메뉴 건너뛰기




Volumn 39, Issue 1, 2006, Pages 37-43

Structure-function relationships of EcDOS, a heme-regulated phosphodiesterase from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

HEMOPROTEIN; PHOSPHODIESTERASE;

EID: 33344477903     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar0501525     Document Type: Article
Times cited : (69)

References (65)
  • 1
    • 10444268892 scopus 로고    scopus 로고
    • Heme-based sensors: Defining characteristics, recent developments, and regulatory hypotheses
    • Gilles-Gonzalez, M. A.; Gonzalez, G. Heme-based sensors: defining characteristics, recent developments, and regulatory hypotheses. J. Inorg. Biochem. 2005, 99, 1-22.
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 1-22
    • Gilles-Gonzalez, M.A.1    Gonzalez, G.2
  • 2
    • 24344498616 scopus 로고    scopus 로고
    • Mechanism for Transduction of the Ligand-Binding Signal in Heme-Based Gas Sensory Proteins Revealed by Resonance Raman Spectroscopy
    • Uchida, T.; Kitagawa, T. Mechanism for Transduction of the Ligand-Binding Signal in Heme-Based Gas Sensory Proteins Revealed by Resonance Raman Spectroscopy. Acc. Chem. Res. 2005, 38 (8), 662-670.
    • (2005) Acc. Chem. Res. , vol.38 , Issue.8 , pp. 662-670
    • Uchida, T.1    Kitagawa, T.2
  • 4
    • 0000021902 scopus 로고    scopus 로고
    • T. Heme/Copper Terminal Oxidases
    • Ferguson-Miller, S.; Babcock, G. T. Heme/Copper Terminal Oxidases. Chem. Rev. 1996, 96, 2889-2908.
    • (1996) Chem. Rev. , vol.96 , pp. 2889-2908
    • Ferguson-Miller, S.1    Babcock, G.2
  • 5
    • 0022653364 scopus 로고
    • Product of per locus of Drosophila shares homology with proteoglycans
    • Jackson, F. R.; Bargiello, T. A.; Yun, S. H.; Young, M. W. Product of per locus of Drosophila shares homology with proteoglycans. Nature 1986, 320, 185-188.
    • (1986) Nature , vol.320 , pp. 185-188
    • Jackson, F.R.1    Bargiello, T.A.2    Yun, S.H.3    Young, M.W.4
  • 6
    • 0027403810 scopus 로고
    • Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor
    • Whitelaw, M.; Pongratz, I.; Wilhelmsson, A.; Gustafsson, J. A.; Poellinger, L. Ligand-dependent recruitment of the Arnt coregulator determines DNA recognition by the dioxin receptor. Mol. Cell. Biol. 1993, 13, 2504-2514.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 2504-2514
    • Whitelaw, M.1    Pongratz, I.2    Wilhelmsson, A.3    Gustafsson, J.A.4    Poellinger, L.5
  • 7
    • 0026314893 scopus 로고
    • The Drosophila single-minded gene encodes a helix-loop-helix protein that acts as a master regulator of CNS midline development
    • Nambu, J. R.; Lewis, J. O.; Wharton, K. A., Jr.; Crews, S. T. The Drosophila single-minded gene encodes a helix-loop-helix protein that acts as a master regulator of CNS midline development. Cell 1991, 67, 1157-1167.
    • (1991) Cell , vol.67 , pp. 1157-1167
    • Nambu, J.R.1    Lewis, J.O.2    Wharton Jr., K.A.3    Crews, S.T.4
  • 8
    • 0032990441 scopus 로고    scopus 로고
    • PAS domains: Internal sensors of oxygen, redox potential, and light
    • Taylor, B. L.; Zhulin, I. B. PAS domains: internal sensors of oxygen, redox potential, and light. Microbiol. Mol. Biol. Rev. 1999, 63, 479-506.
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 479-506
    • Taylor, B.L.1    Zhulin, I.B.2
  • 9
    • 0025878267 scopus 로고
    • A haemoprotein with kinase activity encoded by the oxygen sensor of Rhizobium meliloti
    • 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, 170-172.
