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Volumn 587, Issue 8, 2013, Pages 1053-1061

Influence of crowded cellular environments on protein folding, binding, and oligomerization: Biological consequences and potentials of atomistic modeling

Author keywords

Macromolecular crowding; Postprocessing; Protein aggregation; Protein binding; Protein folding

Indexed keywords

OLIGOMER; PROTEIN;

EID: 84876034428     PISSN: 00145793     EISSN: 18733468     Source Type: Journal    
DOI: 10.1016/j.febslet.2013.01.064     Document Type: Review
Times cited : (142)

References (87)
  • 1
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biochemical, biophysical, and physiological consequences
    • S.B. Zimmerman, and A.P. Minton Macromolecular crowding: biochemical, biophysical, and physiological consequences Annu. Rev. Biophys. Biomol. Struct. 22 1993 27 65
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 2
    • 0034047840 scopus 로고    scopus 로고
    • Ten commandments: Lessons from the enzymology of DNA replication
    • A. Kornberg Ten commandments: lessons from the enzymology of DNA replication J. Bacteriol. 182 2000 3613 3618
    • (2000) J. Bacteriol. , vol.182 , pp. 3613-3618
    • Kornberg, A.1
  • 3
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but underappreciated
    • R.J. Ellis Macromolecular crowding: obvious but underappreciated Trends Biochem. Sci. 26 2001 597 604
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 4
    • 0347249969 scopus 로고
    • Enzymatic replication of the origin of the Escherichia coli chromosome
    • R.S. Fuller, J.M. Kaguni, and A. Kornberg Enzymatic replication of the origin of the Escherichia coli chromosome Proc. Natl. Acad. Sci. USA 78 1981 7370 7374
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 7370-7374
    • Fuller, R.S.1    Kaguni, J.M.2    Kornberg, A.3
  • 5
    • 0037177250 scopus 로고    scopus 로고
    • Molecular crowding accelerates fibrillization of alpha-synuclein: Could an increase in the cytoplasmic protein concentration induce Parkinson's disease?
    • M.D. Shtilerman, T.T. Ding, and P.T. Lansbury Jr. Molecular crowding accelerates fibrillization of alpha-synuclein: could an increase in the cytoplasmic protein concentration induce Parkinson's disease? Biochemistry 41 2002 3855 3860
    • (2002) Biochemistry , vol.41 , pp. 3855-3860
    • Shtilerman, M.D.1    Ding, T.T.2    Lansbury, Jr.P.T.3
  • 6
    • 0037181497 scopus 로고    scopus 로고
    • Accelerated alpha-synuclein fibrillation in crowded milieu
    • V.N. Uversky, E.M. Cooper, K.S. Bower, J. Li, and A.L. Fink Accelerated alpha-synuclein fibrillation in crowded milieu FEBS Lett. 515 2002 99 103
    • (2002) FEBS Lett. , vol.515 , pp. 99-103
    • Uversky, V.N.1    Cooper, E.M.2    Bower, K.S.3    Li, J.4    Fink, A.L.5
  • 7
    • 0037040878 scopus 로고    scopus 로고
    • Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II
    • D.M. Hatters, A.P. Minton, and G.J. Howlett Macromolecular crowding accelerates amyloid formation by human apolipoprotein C-II J. Biol. Chem. 277 2002 7824 7830
    • (2002) J. Biol. Chem. , vol.277 , pp. 7824-7830
    • Hatters, D.M.1    Minton, A.P.2    Howlett, G.J.3
  • 8
    • 27644552564 scopus 로고    scopus 로고
    • Effect of macromolecular crowding agents on human immunodeficiency virus type 1 capsid protein assembly in vitro
