveia Z, Fernandes AP, et al. 2010. Probing the chemotaxis periplasmic sensor domains from Geobacter sulfurreducens by combined resonance Raman and molecular dynamic approaches: NO and CO sensing. J. Phys. Chem. B 114:11251-60
    • (2010) J. Phys. Chem. B , vol.114 , pp. 11251-60
    • Catarino, T.1    Pessanha, M.2    De Candia, A.G.3    Gouveia, Z.4    Fernandes, A.P.5
  • 16
    • 75749103345 scopus 로고    scopus 로고
    • Extracytoplasmic PAS-like domains are common in signal transduction proteins
    • Chang C, Tesar C, Gu M, Babnigg G, Joachimiak A, et al. 2010. Extracytoplasmic PAS-like domains are common in signal transduction proteins. J. Bacteriol. 192:1156-59
    • (2010) J. Bacteriol. , vol.192 , pp. 1156-59
    • Chang, C.1    Tesar, C.2    Gu, M.3    Babnigg, G.4    Joachimiak, A.5
  • 17
    • 17144394187 scopus 로고    scopus 로고
    • Regulation of phytochrome B nuclear localization through light-dependent unmasking of nuclear-localization signals
    • Chen M, Tao Y, Lim J, Shaw A, Chory J. 2005. Regulation of phytochrome B nuclear localization through light-dependent unmasking of nuclear-localization signals. Curr. Biol. 15:637-42
    • (2005) Curr. Biol. , vol.15 , pp. 637-42
    • Chen, M.1    Tao, Y.2    Lim, J.3    Shaw, A.4    Chory, J.5
  • 19
    • 77949918665 scopus 로고    scopus 로고
    • Sensor domains of two-component regulatory systems
    • Cheung J, HendricksonWA. 2010. Sensor domains of two-component regulatory systems. Curr. Opin. Microbiol. 13:116-23
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 116-23
    • Cheung, J.1    Hendrickson, W.A.2
  • 20
    • 32044465772 scopus 로고    scopus 로고
    • Metal bridges between the PhoQ sensor domain and the membrane regulate transmembrane signaling
    • DOI 10.1016/j.jmb.2005.12.032, PII S0022283605015949
    • Cho US, Bader MW, Amaya MF, Daley ME, Klevit RE, et al. 2006. Metal bridges between the PhoQ sensor domain and the membrane regulate transmembrane signaling. J. Mol. Biol. 356:1193-206 (Pubitemid 43199923)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.5 , pp. 1193-1206
    • Cho, U.S.1    Bader, M.W.2    Amaya, M.F.3    Daley, M.E.4    Klevit, R.E.5    Miller, S.I.6    Xu, W.7
  • 25
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: Photoresponsive signaling modules coupled to diverse output domains
    • DOI 10.1021/bi026978l
    • Crosson S, Rajagopal S, Moffat K. 2003. The LOV domain family: photoresponsive signaling modules coupled to diverse output domains. Biochemistry 42:2-10 (Pubitemid 36083846)
    • (2003) Biochemistry , vol.42 , Issue.1 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 26
    • 0023731837 scopus 로고
    • Cascade regulation of nif gene expression in Rhizobium meliloti
    • David M, Daveran ML, Batut J, Dedieu A, Domergue O, et al. 1988. Cascade regulation of nif gene expression in Rhizobium meliloti. Cell 54:671-83
    • (1988) Cell , vol.54 , pp. 671-83
    • David, M.1    Daveran, M.L.2    Batut, J.3    Dedieu, A.4    Domergue, O.5
  • 27
    • 0025196088 scopus 로고
    • Rhizobium meliloti FixL is an oxygen sensor and regulates R. meliloti nifA and fixK genes differently in Escherichia coli
    • de Philip P, Batut J, Boistard P. 1990. Rhizobium meliloti FixL is an oxygen sensor and regulates R. meliloti nifA and fixK genes differently in Escherichia coli. J. Bacteriol. 172:4255-62 (Pubitemid 20236713)
    • (1990) Journal of Bacteriology , vol.172 , Issue.8 , pp. 4255-4262
    • De Philip, P.1    Batut, J.2    Boistard, P.3
  • 28
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • DOI 10.1021/bi991911s
    • Delgado-Nixon VM, Gonzalez G, Gilles-Gonzalez MA. 2000. Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor. Biochemistry 39:2685-91 (Pubitemid 30148922)
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.-A.3
  • 29
    • 0031818761 scopus 로고    scopus 로고
    • Energy conservation in the decarboxylation of dicarboxylic acids by fermenting bacteria
    • DOI 10.1007/s002030050616
    • Dimroth P, Schink B. 1998. Energy conservation in the decarboxylation of dicarboxylic acids by fermenting bacteria. Arch. Microbiol. 170:69-77 (Pubitemid 28366023)
    • (1998) Archives of Microbiology , vol.170 , Issue.2 , pp. 69-77
    • Dimroth, P.1    Schink, B.2
  • 30
    • 32544436601 scopus 로고    scopus 로고
    • Multiple Alignment of protein structures and sequences for VMD