    • (1991) Nature , vol.350 , pp. 170-172
    • Gilles-Gonzalez, M.A.1    Ditta, G.S.2    Helinski, D.R.3
  • 11
    • 1542297775 scopus 로고    scopus 로고
    • ADP reduces the oxygen-binding affinity of a sensory histidine kinase, FixL: The possibility of an enhanced reciprocating kinase reaction
    • Nakamura, H.; Kumita, H.; Imai, K.; Iizuka, T.; Shiro, Y. ADP reduces the oxygen-binding affinity of a sensory histidine kinase, FixL: the possibility of an enhanced reciprocating kinase reaction. Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 2742-2746.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2742-2746
    • Nakamura, H.1    Kumita, H.2    Imai, K.3    Iizuka, T.4    Shiro, Y.5
  • 14
    • 9444278384 scopus 로고    scopus 로고
    • Oxygen-sensing mechanism of HemAT from Bacillus subtilis: A resonance Raman spectroscopic study
    • Ohta, T.; Yoshimura, H.; Yoshioka, S.; Aono, S.; Kitagawa, T. Oxygen-sensing mechanism of HemAT from Bacillus subtilis: a resonance Raman spectroscopic study. J. Am. Chem. Soc. 2004, 126, 15000-15001.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 15000-15001
    • Ohta, T.1    Yoshimura, H.2    Yoshioka, S.3    Aono, S.4    Kitagawa, T.5
  • 15
    • 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
    • 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. J. Bacteriol. 1995, 177, 2157-2163.
    • (1995) J. Bacteriol. , vol.177 , pp. 2157-2163
    • Shelver, D.1    Kerby, R.L.2    He, Y.3    Roberts, G.P.4
  • 16
    • 0030597287 scopus 로고    scopus 로고
    • A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum
    • Aono, S.; Nakajima, H.; Saito, K.; Okada, M. A novel heme protein that acts as a carbon monoxide-dependent transcriptional activator in Rhodospirillum rubrum. Biochem. Biophys. Res. Commun. 1996, 228, 752-756.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 752-756
    • Aono, S.1    Nakajima, H.2    Saito, K.3    Okada, M.4
  • 17
    • 0344066227 scopus 로고    scopus 로고
    • Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA
    • Aono, S. Biochemical and biophysical properties of the CO-sensing transcriptional activator CooA. Acc. Chem. Res. 2003, 36, 825-831.
    • (2003) Acc. Chem. Res. , vol.36 , pp. 825-831
    • Aono, S.1
  • 20
    • 10044276844 scopus 로고    scopus 로고
    • NO activation of guanylyl cyclase
    • Russwurm, M.; Koesling, D. NO activation of guanylyl cyclase. EMBO J. 2004, 23, 4443-4450.
    • (2004) EMBO J. , vol.23 , pp. 4443-4450
    • Russwurm, M.1    Koesling, D.2
  • 21
    • 25144432064 scopus 로고    scopus 로고
    • A A molecular basis for NO selectivity in soluble guanylate cyclase
    • Boon, E. M.; Huang, S.H.; Marletta, M. A A molecular basis for NO selectivity in soluble guanylate cyclase. Nat. Chem. Biol. 2005, 1, 53-59.
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 53-59
    • Boon, E.M.1    Huang, S.H.2    Marletta, M.3
  • 22
    • 0034646392 scopus 로고    scopus 로고
    • Dos, a heme-binding PAS protein from Escherichia coli, is a direct oxygen sensor
    • 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, 2685-2691.
    • (2000) Biochemistry , vol.39 , pp. 2685-2691
    • Delgado-Nixon, V.M.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3
  • 23
    • 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.; Matsui, T.; Sagami, I.; Shimizu, T. 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. J. Biol. Chem. 2002, 277, 23821-23827.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23821-23827
    • Sasakura, Y.1    Hirata, S.2    Sugiyama, S.3    Suzuki, S.4    Taguchi, S.5    Watanabe, M.6    Matsui, T.7    Sagami, I.8    Shimizu, T.9
  • 24
    • 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
    • Sato, A.; Sasakura, Y.; Sugiyama, S.; Sagami, I.; Shimizu, T.; Mizutani, Y.; Kitagawa, T. 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. J. Biol. Chem. 2002, 277, 32650-32658.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32650-32658
    • Sato, A.1    Sasakura, Y.2    Sugiyama, S.3    Sagami, I.4    Shimizu, T.5    Mizutani, Y.6    Kitagawa, T.7
  • 25
    • 0036436657 scopus 로고    scopus 로고
    • Unusual cyanide bindings to a heme-regulated phosphodiesterase from Escherichia coli: Effect of Met95 mutations
    • Watanabe, M.; Matsui, T.; Sasakura, Y.; Sagami, I.; Shimizu, T. Unusual cyanide bindings to a heme-regulated phosphodiesterase from Escherichia coli: effect of Met95 mutations. Biochem. Biophys. Res. Commun. 2002, 299, 169-172.
