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Volumn 108, Issue 51, 2011, Pages 20467-20472

Systematic control of protein interaction using a modular ER/K α-helix linker

Author keywords

Cell signaling; Modulation; Systematic protein affinity strength

Indexed keywords

ARGININE; CALMODULIN; GLUTAMIC ACID; LYSINE;

EID: 84855513111     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1116066108     Document Type: Article
Times cited : (64)

References (31)
  • 2
    • 39749138785 scopus 로고    scopus 로고
    • A structural understanding of the dynamic ribosome machine
    • Steitz TA (2008) A structural understanding of the dynamic ribosome machine. Nat Rev Mol Cell Biol 9:242-253.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 242-253
    • Steitz, T.A.1
  • 3
    • 59749095198 scopus 로고    scopus 로고
    • Protein scaffolds in MAP kinase signalling
    • Brown MD, Sacks DB (2009) Protein scaffolds in MAP kinase signalling. Cell Signal 21:462-469.
    • (2009) Cell Signal , vol.21 , pp. 462-469
    • Brown, M.D.1    Sacks, D.B.2
  • 4
    • 0036441510 scopus 로고    scopus 로고
    • Autoinhibitory domains: Modular effectors of cellular regulation
    • DOI 10.1146/annurev.cellbio.18.031502.133614
    • Pufall MA, Graves BJ (2002) Autoinhibitory domains: Modular effectors of cellular regulation. Annu Rev Cell Dev Biol 18:421-462. (Pubitemid 35387357)
    • (2002) Annual Review of Cell and Developmental Biology , vol.18 , pp. 421-462
    • Pufall, M.A.1    Graves, B.J.2
  • 5
    • 0027122748 scopus 로고
    • Proteins. One thousand families for the molecular biologist
    • Chothia C (1992) Proteins. One thousand families for the molecular biologist. Nature 357:543-544.
    • (1992) Nature , vol.357 , pp. 543-544
    • Chothia, C.1
  • 6
    • 5044235050 scopus 로고    scopus 로고
    • Ten thousand interactions for the molecular biologist
    • DOI 10.1038/nbt1018
    • Aloy P, Russell RB (2004) Ten thousand interactions for the molecular biologist. Nat Biotechnol 22:1317-1321. (Pubitemid 39336787)
    • (2004) Nature Biotechnology , vol.22 , Issue.10 , pp. 1317-1321
    • Aloy, P.1    Russell, R.B.2
  • 7
    • 34247586171 scopus 로고    scopus 로고
    • Deciphering protein-protein interactions. Part II. Computational methods to predict protein and domain interaction partners
    • Shoemaker BA, Panchenko AR (2007) Deciphering protein-protein interactions. Part II. Computational methods to predict protein and domain interaction partners. PLoS Comput Biol 3:e43.
    • (2007) PLoS Comput Biol , vol.3
    • Shoemaker, B.A.1    Panchenko, A.R.2
  • 8
    • 34047202181 scopus 로고    scopus 로고
    • Deciphering protein-protein interactions. Part I. Experimental techniques and databases
    • Shoemaker BA, Panchenko AR (2007) Deciphering protein-protein interactions. Part I. Experimental techniques and databases. PLoS Comput Biol 3:e42.
    • (2007) PLoS Comput Biol , vol.3
    • Shoemaker, B.A.1    Panchenko, A.R.2
  • 10
    • 51649115555 scopus 로고    scopus 로고
    • Dynamic charge interactions create surprising rigidity in the ER/K alpha-helical protein motif
    • Sivaramakrishnan S, Spink BJ, Sim AY, Doniach S, Spudich JA (2008) Dynamic charge interactions create surprising rigidity in the ER/K alpha-helical protein motif. Proc Natl Acad Sci USA 105:13356-13361.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 13356-13361
    • Sivaramakrishnan, S.1    Spink, B.J.2    Sim, A.Y.3    Doniach, S.4    Spudich, J.A.5
  • 11
    • 72249096074 scopus 로고    scopus 로고
    • Combining single-molecule optical trapping and small-angle X-ray scattering measurements to compute the persistence length of a protein ER/K alpha-helix
    • Sivaramakrishnan S, et al. (2009) Combining single-molecule optical trapping and small-angle X-ray scattering measurements to compute the persistence length of a protein ER/K alpha-helix. Biophys J 97:2993-2999.
    • (2009) Biophys J , vol.97 , pp. 2993-2999
    • Sivaramakrishnan, S.1
  • 13
    • 34447297323 scopus 로고    scopus 로고
    • Energetics of protein folding
    • Baldwin RL (2007) Energetics of protein folding. J Mol Biol 371:283-301.
    • (2007) J Mol Biol , vol.371 , pp. 283-301
    • Baldwin, R.L.1
  • 14
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • DOI 10.1016/S0962-8924(00)01800-6, PII S0962892400018006
    • Chin D, Means AR (2000) Calmodulin: A prototypical calcium sensor. Trends Cell Biol 10:322-328. (Pubitemid 30445239)
    • (2000) Trends in Cell Biology , vol.10 , Issue.8 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 15
    • 0025159272 scopus 로고