    • DOI 10.1093/bioinformatics/bti825
    • Eargle J, Wright D, Luthey-Schulten Z. 2006. Multiple alignment of protein structures and sequences for VMD. Bioinformatics 22:504-6 (Pubitemid 43231430)
    • (2006) Bioinformatics , vol.22 , Issue.4 , pp. 504-506
    • Eargle, J.1    Wright, D.2    Luthey-Schulten, Z.3
  • 31
    • 0035678319 scopus 로고    scopus 로고
    • Salmonella typhimurium outer membrane remodeling: Role in resistance to host innate immunity
    • DOI 10.1016/S1286-4579(01)01494-0
    • Ernst RK, Guina T,Miller SI. 2001. Salmonella typhimurium outer membrane remodeling: role in resistance to host innate immunity. Microbes Infect. 3:1327-34 (Pubitemid 34033769)
    • (2001) Microbes and Infection , vol.3 , Issue.14-15 , pp. 1327-1334
    • Ernst, R.K.1    Guina, T.2    Miller, S.I.3
  • 32
    • 63749110404 scopus 로고    scopus 로고
    • Control of Salmonella pathogenicity island-2 gene expression
    • Fass E, Groisman EA. 2009. Control of Salmonella pathogenicity island-2 gene expression. Curr. Opin. Microbiol. 12:199-204
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 199-204
    • Fass, E.1    Groisman, E.A.2
  • 35
    • 0028108941 scopus 로고
    • Genetic regulation of nitrogen fixation in rhizobia
    • Fischer HM. 1994. Genetic regulation of nitrogen fixation in rhizobia. Microbiol. Rev. 58:352-86
    • (1994) Microbiol. Rev. , vol.58 , pp. 352-86
    • Fischer, H.M.1
  • 36
    • 37049246982 scopus 로고
    • Construction of phylogenetic trees
    • FitchWM, Margoliash E. 1967. Construction of phylogenetic trees. Science 155:279-84
    • (1967) Science , vol.155 , pp. 279-84
    • Fitch, W.M.1    Margoliash, E.2
  • 37
    • 2642554922 scopus 로고    scopus 로고
    • Bacterial signal transduction network in a genomic perspective
    • DOI 10.1111/j.1462-2920.2004.00633.x
    • Galperin MY. 2004. Bacterial signal transduction network in a genomic perspective. Environ. Microbiol. 6:552-67 (Pubitemid 38708690)
    • (2004) Environmental Microbiology , vol.6 , Issue.6 , pp. 552-567
    • Galperin, M.Y.1
  • 39
    • 0029671310 scopus 로고    scopus 로고
    • Mg2+ as an extracellular signal: Environmental regulation of Salmonella virulence
    • Garcia-Vescovi E, Soncini FC, Groisman EA. 1996. Mg2+ as an extracellular signal: environmental regulation of Salmonella virulence. Cell 84:165-74
    • (1996) Cell , vol.84 , pp. 165-74
    • Garcia-Vescovi, E.1    Soncini, F.C.2    Groisman, E.A.3
  • 40
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • Gilles-GonzalezMA, Ditta GS,Helinski DR. 1991. A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti. Nature 350:170-72 (Pubitemid 21912192)
    • (1991) Nature , vol.350 , Issue.6314 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 41
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation
    • DOI 10.1021/bi00192a011
    • Gilles-Gonzalez MA, Gonzalez G, Perutz MF, Kiger L, Marden MC, Poyart C. 1994. Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation. Biochemistry 33:8067-73 (Pubitemid 24223828)
    • (1994) Biochemistry , vol.33 , Issue.26 , pp. 8067-8073
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2    Perutz, M.F.3
  • 42
  • 43
    • 0033020794 scopus 로고    scopus 로고
    • 4-Dicarboxylates in Escherichia coli
    • Golby P, Davies S, Kelly DJ, Guest JR, Andrews SC. 1999. Identification and characterization of a twocomponent sensor-kinase and response-regulator system (DcuS-DcuR) controlling gene expression in response to C4-dicarboxylates in Escherichia coli. J. Bacteriol. 181:1238-48 (Pubitemid 29119563)
    • (1999) Journal of Bacteriology , vol.181 , Issue.4 , pp. 1238-1248
    • Golby, P.1    Davies, S.2    Kelly, D.J.3    Guest, J.R.4    Andrews, S.C.5
  • 45
    • 0035968198 scopus 로고    scopus 로고
    • A novel snare N-terminal domain revealed by the crystal structure of Sec22b
    • Gonzalez LC, Weis WI, Scheller RH. 2001. A novel snare N-terminal domain revealed by the crystal structure of Sec22b. J. Biol. Chem. 276:24203-11
    • (2001) J. Biol. Chem. , vol.276 , pp. 24203-11
    • Gonzalez, L.C.1    Weis, W.I.2    Scheller, R.H.3
  • 47
    • 4944243738 scopus 로고    scopus 로고
    • PAS domain of the Aer redox sensor requires C-terminal residues for native-fold formation and flavin adenine dinucleotide binding
    • DOI 10.1128/JB.186.20.6782-6791.2004