    • (2002) Biochem. Biophys. Res. Commun. , vol.299 , pp. 169-172
    • Watanabe, M.1    Matsui, T.2    Sasakura, Y.3    Sagami, I.4    Shimizu, T.5
  • 26
    • 0346732270 scopus 로고    scopus 로고
    • Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: A study of deletion and site-directed mutants
    • Yoshimura, T.; Sagami, I.; Sasakura, Y.; Shimizu, T. Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: a study of deletion and site-directed mutants. J. Biol. Chem. 2003, 278, 53105-53111.
    • (2003) J. Biol. Chem. , vol.278 , pp. 53105-53111
    • Yoshimura, T.1    Sagami, I.2    Sasakura, Y.3    Shimizu, T.4
  • 27
    • 0344393534 scopus 로고    scopus 로고
    • Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli. Optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials
    • Hirata, S.; Matsui, T.; Sasakura, Y.; Sugiyama, S.; Yoshimura, T.; Sagami, I.; Shimizu, T. Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli. Optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials. Eur. J. Biochem. 2003, 270, 4771-4779.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4771-4779
    • Hirata, S.1    Matsui, T.2    Sasakura, Y.3    Sugiyama, S.4    Yoshimura, T.5    Sagami, I.6    Shimizu, T.7
  • 28
    • 4944244330 scopus 로고    scopus 로고
    • Critical roles of Asp40 at the haem proximal side of haem-regulated phosphodiesterase from Escherichia coli in redox potential, auto-oxidation and catalytic control
    • Watanabe, M.; Kurokawa, H.; Yoshimura-Suzuki, T.; Sagami, I.; Shimizu, T. Critical roles of Asp40 at the haem proximal side of haem-regulated phosphodiesterase from Escherichia coli in redox potential, auto-oxidation and catalytic control. Eur. J. Biochem. 2004, 271, 3937-3942.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 3937-3942
    • Watanabe, M.1    Kurokawa, H.2    Yoshimura-Suzuki, T.3    Sagami, I.4    Shimizu, T.5
  • 29
    • 2442624510 scopus 로고    scopus 로고
    • A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor
    • Kurokawa, H.; Lee, D. S.; Watanabe, M.; Sagami, I.; Mikami, B.; Raman, C. S.; Shimizu, T. A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor. J. Biol. Chem. 2004, 279, 20186-20193.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20186-20193
    • Kurokawa, H.1    Lee, D.S.2    Watanabe, M.3    Sagami, I.4    Mikami, B.5    Raman, C.S.6    Shimizu, T.7
  • 30
    • 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.; Sugiyama, S.; Sagami, I.; Shimizu, T. 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. J. Biol. Chem. 2004, 279, 3340-3347.
    • (2004) J. Biol. Chem. , vol.279 , pp. 3340-3347
    • Taguchi, S.1    Matsui, T.2    Igarashi, J.3    Sasakura, Y.4    Araki, Y.5    Ito, O.6    Sugiyama, S.7    Sagami, I.8    Shimizu, T.9
  • 31
    • 4644373192 scopus 로고    scopus 로고
    • Fluorescence Spectra of Trp53Phe and Trp110Ile Mutants of a Heme-regulated Phosphodiesterase from Escherichia coli
    • Hirata, S.; Hirofumi, K.; Sagami, I.; Shimizu, T. Fluorescence Spectra of Trp53Phe and Trp110Ile Mutants of a Heme-regulated Phosphodiesterase from Escherichia coli. Chem. Lett. 2004, 33, 870-871.
