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Volumn 19, Issue 3, 2011, Pages 378-385

The mechanisms of HAMP-mediated signaling in transmembrane receptors

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; MEMBRANE RECEPTOR;

EID: 79952470482     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.01.006     Document Type: Article
Times cited : (82)

References (21)
  • 1
    • 77951643013 scopus 로고    scopus 로고
    • Structure of concatenated HAMP domains provides a mechanism for signal transduction
    • Airola, M.V., Watts, K.J., Bilwes, A.M., and Crane, B.R. (2010). Structure of concatenated HAMP domains provides a mechanism for signal transduction. Structure 18, 436-448.
    • (2010) Structure , vol.18 , pp. 436-448
    • Airola, M.V.1    Watts, K.J.2    Bilwes, A.M.3    Crane, B.R.4
  • 2
    • 0037216619 scopus 로고    scopus 로고
    • Mutational analysis of a conserved signal-transducing element: The HAMP linker of the Escherichia coli nitrate sensor NarX
    • DOI 10.1128/JB.185.1.89-97.2003
    • Appleman, J.A., and Stewart, V. (2003). Mutational analysis of a conserved signal-transducing element: the HAMP linker of the Escherichia coli nitrate sensor NarX. J. Bacteriol. 185, 89-97. (Pubitemid 36008825)
    • (2003) Journal of Bacteriology , vol.185 , Issue.1 , pp. 89-97
    • Appleman, J.A.1    Stewart, V.2
  • 3
    • 0032766134 scopus 로고    scopus 로고
    • The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins
    • Aravind, L., and Ponting, C.P. (1999). The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol. Lett. 176, 111-116.
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 4
    • 0028115617 scopus 로고
    • Transmembrane signalling by a hybrid protein: Communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor EnvZ
    • Baumgartner, J.W., Kim, C., Brissette, R.E., Inouye, M., Park, C., and Hazelbauer, G.L. (1994). Transmembrane signalling by a hybrid protein: communication from the domain of chemoreceptor Trg that recognizes sugar-binding proteins to the kinase/phosphatase domain of osmosensor EnvZ. J. Bacteriol. 176, 1157-1163. (Pubitemid 24060134)
    • (1994) Journal of Bacteriology , vol.176 , Issue.4 , pp. 1157-1163
    • Baumgartner, J.W.1    Kim, C.2    Brissette, R.E.3    Inouye, M.4    Park, C.5    Hazelbauer, G.L.6
  • 5
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • DOI 10.1023/A:1008392405740
    • Cornilescu, G., Delaglio, F., and Bax, A. (1999). Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13, 289-302. (Pubitemid 29143535)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 6
    • 0032694547 scopus 로고    scopus 로고
    • An efficient strategy for assignment of cross-peaks in 3D heteronuclear NOESY experiments
    • Diercks, T., Coles, M., and Kessler, H. (1999). An efficient strategy for assignment of cross-peaks in 3D heteronuclear NOESY experiments. J. Biomol. NMR 15, 177-180.
    • (1999) J. Biomol. NMR , vol.15 , pp. 177-180
    • Diercks, T.1    Coles, M.2    Kessler, H.3
  • 7
    • 77950492834 scopus 로고    scopus 로고
    • Comprehensive analysis of HAMP domains: Implications for transmembrane signal transduction
    • Dunin-Horkawicz, S., and Lupas, A.N. (2010a). Comprehensive analysis of HAMP domains: Implications for transmembrane signal transduction. J. Mol. Biol. 397, 1156-1174.
    • (2010) J. Mol. Biol. , vol.397 , pp. 1156-1174
    • Dunin-Horkawicz, S.1    Lupas, A.N.2
  • 8
    • 77951974524 scopus 로고    scopus 로고
    • Measuring the conformational space of square four-helical bundles with the program samCC
    • Dunin-Horkawicz, S., and Lupas, A.N. (2010b). Measuring the conformational space of square four-helical bundles with the program samCC. J. Struct. Biol. 170, 226-235.
    • (2010) J. Struct. Biol. , vol.170 , pp. 226-235
    • Dunin-Horkawicz, S.1    Lupas, A.N.2
  • 9
  • 10
    • 33748183257 scopus 로고    scopus 로고
    • The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling
    • DOI 10.1016/j.cell.2006.06.058, PII S0092867406010233
    • Hulko, M., Berndt, F., Gruber, M., Linder, J.U., Truffault, V., Schultz, A., Martin, J., Schultz, J.E., Lupas, A.N., and Coles, M. (2006). The HAMP domain structure implies helix rotation in transmembrane signaling. Cell 126, 929-940. (Pubitemid 44310780)
    • (2006) Cell , vol.126 , Issue.5 , pp. 929-940