    • M. del Alamo, G. Rivas, and M.G. Mateu Effect of macromolecular crowding agents on human immunodeficiency virus type 1 capsid protein assembly in vitro J. Virol. 79 2005 14271 14281
    • (2005) J. Virol. , vol.79 , pp. 14271-14281
    • Del Alamo, M.1    Rivas, G.2    Mateu, M.G.3
  • 9
    • 0242584670 scopus 로고    scopus 로고
    • Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment
    • J.M. Gonzalez, M. Jimenez, M. Velez, J. Mingorance, J.M. Andreu, M. Vicente, and G. Rivas Essential cell division protein FtsZ assembles into one monomer-thick ribbons under conditions resembling the crowded intracellular environment J. Biol. Chem. 278 2003 37664 37671
    • (2003) J. Biol. Chem. , vol.278 , pp. 37664-37671
    • Gonzalez, J.M.1    Jimenez, M.2    Velez, M.3    Mingorance, J.4    Andreu, J.M.5    Vicente, M.6    Rivas, G.7
  • 10
    • 15244361470 scopus 로고    scopus 로고
    • Molecular crowding limits the role of fetal hemoglobin in therapy for sickle cell disease
    • M. Rotter, A. Aprelev, K. Adachi, and F.A. Ferrone Molecular crowding limits the role of fetal hemoglobin in therapy for sickle cell disease J. Mol. Biol. 347 2005 1015 1023
    • (2005) J. Mol. Biol. , vol.347 , pp. 1015-1023
    • Rotter, M.1    Aprelev, A.2    Adachi, K.3    Ferrone, F.A.4
  • 11
    • 17044454299 scopus 로고    scopus 로고
    • Efficacy of macromolecular crowding in forcing proteins to fold
    • Y. Qu, and D.W. Bolen Efficacy of macromolecular crowding in forcing proteins to fold Biophys. Chem. 101-102 2002 155 165
    • (2002) Biophys. Chem. , vol.101-102 , pp. 155-165
    • Qu, Y.1    Bolen, D.W.2
  • 12
    • 22144469126 scopus 로고    scopus 로고
    • Effects of pH, salt, and macromolecular crowding on the stability of FK506-binding protein: An integrated experimental and theoretical study
    • D.S. Spencer, K. Xu, T.M. Logan, and H.-X. Zhou Effects of pH, salt, and macromolecular crowding on the stability of FK506-binding protein: an integrated experimental and theoretical study J. Mol. Biol. 351 2005 219 232
    • (2005) J. Mol. Biol. , vol.351 , pp. 219-232
    • Spencer, D.S.1    Xu, K.2    Logan, T.M.3    Zhou, H.-X.4
  • 13
    • 33645454904 scopus 로고    scopus 로고
    • 15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions
    • 15N NMR spin relaxation dispersion study of the molecular crowding effects on protein folding under native conditions J. Am. Chem. Soc. 128 2006 3916 3917
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3916-3917
    • Ai, X.1    Zhou, Z.2    Bai, Y.3    Choy, W.Y.4
  • 14
    • 34249787868 scopus 로고    scopus 로고
    • Destabilised mutants of ubiquitin gain equal stability in crowded solutions
    • A. Roberts, and S.E. Jackson Destabilised mutants of ubiquitin gain equal stability in crowded solutions Biophys. Chem. 128 2007 140 149
    • (2007) Biophys. Chem. , vol.128 , pp. 140-149
    • Roberts, A.1    Jackson, S.E.2
  • 15
    • 44349088135 scopus 로고    scopus 로고
    • Residue-level interrogation of macromolecular crowding effects on protein stability
    • L.M. Charlton, C.O. Barnes, C. Li, J. Orans, G.B. Young, and G.J. Pielak Residue-level interrogation of macromolecular crowding effects on protein stability J. Am. Chem. Soc. 130 2008 6826 6830
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6826-6830
    • Charlton, L.M.1    Barnes, C.O.2    Li, C.3    Orans, J.4    Young, G.B.5    Pielak, G.J.6
  • 16