    • (2004) Chem. Lett. , vol.33 , pp. 870-871
    • Hirata, S.1    Hirofumi, K.2    Sagami, I.3    Shimizu, T.4
  • 32
    • 8644279707 scopus 로고    scopus 로고
    • Protein Microarray System for Detecting Protein-Protein Interactions Using an Anti-His-Tag Antibody and Fluorescence Scanning: Effects of the Heme Redox State on Protein-Protein Interactions of Heme-Regulated Phosphodiesterase from Escherichia coli
    • Sasakura, Y.; Kanda, K.; Yoshimura-Suzuki, T.; Matsui, T.; Fukuzono, S.; Han, M. H.; Shimizu, T. Protein Microarray System for Detecting Protein-Protein Interactions Using an Anti-His-Tag Antibody and Fluorescence Scanning: Effects of the Heme Redox State on Protein-Protein Interactions of Heme-Regulated Phosphodiesterase from Escherichia coli. Anal. Chem. 2004, 76, 6521-6527.
    • (2004) Anal. Chem. , vol.76 , pp. 6521-6527
    • Sasakura, Y.1    Kanda, K.2    Yoshimura-Suzuki, T.3    Matsui, T.4    Fukuzono, S.5    Han, M.H.6    Shimizu, T.7
  • 33
    • 22244440813 scopus 로고    scopus 로고
    • Investigation of the Relationship between Protein-Protein Interaction and Catalytic Activity of a Heme-Regulated Phosphodiesterase from Escherichia coli (Ec DOS) by Protein Microarray
    • Sasakura, Y.; Kanda, K.; Yoshimura-Suzuki, T.; Matsui, T.; Fukuzono, S.; Shimizu, T. Investigation of the Relationship between Protein-Protein Interaction and Catalytic Activity of a Heme-Regulated Phosphodiesterase from Escherichia coli (Ec DOS) by Protein Microarray. Biochemistry 2005, 44, 9598-9605.
    • (2005) Biochemistry , vol.44 , pp. 9598-9605
    • Sasakura, Y.1    Kanda, K.2    Yoshimura-Suzuki, T.3    Matsui, T.4    Fukuzono, S.5    Shimizu, T.6
  • 34
    • 25144498358 scopus 로고    scopus 로고
    • Ec DOS, a Heme-regulated Phosphodiesterase, Plays an Important Role in the Regulation of the cAMP
    • Yoshimura-Suzuki, T. Sagami, I., Yokota, N.; Kurokawa, H.; Shimizu, T. Ec DOS, a Heme-regulated Phosphodiesterase, Plays an Important Role in the Regulation of the cAMP. J. Bacteriol. 2005, 187, 6678-6682.
    • (2005) J. Bacteriol. , vol.187 , pp. 6678-6682
    • Yoshimura-Suzuki, T.1    Sagami, I.2    Yokota, N.3    Kurokawa, H.4    Shimizu, T.5
  • 35
    • 0029782887 scopus 로고    scopus 로고
    • Structural basis for ligand discrimination and response initiation in the heme-based oxygen sensor FixL
    • 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, 9539-9548.
    • (1996) Biochemistry , vol.35 , pp. 9539-9548
    • Rodgers, K.R.1    Lukat-Rodgers, G.S.2    Barron, J.A.3
  • 36
    • 0033120934 scopus 로고    scopus 로고
    • Heme-based sensors in biological systems
    • Rodgers, K. R. Heme-based sensors in biological systems. Curr. Opin. Chem. Biol. 1999, 3, 158-167.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 158-167
    • Rodgers, K.R.1
  • 37
    • 0023810222 scopus 로고
    • Heme enzyme crystal structures
    • Poulos, T. L. Heme enzyme crystal structures. Adv. Inorg. Biochem. 1988, 7, 1-36.
