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Volumn 103, Issue 12, 2012, Pages 2484-2491

Role of nonspecific interactions in molecular chaperones through model-based bioinformatics

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN 60; EARLY PREGNANCY FACTOR; ESCHERICHIA COLI PROTEIN;

EID: 84871267976     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.10.040     Document Type: Article
Times cited : (11)

References (40)
  • 2
    • 0020336190 scopus 로고
    • Living with water stress: Evolution of osmolyte systems
    • P.H. Yancey, and M.E. Clark G.N. Somero Living with water stress: evolution of osmolyte systems Science 217 1982 1214 1222 (Pubitemid 13283134)
    • (1982) Science , vol.217 , Issue.4566 , pp. 1214-1222
    • Yancey, P.H.1    Clark, M.E.2    Hand, S.C.3    Bowlus, R.D.4    Somero, G.N.5
  • 4
    • 68649123756 scopus 로고    scopus 로고
    • The GroEL/GroES cis cavity as a passive anti-aggregation device
    • A.L. Horwich, A.C. Apetri, and W.A. Fenton The GroEL/GroES cis cavity as a passive anti-aggregation device FEBS Lett. 583 2009 2654 2662
    • (2009) FEBS Lett. , vol.583 , pp. 2654-2662
    • Horwich, A.L.1    Apetri, A.C.2    Fenton, W.A.3
  • 5
    • 0033617534 scopus 로고    scopus 로고
    • Chaperonin function: Folding by forced unfolding
    • DOI 10.1126/science.284.5415.822
    • M. Shtilerman, G.H. Lorimer, and S.W. Englander Chaperonin function: folding by forced unfolding Science 284 1999 822 825 (Pubitemid 29291351)
    • (1999) Science , vol.284 , Issue.5415 , pp. 822-825
    • Shtilerman, M.1    Lorimer, G.H.2    Englander, S.W.3
  • 6
    • 77955360949 scopus 로고    scopus 로고
    • Single-molecule spectroscopy of protein folding in a chaperonin cage
    • H. Hofmann, and F. Hillger B. Schuler Single-molecule spectroscopy of protein folding in a chaperonin cage Proc. Natl. Acad. Sci. USA 107 2010 11793 11798
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 11793-11798
    • Hofmann, H.1    Hillger, F.2    Schuler, B.3
  • 8
    • 84868121425 scopus 로고    scopus 로고
    • Decoding nonspecific interactions from nature
    • A.D. White, and A.K. Nowinski S. Jiang Decoding nonspecific interactions from nature Chem. Sci. 3 2012 3488 3494
    • (2012) Chem. Sci. , vol.3 , pp. 3488-3494
    • White, A.D.1    Nowinski, A.K.2    Jiang, S.3
  • 9
    • 77649210916 scopus 로고    scopus 로고
    • Ultralow-fouling, functionalizable, and hydrolyzable zwitterionic materials and their derivatives for biological applications
    • S. Jiang, and Z. Cao Ultralow-fouling, functionalizable, and hydrolyzable zwitterionic materials and their derivatives for biological applications Adv. Mater. (Deerfield Beach, Fla.) 22 2010 920 932
    • (2010) Adv. Mater. (Deerfield Beach, Fla.) , vol.22 , pp. 920-932
    • Jiang, S.1    Cao, Z.2
  • 10
    • 33644515328 scopus 로고    scopus 로고
    • Mimicking the action of GroEL in molecular dynamics simulations: Application to the refinement of protein structures
    • H. Fan, and A.E. Mark Mimicking the action of GroEL in molecular dynamics simulations: application to the refinement of protein structures Protein Sci. 15 2006 441 448
    • (2006) Protein Sci. , vol.15 , pp. 441-448
    • Fan, H.1    Mark, A.E.2
  • 11
    • 80053060122 scopus 로고    scopus 로고
    • Simulation studies of protein folding/unfolding equilibrium under polar and nonpolar confinement
    • J. Tian, and A.E. Garcia Simulation studies of protein folding/unfolding equilibrium under polar and nonpolar confinement J. Am. Chem. Soc. 133 2011 15157 15164