    • Herrmann S,Ma Q, Johnson MS, Repik AV, Taylor BL. 2004. PAS domain of the Aer redox sensor requires C-terminal residues for native-fold formation and flavin adenine dinucleotide binding. J. Bacteriol. 186:6782-91 (Pubitemid 39332116)
    • (2004) Journal of Bacteriology , vol.186 , Issue.20 , pp. 6782-6791
    • Herrmann, S.1    Ma, Q.2    Johnson, M.S.3    Repik, A.V.4    Taylor, B.L.5
  • 48
    • 0034676026 scopus 로고    scopus 로고
    • Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor
    • Ho YS, Burden LM, Hurley JH. 2000. Structure of the GAF domain, a ubiquitous signaling motif and a new class of cyclic GMP receptor. EMBO J. 19:5288-99
    • (2000) EMBO J. , vol.19 , pp. 5288-99
    • Ho, Y.S.1    Burden, L.M.2    Hurley, J.H.3
  • 50
    • 0027057526 scopus 로고
    • A database of protein structure families with common folding motifs
    • Holm L, Ouzounis C, Sander C, Tuparev G, Vriend G. 1992. A database of protein structure families with common folding motifs. Protein Sci. 1:1691-98 (Pubitemid 23047485)
    • (1992) Protein Science , vol.1 , Issue.12 , pp. 1691-1698
    • Holm, L.1    Ouzounis, C.2    Sander, C.3    Tuparev, G.4    Vriend, G.5
  • 51
    • 31844444593 scopus 로고    scopus 로고
    • Interaction of pathogenic mycobacteria with the host immune system
    • DOI 10.1016/j.mib.2005.12.014, PII S1369527405002080, Host-Microbe Interactions: Bacteria
    • Houben EN, Nguyen L, Pieters J. 2006. Interaction of pathogenic mycobacteria with the host immune system. Curr. Opin. Microbiol. 9:76-85 (Pubitemid 43184340)
    • (2006) Current Opinion in Microbiology , vol.9 , Issue.1 , pp. 76-85
    • Houben, E.N.G.1    Nguyen, L.2    Pieters, J.3
  • 52
    • 0031470701 scopus 로고    scopus 로고
    • Arabidopsis NPH1: A protein kinase with a putative redox-sensing domain
    • DOI 10.1126/science.278.5346.2120
    • Huala E, Oeller PW, Liscum E, Han IS, Larsen E, Briggs WR. 1997. Arabidopsis NPH1: a protein kinase with a putative redox-sensing domain. Science 278:2120-23 (Pubitemid 28028321)
    • (1997) Science , vol.278 , Issue.5346 , pp. 2120-2123
    • Huala, E.1    Oeller, P.W.2    Liscum, E.3    Han, I.-S.4    Larsen, E.5    Briggs, W.R.6
  • 53
    • 0027184569 scopus 로고
    • PAS is a dimerization domain common to Drosophila period and several transcription factors
    • DOI 10.1038/364259a0
    • Huang ZJ, Edery I, Rosbash M. 1993. PAS is a dimerization domain common to Drosophila period and several transcription factors. Nature 364:259-62 (Pubitemid 23257088)
    • (1993) Nature , vol.364 , Issue.6434 , pp. 259-262
    • Zuoshi Josh Huang1    Edery, I.2    Rosbash, M.3
  • 54
    • 77955275743 scopus 로고    scopus 로고
    • Role of a PAS sensor domain in the Mycobacterium tuberculosis transcription regulator Rv1364c
    • Jaiswal RK, Manjeera G, Gopal B. 2010. Role of a PAS sensor domain in the Mycobacterium tuberculosis transcription regulator Rv1364c. Biochem. Biophys. Res. Commun. 398:342-49
    • (2010) Biochem. Biophys. Res. Commun. , vol.398 , pp. 342-49
    • Jaiswal, R.K.1    Manjeera, G.2    Gopal, B.3
  • 56
    • 0033575370 scopus 로고    scopus 로고
    • Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes
    • DOI 10.1126/science.285.5426.406
    • Jiang Z, Swem LR, Rushing BG, Devanathan S, Tollin G, Bauer CE. 1999. Bacterial photoreceptor with similarity to photoactive yellow protein and plant phytochromes. Science 285:406-9 (Pubitemid 29343962)
    • (1999) Science , vol.285 , Issue.5426 , pp. 406-409
    • Jiang, Z.1    Swem, L.R.2    Rushing, B.C.3    Devanathan, S.4    Tollin, G.5    Bauer, C.E.6
  • 57
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley LA, Sternberg MJ. 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protocols 4:363-71
    • (2009) Nat. Protocols , vol.4 , pp. 363-71
    • Kelley, L.A.1    Sternberg, M.J.2
  • 58
    • 33947412138 scopus 로고    scopus 로고
    • Structure of the redox sensor domain of Azotobacter vinelandii NifL at atomic resolution: Signaling, dimerization, and mechanism
    • DOI 10.1021/bi0620407
    • Key J,Hefti M, Purcell EB, Moffat K. 2007. Structure of the redox sensor domain of Azotobacter vinelandii NifL at atomic resolution: signaling, dimerization, and mechanism. Biochemistry 46:3614-23 (Pubitemid 46493462)
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3614-3623
    • Key, J.1    Hefti, M.2    Purcell, E.B.3    Moffat, K.4
  • 59
