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Volumn 471, Issue , 2010, Pages 115-123

Transmembrane Receptor Chimeras to Probe HAMP Domain Function

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATE CYCLASE; BACTERIAL PROTEIN; MEMBRANE PROTEIN; RECOMBINANT PROTEIN;

EID: 79952201046     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)71007-7     Document Type: Chapter
Times cited : (6)

References (13)
  • 1
    • 53849112614 scopus 로고    scopus 로고
    • Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor
    • Ames, P., Zhou, Q., Parkinson, J.S., Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor. J. Bacteriol. 190 (2008), 6676–6685.
    • (2008) J. Bacteriol. , vol.190 , pp. 6676-6685
    • Ames, P.1    Zhou, Q.2    Parkinson, J.S.3
  • 2
    • 34248371291 scopus 로고    scopus 로고
    • The signaling helix: A common functional theme in diverse signaling proteins
    • Anantharaman, V., Balaji, S., Aravind, L., The signaling helix: A common functional theme in diverse signaling proteins. Biol. Direct., 1, 2006, 25.
    • (2006) Biol. Direct. , vol.1 , pp. 25
    • Anantharaman, V.1    Balaji, S.2    Aravind, L.3
  • 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., Ponting, C.P., The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins. FEMS Microbiol. Lett. 176 (1999), 111–116.
    • (1999) FEMS Microbiol. Lett. , vol.176 , pp. 111-116
    • Aravind, L.1    Ponting, C.P.2
  • 4
    • 0025908814 scopus 로고
    • Signal transduction pathways involving protein phosphorylation in prokaryotes
    • Bourret, R.B., Borkovich, K.A., Simon, M.I., Signal transduction pathways involving protein phosphorylation in prokaryotes. Annu. Rev. Biochem. 60 (1991), 401–441.
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 401-441
    • Bourret, R.B.1    Borkovich, K.A.2    Simon, M.I.3
  • 5
    • 0035312774 scopus 로고    scopus 로고
    • Transmembrane signaling in bacterial chemoreceptors
    • Falke, J.J., Hazelbauer, G.L., Transmembrane signaling in bacterial chemoreceptors. Trends Biochem. Sci. 26 (2001), 257–265.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 257-265
    • Falke, J.J.1    Hazelbauer, G.L.2
  • 6
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin, M.Y., Nikolskaya, A.N., Koonin, E.V., Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol. Lett. 203 (2001), 11–21.
    • (2001) FEMS Microbiol. Lett. , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 8
    • 84902405976 scopus 로고    scopus 로고
    • Regulation of porins in Escherichia coli by the osmosensing histidine kinase/phosphatase EnvZ
    • M. Inouye R. Dutta M. Inouye R. Dutta Academic Press, Inc. San Diego, CA
    • Inouye, M., Dutta, R., Zhu, Y., Regulation of porins in Escherichia coli by the osmosensing histidine kinase/phosphatase EnvZ. Inouye, M., Dutta, R., Inouye, M., Dutta, R., (eds.) Histidine Kinases in Signal Transduction, 2003, Academic Press, Inc., San Diego, CA, 25–46.
    • (2003) Histidine Kinases in Signal Transduction , pp. 25-46
    • Inouye, M.1    Dutta, R.2    Zhu, Y.3
  • 9
    • 0025793604 scopus 로고
    • Assay of adenylyl cyclase catalytic activity
    • Johnson, R.A., Salomon, Y., Assay of adenylyl cyclase catalytic activity. Methods Enzymol. 195 (1991), 3–21.
    • (1991) Methods Enzymol. , vol.195 , pp. 3-21
    • Johnson, R.A.1    Salomon, Y.2
  • 10
    • 3042516998 scopus 로고    scopus 로고
    • The effect of HAMP domains on class IIIb adenylyl cyclases from Mycobacterium tuberculosis
    • Linder, J.U., Hammer, A., Schultz, J.E., The effect of HAMP domains on class IIIb adenylyl cyclases from Mycobacterium tuberculosis. Eur. J. Biochem. 271 (2004), 2446–2451.
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2446-2451
    • Linder, J.U.1    Hammer, A.2    Schultz, J.E.3
  • 11
    • 0032826834 scopus 로고    scopus 로고
    • Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction
    • Williams, S.B., Stewart, V., Functional similarities among two-component sensors and methyl-accepting chemotaxis proteins suggest a role for linker region amphipathic helices in transmembrane signal transduction. Mol. Microbiol. 33 (1999), 1093–1102.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1093-1102
    • Williams, S.B.1    Stewart, V.2
  • 12
    • 70350163201 scopus 로고    scopus 로고
    • Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors
    • Zhou, Q., Ames, P., Parkinson, J.S., Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors. Mol. Microbiol. 73 (2009), 801–814.
    • (2009) Mol. Microbiol. , vol.73 , pp. 801-814
    • Zhou, Q.1    Ames, P.2    Parkinson, J.S.3
  • 13
    • 9144234840 scopus 로고    scopus 로고
    • The HAMP linker in histidine kinase dimeric receptors is critical for symmetric transmembrane signal transduction
    • Zhu, Y., Inouye, M., The HAMP linker in histidine kinase dimeric receptors is critical for symmetric transmembrane signal transduction. J. Biol. Chem. 279 (2004), 48152–48158.
    • (2004) J. Biol. Chem. , vol.279 , pp. 48152-48158
    • Zhu, Y.1    Inouye, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.