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15157-15164
    • Tian, J.1    Garcia, A.E.2
  • 12
    • 0002617993 scopus 로고    scopus 로고
    • A simple model of chaperonin-mediated protein folding
    • DOI 10.1002/(SICI)1097-0134 (199603)24:3<345:: AID-PROT7>3.0.CO;2-F
    • H.S. Chan, and K.A. Dill A simple model of chaperonin-mediated protein folding Proteins 24 1996 345 351 (Pubitemid 26095966)
    • (1996) Proteins: Structure, Function and Genetics , vol.24 , Issue.3 , pp. 345-351
    • Chan, H.S.1    Dill, K.A.2
  • 15
    • 0032548904 scopus 로고    scopus 로고
    • Adaptation of protein surfaces to subcellular location
    • DOI 10.1006/jmbi.1997.1498
    • M.A. Andrade, S.I. O'Donoghue, and B. Rost Adaptation of protein surfaces to subcellular location J. Mol. Biol. 276 1998 517 525 (Pubitemid 28085337)
    • (1998) Journal of Molecular Biology , vol.276 , Issue.2 , pp. 517-525
    • Andrade, M.A.1    O'Donoghue, S.I.2    Rost, B.3
  • 16
    • 12544256134 scopus 로고    scopus 로고
    • Calculation of standard atomic volumes for RNA and comparison with proteins: RNA is packed more tightly
    • N.R. Voss, and M. Gerstein Calculation of standard atomic volumes for RNA and comparison with proteins: RNA is packed more tightly J. Mol. Biol. 346 2005 477 492
    • (2005) J. Mol. Biol. , vol.346 , pp. 477-492
    • Voss, N.R.1    Gerstein, M.2
  • 17
    • 1842326139 scopus 로고    scopus 로고
    • Bayesian statistical analysis of protein side-chain rotamer preferences
    • R.L. Dunbrack Jr., and F.E. Cohen Bayesian statistical analysis of protein side-chain rotamer preferences Protein Sci. 6 1997 1661 1681 (Pubitemid 27333069)
    • (1997) Protein Science , vol.6 , Issue.8 , pp. 1661-1681
    • Dunbrack Jr., R.L.1    Cohen, F.E.2
  • 19
    • 58149498257 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of protein folding under confinement
    • J. Mittal, and R.B. Best Thermodynamics and kinetics of protein folding under confinement Proc. Natl. Acad. Sci. USA 105 2008 20233 20238
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 20233-20238
    • Mittal, J.1    Best, R.B.2
  • 22
    • 33845377127 scopus 로고
    • Estimation of effective interresidue contact energies from protein crystal structures: Quasi-chemical approximation
    • S. Miyazawa, and R.L. Jernigan Estimation of effective interresidue contact energies from protein crystal structures: quasi-chemical approximation Macromolecules 18 1985 534 552
    • (1985) Macromolecules , vol.18 , pp. 534-552
    • Miyazawa, S.1    Jernigan, R.L.2
  • 23
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • J. Frydman Folding of newly translated proteins in vivo: the role of molecular chaperones Annu. Rev. Biochem. 70 2001 603 647
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 24
    • 4944221602 scopus 로고    scopus 로고
    • Expansion and compression of a protein folding intermediate by GroEL
    • DOI 10.1016/j.molcel.2004.09.003, PII S1097276504005210
    • Z. Lin, and H.S. Rye Expansion and compression of a protein folding intermediate by GroEL Mol. Cell 16 2004 23 34 (Pubitemid 39330149)
    • (2004) Molecular Cell , vol.16 , Issue.1 , pp. 23-34
    • Lin, Z.1    Rye, H.S.2
  • 25
    • 0028025404 scopus 로고
    • Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature β-lactamase
    • R. Zahn, and A. Plückthun Thermodynamic partitioning model for hydrophobic binding of polypeptides by GroEL. II. GroEL recognizes thermally unfolded mature β-lactamase J. Mol. Biol. 242 1994 165 174
    • (1994) J. Mol. Biol. , vol.242 , pp. 165-174
