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Volumn 426, Issue 1, 2014, Pages 11-20

The extracellular protein VlsE is destabilized inside cells

Author keywords

extracellular protein; fast relaxation imaging (FReI); fluorescence resonance energy transfer (FRET); protein folding; variable major protein like sequence expressed (VlsE)

Indexed keywords

CELL SURFACE ANTIGEN VLSE; MEMBRANE ANTIGEN; UNCLASSIFIED DRUG;

EID: 84890856805     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.08.024     Document Type: Article
Times cited : (72)

References (33)
  • 1
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • C.M. Dobson Principles of protein folding, misfolding and aggregation Semin Cell Dev Biol 15 2004 3 16
    • (2004) Semin Cell Dev Biol , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 2
    • 33646557371 scopus 로고    scopus 로고
    • Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling
    • P. De Los Rios, A. Ben-Zvi, O. Slutsky, A. Azem, and P. Goloubinoff Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling Proc Natl Acad Sci 103 2006 6166 6171
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 6166-6171
    • De Los Rios, P.1    Ben-Zvi, A.2    Slutsky, O.3    Azem, A.4    Goloubinoff, P.5
  • 3
    • 0031239894 scopus 로고    scopus 로고
    • Molecular chaperones: Avoiding the crowd
    • R.J. Ellis Molecular chaperones: avoiding the crowd Curr Biol 7 1997 R531 R533
    • (1997) Curr Biol , vol.7
    • Ellis, R.J.1
  • 4
    • 0034487424 scopus 로고    scopus 로고
    • Roles of molecular chaperones in cytoplasmic protein folding
    • V.R. Agashe, and F.U. Hartl Roles of molecular chaperones in cytoplasmic protein folding Semin Cell Dev Biol 11 2000 15 25
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 15-25
    • Agashe, V.R.1    Hartl, F.U.2
  • 5
    • 77951643591 scopus 로고    scopus 로고
    • Protein folding stability and dynamics imaged in a living cell
    • S. Ebbinghaus, A. Dhar, J.D. McDonald, and M. Gruebele Protein folding stability and dynamics imaged in a living cell Nat Methods 7 2010 319 323
    • (2010) Nat Methods , vol.7 , pp. 319-323
    • Ebbinghaus, S.1    Dhar, A.2    McDonald, J.D.3    Gruebele, M.4
  • 7
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • A.P. Minton Implications of macromolecular crowding for protein assembly Curr Opin Struct Biol 10 2000 34 39
    • (2000) Curr Opin Struct Biol , vol.10 , pp. 34-39
    • Minton, A.P.1
  • 8
    • 16344364032 scopus 로고    scopus 로고
    • Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: Macromolecular crowding and protein stability revisited
    • A.P. Minton Models for excluded volume interaction between an unfolded protein and rigid macromolecular cosolutes: macromolecular crowding and protein stability revisited Biophys J 88 2005 971 985
    • (2005) Biophys J , vol.88 , pp. 971-985
    • Minton, A.P.1
  • 9
    • 16344389134 scopus 로고    scopus 로고
    • Molecular crowding enhances native state stability and refolding rates of globular proteins
    • M.S. Cheung, D. Klimov, and D. Thirumalai Molecular crowding enhances native state stability and refolding rates of globular proteins Proc Natl Acad Sci USA 102 2005 4753 4758
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 4753-4758
    • Cheung, M.S.1    Klimov, D.2    Thirumalai, D.3
  • 10
    • 61449196621 scopus 로고    scopus 로고
    • Folding, stability and shape of proteins in crowded environments: Experimental and computational approaches
    • A. Samiotakis, P. Wittung-Stafshede, and M.S. Cheung Folding, stability and shape of proteins in crowded environments: experimental and computational approaches Int J Mol Sci 10 2009 572 588
    • (2009) Int J Mol Sci , vol.10 , pp. 572-588
    • Samiotakis, A.1    Wittung-Stafshede, P.2    Cheung, M.S.3
  • 12
    • 35348851499 scopus 로고    scopus 로고
    • Macromolecular crowding increases structural content of folded proteins
    • M. Perham, L. Stagg, and P. Wittung-Stafshede Macromolecular crowding increases structural content of folded proteins FEBS Lett 581 2007 5065 5069
    • (2007) FEBS Lett , vol.581 , pp. 5065-5069
    • Perham, M.1    Stagg, L.2    Wittung-Stafshede, P.3
  • 15
    • 77955686807 scopus 로고    scopus 로고
    • Effects of proteins on protein diffusion
    • Y. Wang, C. Li, and G.J. Pielak Effects of proteins on protein diffusion J Am Chem Soc 132 2010 9392 9397
    • (2010) J Am Chem Soc , vol.132 , pp. 9392-9397
    • Wang, Y.1    Li, C.2    Pielak, G.J.3
  • 16
    • 45849120983 scopus 로고    scopus 로고
    • Simulation-based fitting of protein-protein interaction potentials to SAXS experiments
    • S.J. Kim, C. Dumont, and M. Gruebele Simulation-based fitting of protein-protein interaction potentials to SAXS experiments Biophys J 94 2008 4924 4931