    • 70349310244 scopus 로고    scopus 로고
    • Nonaddtive effects of mixed crowding on protein stability
    • J. Batra, K. Xu, and H.-X. Zhou Nonaddtive effects of mixed crowding on protein stability Proteins 77 2009 133 138
    • (2009) Proteins , vol.77 , pp. 133-138
    • Batra, J.1    Xu, K.2    Zhou, H.-X.3
  • 17
    • 68949143016 scopus 로고    scopus 로고
    • Common crowding agents have only a small effect on protein-protein interactions
    • Y. Phillip, E. Sherman, G. Haran, and G. Schreiber Common crowding agents have only a small effect on protein-protein interactions Biophys. J. 97 2009 875 885
    • (2009) Biophys. J. , vol.97 , pp. 875-885
    • Phillip, Y.1    Sherman, E.2    Haran, G.3    Schreiber, G.4
  • 18
    • 68949083274 scopus 로고    scopus 로고
    • Effect of macromolecular crowding on protein binding stability: Modest stabilization and significant biological consequences
    • J. Batra, K. Xu, S. Qin, and H.-X. Zhou Effect of macromolecular crowding on protein binding stability: modest stabilization and significant biological consequences Biophys. J. 97 2009 906 911
    • (2009) Biophys. J. , vol.97 , pp. 906-911
    • Batra, J.1    Xu, K.2    Qin, S.3    Zhou, H.-X.4
  • 19
    • 77957117205 scopus 로고    scopus 로고
    • Rate theories for biologists
    • H.X. Zhou Rate theories for biologists Q. Rev. Biophys. 43 2010 219 293
    • (2010) Q. Rev. Biophys. , vol.43 , pp. 219-293
    • Zhou, H.X.1
  • 20
    • 84985735713 scopus 로고
    • Excluded volume as a determinant of macromolecular structure and reactivity
    • A.P. Minton Excluded volume as a determinant of macromolecular structure and reactivity Biopolymers 20 1981 2093 2120
    • (1981) Biopolymers , vol.20 , pp. 2093-2120
    • Minton, A.P.1
  • 21
    • 0032311227 scopus 로고    scopus 로고
    • Molecular crowding: Analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion
    • A.P. Minton Molecular crowding: analysis of effects of high concentrations of inert cosolutes on biochemical equilibria and rates in terms of volume exclusion Methods Enzymol. 295 1998 127 149
    • (1998) Methods Enzymol. , vol.295 , pp. 127-149
    • Minton, A.P.1
  • 22
    • 33746099650 scopus 로고    scopus 로고
    • Protein aggregation in crowded environments
    • R.J. Ellis, and A.P. Minton Protein aggregation in crowded environments Biol. Chem. 387 2006 485 497
    • (2006) Biol. Chem. , vol.387 , pp. 485-497
    • Ellis, R.J.1    Minton, A.P.2
  • 23
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • H.X. Zhou, G. Rivas, and A.P. Minton Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences Ann. Rev. Biophys. 37 2008 375 397
    • (2008) Ann. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 24
    • 77951298407 scopus 로고    scopus 로고
    • Models of macromolecular crowding effects and the need for quantitative comparisons with experiment
    • A.H. Elcock Models of macromolecular crowding effects and the need for quantitative comparisons with experiment Curr. Opin. Struct. Biol. 20 2010 196 206
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 196-206
    • Elcock, A.H.1
  • 25
    • 79551687316 scopus 로고    scopus 로고
    • Protein folding in the cell: Challenges and progress
    • A. Gershenson, and L.M. Gierasch Protein folding in the cell: challenges and progress Curr. Opin. Struct. Biol. 21 2011 32 41
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 32-41