    • (1988) Adv. Inorg. Biochem. , vol.7 , pp. 1-36
    • Poulos, T.L.1
  • 39
    • 0029867916 scopus 로고    scopus 로고
    • Control of Myoglobin Electron-Transfer Rates by the Distal (Nonbound) Histidine Residue
    • Van Dyke, B. R.; Saltman, P.; Armstrong, F. A. Control of Myoglobin Electron-Transfer Rates by the Distal (Nonbound) Histidine Residue. J. Am. Chem. Soc. 1996, 118, 3490-3492.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 3490-3492
    • Van Dyke, B.R.1    Saltman, P.2    Armstrong, F.A.3
  • 40
    • 0021096850 scopus 로고
    • Oxidation-reduction properties of rat liver cytochromes P-450 and NADPH-cytochrome p-450 reductase related to catalysis in reconstituted systems
    • Guengerich, F. P. Oxidation-reduction properties of rat liver cytochromes P-450 and NADPH-cytochrome p-450 reductase related to catalysis in reconstituted systems. Biochemistry 1983, 22, 2811-2820.
    • (1983) Biochemistry , vol.22 , pp. 2811-2820
    • Guengerich, F.P.1
  • 41
    • 21844451590 scopus 로고    scopus 로고
    • The Ubiquitous Protein Domain EAL Is a Cyclic Diguanylate-Specific Phosphodiesterase: Enzymatically Active and Inactive EAL Domains
    • Schmidt, J.; Ryjenkov, D. A.; Gomelsky, M The Ubiquitous Protein Domain EAL Is a Cyclic Diguanylate-Specific Phosphodiesterase: Enzymatically Active and Inactive EAL Domains. J. Bacteriol. 2005, 187, 4774-4781.
    • (2005) J. Bacteriol. , vol.187 , pp. 4774-4781
    • Schmidt, J.1    Ryjenkov, D.A.2    Gomelsky, M.3
  • 44
    • 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)
    • 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, 2738-2746.
    • (2004) Biochemistry , vol.43 , pp. 2738-2746
    • Park, H.1    Suquet, C.2    Satterlee, J.D.3    Kang, C.4
  • 46
    • 0032497407 scopus 로고    scopus 로고
    • Structural changes in the heme proximal pocket induced by nitric oxide binding to soluble guanylate cyclase
    • Zhao, Y.; Hoganson, C.; Babcock, G. T.; Marletta, M. A. Structural changes in the heme proximal pocket induced by nitric oxide binding to soluble guanylate cyclase. Biochemistry 1998, 37, 12458-12464.
    • (1998) Biochemistry , vol.37 , pp. 12458-12464
    • Zhao, Y.1    Hoganson, C.2    Babcock, G.T.3    Marletta, M.A.4
  • 47
    • 0037205447 scopus 로고    scopus 로고
    • A ubiquitously expressed human hexacoordinate hemoglobin
    • Trent, J. T., III; Hargrove, M. S. A ubiquitously expressed human hexacoordinate hemoglobin. J. Biol. Chem. 2002, 277, 19538-19545.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19538-19545
    • Trent III, J.T.1    Hargrove, M.S.2
  • 48
    • 0029560867 scopus 로고
    • The ferrous heme of soluble guanylate cyclase: Formation of hexacoordinate complexes with carbon monoxide and nitrosomethane
    • Stone, J. R.; Marletta, M. A. The ferrous heme of soluble guanylate cyclase: formation of hexacoordinate complexes with carbon monoxide and nitrosomethane. Biochemistry 1995, 34, 16397-16403.
    • (1995) Biochemistry , vol.34 , pp. 16397-16403
    • Stone, J.R.1    Marletta, M.A.2
  • 49
    • 0028241788 scopus 로고
    • Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation
    • 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, 8067-8073.
    • (1994) Biochemistry , vol.33 , 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
  • 52
    • 0036774056 scopus 로고    scopus 로고
    • Structure and interactions of PAS kinase N-terminal PAS domain: Model for intramolecular kinase regulation
    • Amezcua, C. A.; Harper, S. M.; Rutter, J.; Gardner, K. H. Structure and interactions of PAS kinase N-terminal PAS domain: model for intramolecular kinase regulation. Structure (Cambridge) 2002, 10, 1349-1361.