    • How calmodulin binds its targets: Sequence independent recognition of amphiphilic alpha-helices
    • O'Neil KT, DeGrado WF (1990) How calmodulin binds its targets: Sequence independent recognition of amphiphilic alpha-helices. Trends Biochem Sci 15:59-64. (Pubitemid 20036857)
    • (1990) Trends in Biochemical Sciences , vol.15 , Issue.2 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 16
    • 70349304323 scopus 로고    scopus 로고
    • The structure and function of fluorescent proteins
    • Sample V, Newman RH, Zhang J (2009) The structure and function of fluorescent proteins. Chem Soc Rev 38:2852-2864.
    • (2009) Chem Soc Rev , vol.38 , pp. 2852-2864
    • Sample, V.1    Newman, R.H.2    Zhang, J.3
  • 17
    • 0034846540 scopus 로고    scopus 로고
    • Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy
    • Kenworthy AK (2001) Imaging protein-protein interactions using fluorescence resonance energy transfer microscopy. Methods 24:289-296.
    • (2001) Methods , vol.24 , pp. 289-296
    • Kenworthy, A.K.1
  • 18
    • 35348887075 scopus 로고    scopus 로고
    • FRET-based biosensors for protein kinases: Illuminating the kinome
    • DOI 10.1039/b706628g
    • Zhang J, Allen MD (2007) FRET-based biosensors for protein kinases: Illuminating the kinome. Mol Biosyst 3:759-765. (Pubitemid 47587185)
    • (2007) Molecular BioSystems , vol.3 , Issue.11 , pp. 759-765
    • Zhang, J.1    Allen, M.D.2
  • 20
    • 0034720711 scopus 로고    scopus 로고
    • Measurement of molecular interactions in living cells by fluorescence resonance energy transfer between variants of the green fluorescent protein
    • Siegel RM, et al. (2000) Measurement of molecular interactions in living cells by fluorescence resonance energy transfer between variants of the green fluorescent protein. Sci STKE 2000:lp1.
    • (2000) Sci STKE , vol.2000
    • Siegel, R.M.1
  • 22
    • 0015829989 scopus 로고
    • Principles of competitive binding assays (saturation analysis). 1. Equilibrium techniques
    • Zettner A (1973) Principles of competitive binding assays (saturation analysis). 1. Equilibrium techniques. Clin Chem 19:699-705.
    • (1973) Clin Chem , vol.19 , pp. 699-705
    • Zettner, A.1
  • 23
    • 0020541529 scopus 로고
    • Binding of hormones and neuropeptides by calmodulin
    • Malencik DA, Anderson SR (1983) Binding of hormones and neuropeptides by calmodulin. Biochemistry 22:1995-2001. (Pubitemid 13093465)
    • (1983) Biochemistry , vol.22 , Issue.8 , pp. 1995-2001
    • Malencik, D.A.1    Anderson, S.R.2
  • 24
    • 77954599241 scopus 로고    scopus 로고
    • Single-molecule dual-beam optical trap analysis of protein structure and function
    • Sung J, Sivaramakrishnan S, Dunn AR, Spudich JA (2010) Single-molecule dual-beam optical trap analysis of protein structure and function. Methods Enzymol 475:321-375.
    • (2010) Methods Enzymol , vol.475 , pp. 321-375
    • Sung, J.1    Sivaramakrishnan, S.2    Dunn, A.R.3    Spudich, J.A.4
  • 26
    • 0030610646 scopus 로고    scopus 로고
    • 2+ based on green fluorescent proteins and calmodulin
    • 2+ based on green fluorescent proteins and calmodulin. Nature 388:882-887.
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1
  • 27
    • 79951981589 scopus 로고    scopus 로고
    • Spatiotemporal regulation of small GTPases as revealed by probes based on the principle of Forster Resonance Energy Transfer (FRET): Implications for signaling and pharmacology
    • Kiyokawa E, Aoki K, Nakamura T, Matsuda M (2011) Spatiotemporal regulation of small GTPases as revealed by probes based on the principle of Forster Resonance Energy Transfer (FRET): Implications for signaling and pharmacology. Annu Rev Pharmacol Toxicol 51:337-358.
    • (2011) Annu Rev Pharmacol Toxicol , vol.51 , pp. 337-358
    • Kiyokawa, E.1    Aoki, K.2    Nakamura, T.3    Matsuda, M.4
  • 28
    • 0037780971 scopus 로고    scopus 로고
    • A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C
    • DOI 10.1083/jcb.200302125
    • Violin JD, Zhang J, Tsien RY, Newton AC (2003) A genetically encoded fluorescent reporter reveals oscillatory phosphorylation by protein kinase C. J Cell Biol 161:899-909. (Pubitemid 36718423)
    • (2003) Journal of Cell Biology , vol.161 , Issue.5 , pp. 899-909
    • Violin, J.D.1    Zhang, J.2    Tsien, R.Y.3    Newton, A.C.4
  • 29
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein
    • DOI 10.1016/S0076-6879(00)27297-2
    • Miyawaki A, Tsien RY (2000) Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescent protein. Methods Enzymol 327:472-500. (Pubitemid 34193328)
    • (2000) Methods in Enzymology , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.