    • 15444362702 scopus 로고    scopus 로고
    • Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling
    • DOI 10.1021/bi047942r
    • Key J, Moffat K. 2005. Crystal structures of deoxy and CO-bound bjFixLH reveal details of ligand recognition and signaling. Biochemistry 44:4627-35 (Pubitemid 40396741)
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4627-4635
    • Key, J.1    Moffat, K.2
  • 61
    • 78651257345 scopus 로고    scopus 로고
    • Structural characterization of the multi-domain regulatory protein Rv1364c from Mycobacterium tuberculosis
    • King-Scott J, Konarev PV, Panjikar S, Jordanova R, Svergun DI, Tucker PA. 2010. Structural characterization of the multi-domain regulatory protein Rv1364c from Mycobacterium tuberculosis. Structure 19:56-69
    • (2010) Structure , vol.19 , pp. 56-69
    • King-Scott, J.1    Konarev, P.V.2    Panjikar, S.3    Jordanova, R.4    Svergun, D.I.5    Tucker, P.A.6
  • 62
    • 34249785673 scopus 로고    scopus 로고
    • 4-dicarboxylate- or citrate-specific sensor
    • DOI 10.1128/JB.00168-07
    • Kramer J, Fischer JD, Zientz E, Vijayan V, Griesinger C, et al. 2007. Citrate sensing by the C4- dicarboxylate/citrate sensor kinase DcuS of Escherichia coli: binding site and conversion of DcuS to a C4-dicarboxylate- or citrate-specific sensor. J. Bacteriol. 189:4290-98 (Pubitemid 46847377)
    • (2007) Journal of Bacteriology , vol.189 , Issue.11 , pp. 4290-4298
    • Kramer, J.1    Fischer, J.D.2    Zientz, E.3    Vijayan, V.4    Griesinger, C.5    Lupas, A.6    Unden, G.7
  • 63
    • 72249087161 scopus 로고    scopus 로고
    • Distribution and phylogeny of lightoxygen- voltage-blue-light-signaling proteins in the three kingdoms of life
    • Krauss U, Minh BQ, Losi A, Gärtner W, Eggert T, et al. 2009. Distribution and phylogeny of lightoxygen- voltage-blue-light-signaling proteins in the three kingdoms of life. J. Bacteriol. 191:7234-42
    • (2009) J. Bacteriol. , vol.191 , pp. 7234-42
    • Krauss, U.1    Minh, B.Q.2    Losi, A.3    Gärtner, W.4    Eggert, T.5
  • 65
    • 78049526111 scopus 로고    scopus 로고
    • The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway
    • Kreutel S, Kuhn A, Kiefer D. 2010. The photosensor protein Ppr of Rhodocista centenaria is linked to the chemotaxis signalling pathway. BMC Microbiol. 10:281
    • (2010) BMC Microbiol. , vol.10 , pp. 281
    • Kreutel, S.1    Kuhn, A.2    Kiefer, D.3
  • 67
    • 78249236863 scopus 로고    scopus 로고
    • Sensing of environmental signals: Classification of chemoreceptors according to the size of their ligand binding regions
    • Lacal J, Garcia-Fontana C, Munoz-Martinez F, Ramos J-L, Krell T. 2010. Sensing of environmental signals: classification of chemoreceptors according to the size of their ligand binding regions. Environ. Microbiol. 12:2873-84
    • (2010) Environ. Microbiol. , vol.12 , pp. 2873-84
    • Lacal, J.1    Garcia-Fontana, C.2    Munoz-Martinez, F.3    Ramos, J.-L.4    Krell, T.5
  • 69
    • 1842582674 scopus 로고    scopus 로고
    • Increased transcription of a potential sigma factor regulatory gene Rv1364c in Mycobacterium bovis BCG while residing in macrophages indicates use of alternative promoters
    • DOI 10.1016/j.femsle.2004.02.028, PII S0378109704001715
    • Li MS, Waddell SJ, Monahan IM, Mangan JA, Martin SL, et al. 2004. Increased transcription of a potential sigma factor regulatory gene Rv1364c in Mycobacterium bovisBCGwhile residing in macrophages indicates use of alternative promoters. FEMS Microbiol. Lett. 233:333-39 (Pubitemid 38452637)
    • (2004) FEMS Microbiology Letters , vol.233 , Issue.2 , pp. 333-339
    • Li, M.-S.1    Waddell, S.J.2    Monahan, I.M.3    Mangan, J.A.4    Martin, S.L.5    Everett, M.J.6    Butcher, P.D.7
  • 70
    • 32544442373 scopus 로고    scopus 로고
    • Role of the central region of NifL in conformational switches that regulate nitrogen fixation
    • DOI 10.1042/BST0340162
    • Little R, Martinez-Argudo I, Dixon R. 2006. Role of the central region of NifL in conformational switches that regulate nitrogen fixation. Biochem. Soc. Trans. 34:162-64 (Pubitemid 43235561)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.1 , pp. 162-164
    • Little, R.1    Martinez-Argudo, I.2    Dixon, R.3
  • 71
    • 33646231481 scopus 로고    scopus 로고