    • (2008) Biophys J , vol.94 , pp. 4924-4931
    • Kim, S.J.1    Dumont, C.2    Gruebele, M.3
  • 17
    • 77955699308 scopus 로고    scopus 로고
    • Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria
    • M. Jiao, H.T. Li, J. Chen, A.P. Minton, and Y. Liang Attractive protein-polymer interactions markedly alter the effect of macromolecular crowding on protein association equilibria Biophys J 99 2010 914 923
    • (2010) Biophys J , vol.99 , pp. 914-923
    • Jiao, M.1    Li, H.T.2    Chen, J.3    Minton, A.P.4    Liang, Y.5
  • 18
    • 84874194203 scopus 로고    scopus 로고
    • Polymer crowders and protein crowders act similarly on protein folding stability
    • H.-X. Zhou Polymer crowders and protein crowders act similarly on protein folding stability FEBS Lett 587 2013 394 397
    • (2013) FEBS Lett , vol.587 , pp. 394-397
    • Zhou, H.-X.1
  • 19
    • 0034814860 scopus 로고    scopus 로고
    • Quantitative protein stability measurement in vivo
    • S. Ghaemmaghami, and T.G. Oas Quantitative protein stability measurement in vivo Nat Struct Mol Biol 8 2001 879 882
    • (2001) Nat Struct Mol Biol , vol.8 , pp. 879-882
    • Ghaemmaghami, S.1    Oas, T.G.2
  • 21
    • 80052479046 scopus 로고    scopus 로고
    • Protein stability and folding kinetics in the nucleus and endoplasmic reticulum of eucaryotic cells
    • A. Dhar, K. Girdhar, D. Singh, H. Gelman, S. Ebbinghaus, and M. Gruebele Protein stability and folding kinetics in the nucleus and endoplasmic reticulum of eucaryotic cells Biophys J 101 2011 421 430
    • (2011) Biophys J , vol.101 , pp. 421-430
    • Dhar, A.1    Girdhar, K.2    Singh, D.3    Gelman, H.4    Ebbinghaus, S.5    Gruebele, M.6
  • 22
    • 78049291945 scopus 로고    scopus 로고
    • Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding
    • A. Dhar, A. Samiotakis, S. Ebbinghaus, L. Nienhaus, D. Homouz, and M. Gruebele et al. Structure, function, and folding of phosphoglycerate kinase are strongly perturbed by macromolecular crowding Proc Natl Acad Sci USA 107 2010 17586 17591
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 17586-17591
    • Dhar, A.1    Samiotakis, A.2    Ebbinghaus, S.3    Nienhaus, L.4    Homouz, D.5    Gruebele, M.6
  • 23
    • 0041624356 scopus 로고    scopus 로고
    • The largest protein observed to fold by two-state kinetic mechanism does not obey contact-order correlation
    • K. Jones, and P. Wittung-Stafshede The largest protein observed to fold by two-state kinetic mechanism does not obey contact-order correlation J Am Chem Soc 125 2003 9606 9607
    • (2003) J Am Chem Soc , vol.125 , pp. 9606-9607
    • Jones, K.1    Wittung-Stafshede, P.2
  • 24
    • 0035976777 scopus 로고    scopus 로고
    • Characterization of surface antigen from Lyme disease spirochete Borrelia burgdorferi
    • K. Jones, J. Guidry, and P. Wittung-Stafshede Characterization of surface antigen from Lyme disease spirochete Borrelia burgdorferi Biochem Biophys Res Commun 289 2001 389 394
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 389-394
    • Jones, K.1    Guidry, J.2    Wittung-Stafshede, P.3
  • 25
  • 26
    • 84868130708 scopus 로고    scopus 로고
    • Temperature dependence of protein folding kinetics in living cells
    • M.H. Guo, Y.F. Xu, and M. Gruebele Temperature dependence of protein folding kinetics in living cells Proc Natl Acad Sci USA 109 2012 17863 17867
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 17863-17867
    • Guo, M.H.1    Xu, Y.F.2    Gruebele, M.3
  • 27
  • 29
    • 85198904462 scopus 로고
    • Two-dimensional goodness-of-fit testing in astronomy
    • J.A. Peacock Two-dimensional goodness-of-fit testing in astronomy Mon Not R Astron Soc 202 1983 615 627
    • (1983) Mon Not R Astron Soc , vol.202 , pp. 615-627
    • Peacock, J.A.1
  • 30
    • 41649117883 scopus 로고    scopus 로고
    • A new way to explore the world of extracellular protein interactions
    • C.M. Sanderson A new way to explore the world of extracellular protein interactions Genome Res 18 2008 517 520
    • (2008) Genome Res , vol.18 , pp. 517-520
    • Sanderson, C.M.1
  • 32
    • 79951888750 scopus 로고    scopus 로고
    • Protein folding landscapes in the living cell
    • S. Ebbinghaus, and M. Gruebele Protein folding landscapes in the living cell J Phys Chem Lett 2 2011 314 319
    • (2011) J Phys Chem Lett , vol.2 , pp. 314-319
    • Ebbinghaus, S.1    Gruebele, M.2
  • 33
    • 0020135896 scopus 로고
    • Molecular evolution, intracellular organization, and the quinary structure of proteins
    • E. McConkey Molecular evolution, intracellular organization, and the quinary structure of proteins Proc Natl Acad Sci USA 79 1982 3236 3240
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 3236-3240
    • McConkey, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.