    • (2002) Structure (Cambridge) , vol.10 , pp. 1349-1361
    • Amezcua, C.A.1    Harper, S.M.2    Rutter, J.3    Gardner, K.H.4
  • 53
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: Identification of signaling domains
    • Schultz, J.; Milpetz, F.; Bork, P.; Ponting, C. P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. U.S.A. 1998, 95, 5857-5864.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 54
    • 0037369966 scopus 로고    scopus 로고
    • The cyclic AMP-cyclic AMP receptor protein complex regulates activity of the traJ promoter of the Escherichia coli conjugative plasmid pRK100
    • Starcic, M.; Zgur-Bertok, D.; Jordi, B. J.; Wosten, M. M.; Gaastra, W.; van Putten, J. P. The cyclic AMP-cyclic AMP receptor protein complex regulates activity of the traJ promoter of the Escherichia coli conjugative plasmid pRK100. J. Bacteriol. 2003, 185, 1616-1623.
    • (2003) J. Bacteriol. , vol.185 , pp. 1616-1623
    • Starcic, M.1    Zgur-Bertok, D.2    Jordi, B.J.3    Wosten, M.M.4    Gaastra, W.5    Van Putten, J.P.6
  • 55
    • 0035839435 scopus 로고    scopus 로고
    • Intra-subunit and inter-subunit electron transfer in neuronal nitric-oxide synthase: Effect of calmodulin on heterodimer catalysis
    • Sagami, I.; Daff, S.; Shimizu, T. Intra-subunit and inter-subunit electron transfer in neuronal nitric-oxide synthase: effect of calmodulin on heterodimer catalysis. J. Biol. Chem. 2001, 276, 30036-30042.
    • (2001) J. Biol. Chem. , vol.276 , pp. 30036-30042
    • Sagami, I.1    Daff, S.2    Shimizu, T.3
  • 56
    • 0029815090 scopus 로고    scopus 로고
    • Identification of the cpdA gene encoding cyclic 3′,5′- adenosine monophosphate phosphodiesterase in Escherichia coli
    • Imamura, R.; Yamanaka, K.; Ogura, T.; Hiraga, S.; Fujita, N.; Ishihama, A.; Niki, H. Identification of the cpdA gene encoding cyclic 3′,5′-adenosine monophosphate phosphodiesterase in Escherichia coli. J. Biol. Chem. 1996, 271, 25423-25429.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25423-25429
    • Imamura, R.1    Yamanaka, K.2    Ogura, T.3    Hiraga, S.4    Fujita, N.5    Ishihama, A.6    Niki, H.7
  • 59
    • 2642554922 scopus 로고    scopus 로고
    • Bacterial signal transduction network in a genomic perspective
    • Galperin, M. Y. Bacterial signal transduction network in a genomic perspective. Environ. Microbiol. 2004, 6, 552-567.
    • (2004) Environ. Microbiol. , vol.6 , pp. 552-567
    • Galperin, M.Y.1
  • 60
    • 24744457756 scopus 로고    scopus 로고
    • Identification and characterization of a cyclic di-GMP specific phosphodiesterase and its allosteric control by GTP
    • Christen, M.; Christen, B.; Folcher, M.; Schauerte, A.; Jenal, U. Identification and characterization of a cyclic di-GMP specific phosphodiesterase and its allosteric control by GTP. J. Biol. Chem. 2005, 280, 30829-30837.
    • (2005) J. Biol. Chem. , vol.280 , pp. 30829-30837
    • Christen, M.1    Christen, B.2    Folcher, M.3    Schauerte, A.4    Jenal, U.5
  • 63
    • 1842610464 scopus 로고    scopus 로고
    • Cyclic di-guanosine-monophosphate comes of age: A novel secondary messenger involved in modulating cell surface structures in bacteria?
    • Jenal, U. Cyclic di-guanosine-monophosphate comes of age: a novel secondary messenger involved in modulating cell surface structures in bacteria? Curr. Opin. Microbiol. 2004, 7, 185-191.
    • (2004) Curr. Opin. Microbiol. , vol.7 , pp. 185-191
    • Jenal, U.1
  • 64
    • 4344688129 scopus 로고    scopus 로고
    • GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility
    • 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. Mol. Microbiol. 2004, 53, 1123-1134.
    • (2004) Mol. Microbiol. , vol.53 , pp. 1123-1134
    • Simm, R.1    Morr, M.2    Kader, A.3    Nimtz, M.4    Romling, U.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.