    • Characterization of a ctype heme-containing PAS sensor domain from Geobacter sulfurreducens representing a novel family of periplasmic sensors in Geobacteraceae and other bacteria
    • Londer YY, Dementieva IS, D'Ausilio CA, Pokkuluri PR, Schiffer M. 2006. Characterization of a ctype heme-containing PAS sensor domain from Geobacter sulfurreducens representing a novel family of periplasmic sensors in Geobacteraceae and other bacteria. FEMS Microbiol. Lett. 258:173-81
    • (2006) FEMS Microbiol. Lett. , vol.258 , pp. 173-81
    • Londer, Y.Y.1    Dementieva, I.S.2    Dausilio, C.A.3    Pokkuluri, P.R.4    Schiffer, M.5
  • 72
    • 53749091743 scopus 로고    scopus 로고
    • Bacterial bilin- and flavin-binding photoreceptors
    • Losi A, Gärtner W. 2008. Bacterial bilin- and flavin-binding photoreceptors. Photochem. Photobiol. Sci. 7:1168-78
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 1168-78
    • Losi, A.1    Gärtner, W.2
  • 73
    • 38149078912 scopus 로고    scopus 로고
    • PAS-mediated dimerization of soluble guanylyl cyclase revealed by signal transduction histidine kinase domain crystal structure
    • Ma X, Sayed N, Baskaran P, Beuve A, van den Akker F. 2008. PAS-mediated dimerization of soluble guanylyl cyclase revealed by signal transduction histidine kinase domain crystal structure. J. Biol. Chem. 283:1167-78
    • (2008) J. Biol. Chem. , vol.283 , pp. 1167-78
    • Ma, X.1    Sayed, N.2    Baskaran, P.3    Beuve, A.4    Van Den Akker, F.5
  • 76
    • 0022430790 scopus 로고
    • Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila
    • Meyer TE. 1985. Isolation and characterization of soluble cytochromes, ferredoxins and other chromophoric proteins from the halophilic phototrophic bacterium Ectothiorhodospira halophila. Biochim. Biophys. Acta 806:175-83
    • (1985) Biochim. Biophys. Acta , vol.806 , pp. 175-83
    • Meyer, T.E.1
  • 77
    • 67649746308 scopus 로고    scopus 로고
    • Crystal structures of YkuI and its complex with second messenger cyclic Di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains
    • Minasov G, Padavattan S, Shuvalova L, Brunzelle JS, Miller DJ, et al. 2009. Crystal structures of YkuI and its complex with second messenger cyclic Di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains. J. Biol. Chem. 284:13174-84
    • (2009) J. Biol. Chem. , vol.284 , pp. 13174-84
    • Minasov, G.1    Padavattan, S.2    Shuvalova, L.3    Brunzelle, J.S.4    Miller, D.J.5
  • 78
    • 0034636982 scopus 로고    scopus 로고
    • Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: Crystallographic, mutagenesis and resonance Raman spectroscopic studies
    • Miyatake H, MukaiM, Park SY, Adachi S, Tamura K, et al. 2000. Sensory mechanism of oxygen sensor FixL from Rhizobium meliloti: crystallographic, mutagenesis and resonance Raman spectroscopic studies. J. Mol. Biol. 301:415-31
    • (2000) J. Mol. Biol. , vol.301 , pp. 415-31
    • Miyatake, H.1    Mukai, M.2    Park, S.Y.3    Adachi, S.4    Tamura, K.5
  • 79
    • 70349777587 scopus 로고    scopus 로고
    • Structure and signaling mechanism of Per-ARNT-Sim domains
    • Mö glich A, Ayers RA, Moffat K. 2009. Structure and signaling mechanism of Per-ARNT-Sim domains. Structure 17:1282-94
    • (2009) Structure , vol.17 , pp. 1282-94
    • Möglich, A.1    Ayers, R.A.2    Moffat, K.3
  • 80
    • 78650885619 scopus 로고    scopus 로고
    • Engineered photoreceptors as novel optogenetic tools
    • Möglich A, Moffat K. 2010. Engineered photoreceptors as novel optogenetic tools. Photochem. Photobiol. Sci. 9:1286-300
    • (2010) Photochem. Photobiol. Sci. , vol.9 , pp. 1286-300
    • Möglich, A.1    Moffat, K.2
  • 82
  • 83
    • 50849131895 scopus 로고    scopus 로고
    • Mutant screen distinguishes between residues necessary for light-signal perception and signal transfer by phytochrome B
    • Oka Y, Matsushita T, Mochizuki N, Quail PH, Nagatani A. 2008. Mutant screen distinguishes between residues necessary for light-signal perception and signal transfer by phytochrome B. PLoS Genet. 4:e1000158
    • (2008) PLoS Genet. , vol.4
    • Oka, Y.1    Matsushita, T.2    Mochizuki, N.3    Quail, P.H.4    Nagatani, A.5
  • 85
    • 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)
    • DOI 10.1021/bi035980p
    • Park H, Suquet C, Satterlee JD, Kang C. 2004. 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 43:2738-46 (Pubitemid 38327805)
    • (2004) Biochemistry , vol.43 , Issue.10 , pp. 2738-2746