    • Gershenson, A.1    Gierasch, L.M.2
  • 26
    • 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
  • 27
    • 0005404762 scopus 로고
    • Holobiochemistry: An Integrated Approach to the Understanding of Biochemical Mechanism that Emerges from the Study of Proteins and Protein Associations in Volume-Occupied Solutions
    • P. Srere, M. Jones, C. Mathews, Liss New York
    • A. Minton Holobiochemistry: An Integrated Approach to the Understanding of Biochemical Mechanism that Emerges from the Study of Proteins and Protein Associations in Volume-Occupied Solutions P. Srere, M. Jones, C. Mathews, Structural and Organizational Aspects of Metabolic Regulation 1989 Liss New York 291 306
    • (1989) Structural and Organizational Aspects of Metabolic Regulation , pp. 291-306
    • Minton, A.1
  • 28
    • 4544278751 scopus 로고    scopus 로고
    • Protein folding and binding in confined spaces and in crowded solutions
    • H.X. Zhou Protein folding and binding in confined spaces and in crowded solutions J. Mol. Recognit. 17 2004 368 375
    • (2004) J. Mol. Recognit. , vol.17 , pp. 368-375
    • Zhou, H.X.1
  • 29
    • 4544329005 scopus 로고    scopus 로고
    • Crowding and the polymerization of sickle hemoglobin
    • F.A. Ferrone, and M.A. Rotter Crowding and the polymerization of sickle hemoglobin J. Mol. Recognit. 17 2004 497 504
    • (2004) J. Mol. Recognit. , vol.17 , pp. 497-504
    • Ferrone, F.A.1    Rotter, M.A.2
  • 30
    • 84877043455 scopus 로고    scopus 로고
    • Simulation and modeling of crowding effects on the thermodynamic and kinetic properties of proteins with atomic details
    • Zhou, H.X. and Qin, S. Simulation and modeling of crowding effects on the thermodynamic and kinetic properties of proteins with atomic details, Biophys. Rev.; http://dx.doi.org/10.1007/s12551-013-0101-7.
    • Biophys. Rev
    • Zhou, H.X.1    Qin, S.2
  • 31
    • 77955707910 scopus 로고    scopus 로고
    • Volume exclusion and soft interaction effects on protein stability under crowded conditions
    • A.C. Miklos, C.G. Li, N.G. Sharaf, and G.J. Pielak Volume exclusion and soft interaction effects on protein stability under crowded conditions Biochemistry 49 2010 6984 6991
    • (2010) Biochemistry , vol.49 , pp. 6984-6991
    • Miklos, A.C.1    Li, C.G.2    Sharaf, N.G.3    Pielak, G.J.4
  • 34
    • 84870899331 scopus 로고    scopus 로고
    • Unexpected effects of macromolecular crowding on protein stability
    • L.A. Benton, A.E. Smith, G.B. Young, and G.J. Pielak Unexpected effects of macromolecular crowding on protein stability Biochemistry 51 2012 9773 9775
    • (2012) Biochemistry , vol.51 , pp. 9773-9775
    • Benton, L.A.1    Smith, A.E.2    Young, G.B.3    Pielak, G.J.4
  • 35
    • 0020855355 scopus 로고
    • Hydrogen exchange and structural dynamics of proteins and nucleic acids
    • S.W. Englander, and N.R. Kallenbach Hydrogen exchange and structural dynamics of proteins and nucleic acids Q. Rev. Biophys. 16 1983 521 655
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 521-655
    • Englander, S.W.1    Kallenbach, N.R.2
  • 36
    • 84874194203 scopus 로고    scopus 로고
    • Polymer crowders and protein crowders act similarly on protein folding stability
    • Zhou, H.X. Polymer crowders and protein crowders act similarly on protein folding stability, FEBS Lett.; http://dx.doi.org/10.1016/j.febslet.2013.01.030.