    • Zahn, R.1    Plückthun, A.2
  • 27
    • 78651447522 scopus 로고    scopus 로고
    • Calculation of local water densities in biological systems: A comparison of molecular dynamics simulations and the 3D-RISM-KH molecular theory of solvation
    • M.C. Stumpe, and N. Blinov V.S. Pande Calculation of local water densities in biological systems: a comparison of molecular dynamics simulations and the 3D-RISM-KH molecular theory of solvation J. Phys. Chem. B 115 2011 319 328
    • (2011) J. Phys. Chem. B , vol.115 , pp. 319-328
    • Stumpe, M.C.1    Blinov, N.2    Pande, V.S.3
  • 31
    • 34248349952 scopus 로고    scopus 로고
    • Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL
    • DOI 10.1073/pnas.0700820104
    • G.W. Farr, W.A. Fenton, and A.L. Horwich Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL Proc. Natl. Acad. Sci. USA 104 2007 5342 5347 (Pubitemid 47175682)
    • (2007) Proceedings of the National Academy of Sciences of the United States of America , vol.104 , Issue.13 , pp. 5342-5347
    • Farr, G.W.1    Fenton, W.A.2    Horwich, A.L.3
  • 32
    • 77956256437 scopus 로고    scopus 로고
    • Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle
    • J.H. Pereira, and C.Y. Ralston P.D. Adams Crystal structures of a group II chaperonin reveal the open and closed states associated with the protein folding cycle J. Biol. Chem. 285 2010 27958 27966
    • (2010) J. Biol. Chem. , vol.285 , pp. 27958-27966
    • Pereira, J.H.1    Ralston, C.Y.2    Adams, P.D.3
  • 33
    • 0019883174 scopus 로고
    • Affinities of amino acid side chains for solvent water
    • R. Wolfenden, and L. Andersson C.C. Southgate Affinities of amino acid side chains for solvent water Biochemistry 20 1981 849 855
    • (1981) Biochemistry , vol.20 , pp. 849-855
    • Wolfenden, R.1    Andersson, L.2    Southgate, C.C.3
  • 35
    • 44349090822 scopus 로고    scopus 로고
    • Essential role of the chaperonin folding compartment in vivo
    • DOI 10.1038/emboj.2008.77, PII EMBOJ200877
    • Y.-C. Tang, and H.-C. Chang M. Hayer-Hartl Essential role of the chaperonin folding compartment in vivo EMBO J. 27 2008 1458 1468 (Pubitemid 351733332)
    • (2008) EMBO Journal , vol.27 , Issue.10 , pp. 1458-1468
    • Tang, Y.-C.1    Chang, H.-C.2    Chakraborty, K.3    Hartl, F.U.4    Hayer-Hartl, M.5
  • 37
    • 84859323531 scopus 로고    scopus 로고
    • Sequence, structure, and function of peptide self-assembled monolayers
    • A.K. Nowinski, and F. Sun S. Jiang Sequence, structure, and function of peptide self-assembled monolayers J. Am. Chem. Soc. 134 2012 6000 6005
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 6000-6005
    • Nowinski, A.K.1    Sun, F.2    Jiang, S.3
  • 38
    • 68549103438 scopus 로고    scopus 로고
    • Ultra-low fouling peptide surfaces derived from natural amino acids
    • S. Chen, Z. Cao, and S. Jiang Ultra-low fouling peptide surfaces derived from natural amino acids Biomaterials 30 2009 5892 5896
    • (2009) Biomaterials , vol.30 , pp. 5892-5896
    • Chen, S.1    Cao, Z.2    Jiang, S.3
  • 39
    • 55549139212 scopus 로고    scopus 로고
    • Monolayers of 3-mercaptopropyl-amino acid to reduce the nonspecific adsorption of serum proteins on the surface of biosensors
    • O.R. Bolduc, and J.-F. Masson Monolayers of 3-mercaptopropyl-amino acid to reduce the nonspecific adsorption of serum proteins on the surface of biosensors Langmuir 24 2008 12085 12091
    • (2008) Langmuir , vol.24 , pp. 12085-12091
    • Bolduc, O.R.1    Masson, J.-F.2


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