    • Park, H.1    Suquet, C.2    Satterlee, J.D.3    Kang, C.4
  • 86
    • 0027243652 scopus 로고
    • Signal transduction schemes of bacteria
    • DOI 10.1016/0092-8674(93)90267-T
    • Parkinson JS. 1993. Signal transduction schemes of bacteria. Cell 73:857-71 (Pubitemid 23165604)
    • (1993) Cell , vol.73 , Issue.5 , pp. 857-871
    • Parkinson, J.S.1
  • 87
    • 0032568630 scopus 로고    scopus 로고
    • Photoactive yellow protein: A structural prototype for the three-dimensional fold of the PAS domain superfamily
    • Pellequer JL, Wager-Smith KA, Kay SA, Getzoff ED. 1998. Photoactive yellow protein: a structural prototype for the three-dimensional fold of the PAS domain superfamily. Proc. Natl. Acad. Sci. USA 95:5884-90
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5884-90
    • Pellequer, J.L.1    Wager-Smith, K.A.2    Kay, S.A.3    Getzoff, E.D.4
  • 88
    • 78149272906 scopus 로고    scopus 로고
    • Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain
    • Philip AF, Kumauchi M, Hoff WD. 2010. Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain. Proc. Natl. Acad. Sci. USA 107:17986-91
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17986-91
    • Philip, A.F.1    Kumauchi, M.2    Hoff, W.D.3
  • 89
    • 40949155089 scopus 로고    scopus 로고
    • Structures and solution properties of two novel periplasmic sensor domains with c-type heme from chemotaxis proteins of Geobacter sulfurreducens: Implications for signal transduction
    • Pokkuluri PR, Pessanha M, Londer YY, Wood SJ, Duke NE, et al. 2008. Structures and solution properties of two novel periplasmic sensor domains with c-type heme from chemotaxis proteins of Geobacter sulfurreducens: implications for signal transduction. J. Mol. Biol. 377:1498-517
    • (2008) J. Mol. Biol. , vol.377 , pp. 1498-517
    • Pokkuluri, P.R.1    Pessanha, M.2    Londer, Y.Y.3    Wood, S.J.4    Duke, N.E.5
  • 90
    • 38849124779 scopus 로고    scopus 로고
    • The Salmonellae PhoQ sensor: Mechanisms of detection of phagosome signals
    • DOI 10.1111/j.1462-5822.2007.01111.x
    • Prost LR, Miller SI. 2008. The Salmonellae PhoQ sensor:mechanisms of detection of phagosome signals. Cell Microbiol. 10:576-82 (Pubitemid 351194087)
    • (2008) Cellular Microbiology , vol.10 , Issue.3 , pp. 576-582
    • Prost, L.R.1    Miller, S.I.2
  • 91
    • 77955247454 scopus 로고    scopus 로고
    • An analysis of the solution structure and signaling mechanism of LovK, a sensor histidine kinase integrating light and redox signals
    • Purcell EB, McDonald CA, Palfey BA, Crosson S. 2010. An analysis of the solution structure and signaling mechanism of LovK, a sensor histidine kinase integrating light and redox signals. Biochemistry 49:6761-70
    • (2010) Biochemistry , vol.49 , pp. 6761-70
    • Purcell, E.B.1    McDonald, C.A.2    Palfey, B.A.3    Crosson, S.4
  • 93
    • 70350501347 scopus 로고    scopus 로고
    • A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 from Acetobacter xylinum
    • Qi Y, Rao F, Luo Z, Liang Z-X. 2009. A flavin cofactor-binding PAS domain regulates c-di-GMP synthesis in AxDGC2 from Acetobacter xylinum. Biochemistry 48:10275-85
    • (2009) Biochemistry , vol.48 , pp. 10275-85
    • Qi, Y.1    Rao, F.2    Luo, Z.3    Liang, Z.-X.4
  • 95
    • 0141643091 scopus 로고    scopus 로고
    • The structure of the periplasmic ligand-binding domain of the sensor kinase CitA reveals the first extracellular pas domain
    • DOI 10.1074/jbc.M305864200
    • Reinelt S, Hofmann E, Gerharz T, BottM,Madden DR. 2003. The structure of the periplasmic ligandbinding domain of the sensor kinase CitA reveals the first extracellular PAS domain. J. Biol. Chem. 278:39189-96 (Pubitemid 37221822)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.40 , pp. 39189-39196
    • Reinelt, S.1    Hofmann, E.2    Gerharz, T.3    Bott, M.4    Madden, D.R.5
  • 96
    • 76449108491 scopus 로고    scopus 로고
    • FixK, a global regulator of microaerobic growth, controls photosynthesis in Rhodopseudomonas palustris
    • Rey FE, Harwood CS. 2010. FixK, a global regulator of microaerobic growth, controls photosynthesis in Rhodopseudomonas palustris. Mol. Microbiol. 75:1007-20
    • (2010) Mol. Microbiol. , vol.75 , pp. 1007-20
    • Rey, F.E.1    Harwood, C.S.2
  • 97
    • 0026743174 scopus 로고
    • Multiple protein sequence alignment from tertiary structure comparison: Assignment of global and residue confidence levels