    • Hulko, M.1    Berndt, F.2    Gruber, M.3    Linder, J.U.4    Truffault, V.5    Schultz, A.6    Martin, J.7    Schultz, J.E.8    Lupas, A.N.9    Coles, M.10
  • 11
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, A. (1993). Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, A.1
  • 12
    • 76249125189 scopus 로고    scopus 로고
    • Transmembrane signaling in chimeras of the Escherichia coli aspartate and serine chemotaxis receptors and bacterial class III adenylyl cyclases
    • Kanchan, K., Linder, J., Winkler, K., Hantke, K., Schultz, A., and Schultz, J.E. (2010). Transmembrane signaling in chimeras of the Escherichia coli aspartate and serine chemotaxis receptors and bacterial class III adenylyl cyclases. J. Biol. Chem. 285, 2090-2099.
    • (2010) J. Biol. Chem. , vol.285 , pp. 2090-2099
    • Kanchan, K.1    Linder, J.2    Winkler, K.3    Hantke, K.4    Schultz, A.5    Schultz, J.E.6
  • 13
    • 77957949467 scopus 로고    scopus 로고
    • Signaling mechanisms of HAMP domains in chemoreceptors and sensor kinases
    • Parkinson, J.S. (2010). Signaling mechanisms of HAMP domains in chemoreceptors and sensor kinases. Annu. Rev. Microbiol. 64, 101-122.
    • (2010) Annu. Rev. Microbiol. , vol.64 , pp. 101-122
    • Parkinson, J.S.1
  • 15
    • 36848998769 scopus 로고    scopus 로고
    • Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: A disulfide mapping study
    • DOI 10.1021/bi701832b
    • Swain, K.E., and Falke, J.J. (2007). Structure of the conserved HAMP domain in an intact, membrane-bound chemoreceptor: a disulfide mapping study. Biochemistry 46, 13684-13695. (Pubitemid 350223896)
    • (2007) Biochemistry , vol.46 , Issue.48 , pp. 13684-13695
    • Swain, K.E.1    Falke, J.J.2
  • 16
    • 0016374975 scopus 로고
    • Highly sensitive adenylate cyclase assay
    • Salomon, Y., Londos, C., and Rodbell, M. (1974). Highly sensitive adenylate cyclase assay. Anal. Biochem. 58, 541-548.
    • (1974) Anal. Biochem. , vol.58 , pp. 541-548
    • Salomon, Y.1    Londos, C.2    Rodbell, M.3
  • 17
    • 0026681093 scopus 로고
    • Transmembrane signal transduction and osmoregulation in Escherichia coli: Functional importance of the transmembrane regions of membrane-located protein kinase EnvZ
    • Tokyo
    • Tokishita, S., Kojima, A., and Mizuno, T. (1992). Transmembrane signal transduction and osmoregulation in Escherichia coli: functional importance of the transmembrane regions of membrane-located protein kinase EnvZ. J. Biochem. (Tokyo) 111, 707-713.
    • (1992) J. Biochem. , vol.111 , pp. 707-713
    • Tokishita, S.1    Kojima, A.2    Mizuno, T.3
  • 18
    • 0024462539 scopus 로고
    • Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate
    • Utsumi, R., Brissette, R.E., Rampersaud, A., Forst, S.A., Oosawa, K., and Inouye, M. (1989). Activation of bacterial porin gene expression by a chimeric signal transducer in response to aspartate. Science 245, 1246-1249. (Pubitemid 19238750)
    • (1989) Science , vol.245 , Issue.4923 , pp. 1246-1249
    • Utsumi, R.1    Brissette, R.E.2    Rampersaud, A.3    Forst, S.A.4    Oosawa, K.5    Inouye, M.6
  • 19
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A., and Teplyakov, A. (1997). MOLREP: an automated program for molecular replacement. J. Appl. Cryst. 30, 1022-1025.
    • (1997) J. Appl. Cryst. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 20
    • 40449120005 scopus 로고    scopus 로고
    • Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer
    • DOI 10.1128/JB.01858-07
    • Watts, K.J., Johnson, M.S., and Taylor, B.L. (2008). Structure-function relationships in the HAMP and proximal signaling domains of the aerotaxis receptor Aer. J. Bacteriol. 190, 2118-2127. (Pubitemid 351355335)
    • (2008) Journal of Bacteriology , vol.190 , Issue.6 , pp. 2118-2127
    • Watts, K.J.1    Johnson, M.S.2    Taylor, B.L.3
  • 21
    • 0031931506 scopus 로고    scopus 로고
    • Chimeric chemoreceptors in Escherichia coli: Signaling properties of Tar-Tap and Tap-Tar hybrids
    • Weerasuriya, S., Schneider, B.M., and Manson, M.D. (1998). Chimeric chemoreceptors in Escherichia coli: signaling properties of Tar-Tap and Tap-Tar hybrids. J. Bacteriol. 180, 914-920. (Pubitemid 28084218)
    • (1998) Journal of Bacteriology , vol.180 , Issue.4 , pp. 914-920
    • Weerasuriya, S.1    Schneider, B.M.2    Manson, M.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.