    • Russell RB, Barton GJ. 1992. Multiple protein sequence alignment from tertiary structure comparison: assignment of global and residue confidence levels. Proteins 14:309-23
    • (1992) Proteins , vol.14 , pp. 309-23
    • Russell, R.B.1    Barton, G.J.2
  • 98
    • 0034622586 scopus 로고    scopus 로고
    • Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin
    • DOI 10.1021/bi000585+
    • SalomonM,Christie JM, KniebE,Lempert U, BriggsWR.2000. Photochemical andmutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin. Biochemistry 39:9401-10 (Pubitemid 30626330)
    • (2000) Biochemistry , vol.39 , Issue.31 , pp. 9401-9410
    • Salomon, M.1    Christie, J.M.2    Knieb, E.3    Lempert, U.4    Briggs, W.R.5
  • 101
    • 0031921952 scopus 로고    scopus 로고
    • The redox- and fixed nitrogen-responsive regulatory protein NIFL from Azotobacter vinelandii comprises discrete flavin and nucleotide-binding domains
    • DOI 10.1046/j.1365-2958.1998.00788.x
    • Soderback E, Reyes-Ramirez F, Eydmann T, Austin S, Hill S, Dixon R. 1998. The redox- and fixed nitrogen-responsive regulatory protein NIFL from Azotobacter vinelandii comprises discrete flavin and nucleotide-binding domains. Mol. Microbiol. 28:179-92 (Pubitemid 28160123)
    • (1998) Molecular Microbiology , vol.28 , Issue.1 , pp. 179-192
    • Soderback, E.1    Reyes-Ramirez, F.2    Eydmann, T.3    Austin, S.4    Hill, S.5    Dixon, R.6
  • 102
    • 0027324441 scopus 로고
    • The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein
    • Sprenger WW, Hoff WD, Armitage JP, Hellingwerf KJ. 1993. The eubacterium Ectothiorhodospira halophila is negatively phototactic, with a wavelength dependence that fits the absorption spectrum of the photoactive yellow protein. J. Bacteriol. 175:3096-104 (Pubitemid 23148746)
    • (1993) Journal of Bacteriology , vol.175 , Issue.10 , pp. 3096-3104
    • Sprenger, W.W.1    Hoff, W.D.2    Armitage, J.P.3    Hellingwerf, K.J.4
  • 103
    • 0000984679 scopus 로고
    • Recent developments in carbon transport and metabolism in symbiotic systems
    • Streeter JG. 1995. Recent developments in carbon transport and metabolism in symbiotic systems. Symbiosis 19:175-96
    • (1995) Symbiosis , vol.19 , pp. 175-96
    • Streeter, J.G.1
  • 105
    • 34547137430 scopus 로고    scopus 로고
    • 95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP
    • DOI 10.1074/jbc.M701920200
    • Tanaka A, Takahashi H, Shimizu T. 2007. Critical role of the heme axial ligand, Met95, in locking catalysis of the phosphodiesterase from Escherichia coli (Ec DOS) toward cyclic diGMP. J. Biol. Chem. 282:21301-7 (Pubitemid 47099927)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.29 , pp. 21301-21307
    • Tanaka, A.1    Takahashi, H.2    Shimizu, T.3
  • 106
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor BL, Zhulin IB. 1999. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 63:479-506 (Pubitemid 29264980)
    • (1999) Microbiology and Molecular Biology Reviews , vol.63 , Issue.2 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 107
    • 0032694979 scopus 로고    scopus 로고
    • Aerotaxis and other energy-sensing behavior in bacteria
    • DOI 10.1146/annurev.micro.53.1.103
    • Taylor BL, Zhulin IB, Johnson MS. 1999. Aerotaxis and other energy-sensing behavior in bacteria. Annu. Rev. Microbiol. 53:103-28 (Pubitemid 29503727)
    • (1999) Annual Review of Microbiology , vol.53 , pp. 103-128
    • Taylor, B.L.1    Zhulin, I.B.2    Johnson, M.S.3
  • 108
    • 70350047301 scopus 로고    scopus 로고
    • An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control
    • Tuckerman JR, Gonzalez G, Sousa EH, Wan X, Saito JA, et al. 2009. An oxygen-sensing diguanylate cyclase and phosphodiesterase couple for c-di-GMP control. Biochemistry 48:9764-74
    • (2009) Biochemistry , vol.48 , pp. 9764-74
    • Tuckerman, J.R.1    Gonzalez, G.2    Sousa, E.H.3    Wan, X.4    Saito, J.A.5
  • 109
    • 33748650790 scopus 로고    scopus 로고
    • Biochemical characterization of MmoS, a sensor protein involved in copper-dependent regulation of soluble methane monooxygenase
    • DOI 10.1021/bi060693h
    • Ukaegbu UE,Henery S, Rosenzweig AC. 2006. Biochemical characterization ofMmoS, a sensor protein involved in copper-dependent regulation of soluble methane monooxygenase. Biochemistry 45:10191-98 (Pubitemid 44384794)
    • (2006) Biochemistry , vol.45 , Issue.34 , pp. 10191-10198
    • Ukaegbu, U.E.1    Henery, S.2    Rosenzweig, A.C.3
  • 110
    • 64349123371 scopus 로고    scopus 로고
    • Structure of the redox sensor domain of Methylococcus capsulatus (Bath) MmoS
    • Ukaegbu UE, Rosenzweig AC. 2009. Structure of the redox sensor domain of Methylococcus capsulatus (Bath) MmoS. Biochemistry 48:2207-15
    • (2009) Biochemistry , vol.48 , pp. 2207-15
    • Ukaegbu, U.E.1    Rosenzweig, A.C.2
  • 111
    • 12944325784 scopus 로고    scopus 로고
    • One-component systems dominate signal transduction in prokaryotes
    • DOI 10.1016/j.tim.2004.12.006, PII S0966842X04002720
    • Ulrich LE, Koonin EV, Zhulin IB. 2005. One-component systems dominate signal transduction in prokaryotes. Trends Microbiol. 13:52-56 (Pubitemid 40174862)
    • (2005) Trends in Microbiology , vol.13 , Issue.2 , pp. 52-56
    • Ulrich, L.E.1    Koonin, E.V.2    Zhulin, I.B.3
  • 112
    • 36248934750 scopus 로고    scopus 로고
    • Photosensing in chemotrophic, non-phototrophic bacteria: Let thlre be light sensing too
    • DOI 10.1016/j.tim.2007.09.009, PII S0966842X07002041
    • van der Horst MA, Key J, Hellingwerf KJ. 2007. Photosensing in chemotrophic, non-phototrophic bacteria: let there be light sensing too. Trends Microbiol. 15:554-62 (Pubitemid 350137737)
    • (2007) Trends in Microbiology , vol.15 , Issue.12 , pp. 554-562
    • Van Der Horst, M.A.1    Key, J.2    Hellingwerf, K.J.3
  • 114
    • 0029046744 scopus 로고
    • An assessment of amino acid exchange matrices in aligning protein sequences: The twilight zone revisited
    • Vogt G, Etzold T, Argos P. 1995. An assessment of amino acid exchange matrices in aligning protein sequences: the twilight zone revisited. J. Mol. Biol. 249:816-31
    • (1995) J. Mol. Biol. , vol.249 , pp. 816-831
    • Vogt, G.1    Etzold, T.2    Argos, P.3
  • 115
    • 59649088255 scopus 로고    scopus 로고
    • Crystal structure of the IrrE protein, a central regulator of DNA damage repair in Deinococcaceae
    • Vujicic-Zagar A, Dulermo R, Le Gorrec M, Vannier F, Servant P, et al. 2009. Crystal structure of the IrrE protein, a central regulator of DNA damage repair in Deinococcaceae. J. Mol. Biol. 386:704-16
    • (2009) J. Mol. Biol. , vol.386 , pp. 704-16
    • Vujicic-Zagar, A.1    Dulermo, R.2    Le Gorrec, M.3    Vannier, F.4    Servant, P.5
  • 116
    • 76649086069 scopus 로고    scopus 로고
    • PASdomain containing chemoreceptor couples dynamic changes in metabolism with chemotaxis
    • XieZ,Ulrich LE, Zhulin IB,AlexandreG. 2010.PASdomain containing chemoreceptor couples dynamic changes in metabolism with chemotaxis. Proc. Natl. Acad. Sci. USA 107:2235-40
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 2235-40
    • Xie, Z.1    Ulrich, L.E.2    Zhulin, I.B.3    Alexandre, G.4
  • 117
    • 28044447426 scopus 로고    scopus 로고
    • Biophysical properties of a c-type heme in chemotaxis signal transducer protein DcrA
    • DOI 10.1021/bi0513352
    • Yoshioka S, Kobayashi K, Yoshimura H, Uchida T, Kitagawa T, Aono S. 2005. Biophysical properties of a c-type heme in chemotaxis signal transducer protein DcrA. Biochemistry 44:15406-13 (Pubitemid 41683135)
    • (2005) Biochemistry , vol.44 , Issue.46 , pp. 15406-15413
    • Yoshioka, S.1    Kobayashi, K.2    Yoshimura, H.3    Uchida, T.4    Kitagawa, T.5    Aono, S.6
  • 118
    • 52249108909 scopus 로고    scopus 로고
    • C4-dicarboxylates sensing mechanism revealed by the crystal structures of DctB sensor domain
    • Zhou Y-F, Nan B, Nan J, Ma Q, Panjikar S, et al. 2008. C4-dicarboxylates sensing mechanism revealed by the crystal structures of DctB sensor domain. J. Mol. Biol. 383:49-61
    • (2008) J. Mol. Biol. , vol.383 , pp. 49-61
    • Zhou, Y.-F.1    Nan, B.2    Nan, J.3    Ma, Q.4    Panjikar, S.5
  • 119
    • 78650901467 scopus 로고    scopus 로고
    • Tripping the light fantastic: Blue-light photoreceptors as examples of environmentally modulated protein-protein interactions
    • Zoltowski BD, Gardner KH. 2011. Tripping the light fantastic: blue-light photoreceptors as examples of environmentally modulated protein-protein interactions. Biochemistry 50:4-16
    • (2011) Biochemistry , vol.50 , pp. 4-16
    • Zoltowski, B.D.1    Gardner, K.H.2


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