    • FEBS Lett
    • Zhou, H.X.1
  • 37
    • 84867012423 scopus 로고    scopus 로고
    • Crowding effects on the small, fast-folding protein lambda6-85
    • discussion 475-500
    • S. Denos, A. Dhar, and M. Gruebele Crowding effects on the small, fast-folding protein lambda6-85 Faraday Discuss. 157 2012 451 462 discussion 475-500
    • (2012) Faraday Discuss. , vol.157 , pp. 451-462
    • Denos, S.1    Dhar, A.2    Gruebele, M.3
  • 38
    • 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
  • 39
    • 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
  • 42
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • P.H. Weinreb, W. Zhen, A.W. Poon, K.A. Conway, and P.T. Lansbury Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded Biochemistry 35 1996 13709 13715
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, Jr.P.T.5
  • 43
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of alpha-synuclein in its free and lipid-associated states
    • D. Eliezer, E. Kutluay, R. Bussell Jr.; and G. Browne Conformational properties of alpha-synuclein in its free and lipid-associated states J. Mol. Biol. 307 2001 1061 1073
    • (2001) J. Mol. Biol. , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell, Jr.R.3    Browne, G.4
  • 44
    • 0034773940 scopus 로고    scopus 로고
    • Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c
    • A.S. Morar, A. Olteanu, G.B. Young, and G.J. Pielak Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c Protein Sci. 10 2001 2195 2199
    • (2001) Protein Sci. , vol.10 , pp. 2195-2199
    • Morar, A.S.1    Olteanu, A.2    Young, G.B.3    Pielak, G.J.4
  • 45
    • 0035815664 scopus 로고    scopus 로고
    • Evidence for a partially folded intermediate in alpha-synuclein fibril formation
    • V.N. Uversky, J. Li, and A.L. Fink Evidence for a partially folded intermediate in alpha-synuclein fibril formation J. Biol. Chem. 276 2001 10737 10744
    • (2001) J. Biol. Chem. , vol.276 , pp. 10737-10744
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 46
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human alpha-synuclein
    • T.S. Ulmer, A. Bax, N.B. Cole, and R.L. Nussbaum Structure and dynamics of micelle-bound human alpha-synuclein J. Biol. Chem. 280 2005 9595 9603
    • (2005) J. Biol. Chem. , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 48
    • 80052398365 scopus 로고    scopus 로고
    • Alpha-synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • T. Bartels, J.G. Choi, and D.J. Selkoe Alpha-synuclein occurs physiologically as a helically folded tetramer that resists aggregation Nature 477 2011 107 110
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 51
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of alpha-synuclein: From structure and toxicity to therapeutic target
    • H.A. Lashuel, C.R. Overk, A. Oueslati, and E. Masliah The many faces of alpha-synuclein: from structure and toxicity to therapeutic target Nat. Rev. Neurosci. 14 2013 38 48
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 52
    • 84860172516 scopus 로고    scopus 로고
    • N-terminal acetylation is critical for forming alpha-helical oligomer of alpha-synuclein
    • A.J. Trexler, and E. Rhoades N-terminal acetylation is critical for forming alpha-helical oligomer of alpha-synuclein Protein Sci. 21 2012 601 605
    • (2012) Protein Sci. , vol.21 , pp. 601-605
    • Trexler, A.J.1    Rhoades, E.2
  • 53
    • 33644538922 scopus 로고    scopus 로고
    • Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein
    • B.C. McNulty, A. Tripathy, G.B. Young, L.M. Charlton, J. Orans, and G.J. Pielak Temperature-induced reversible conformational change in the first 100 residues of alpha-synuclein Protein Sci. 15 2006 602 608
    • (2006) Protein Sci. , vol.15 , pp. 602-608
    • McNulty, B.C.1    Tripathy, A.2    Young, G.B.3    Charlton, L.M.4    Orans, J.5    Pielak, G.J.6
  • 54
    • 29544433937 scopus 로고    scopus 로고
    • Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder
    • B.C. McNulty, G.B. Young, and G.J. Pielak Macromolecular crowding in the Escherichia coli periplasm maintains alpha-synuclein disorder J. Mol. Biol. 355 2006 893 897
    • (2006) J. Mol. Biol. , vol.355 , pp. 893-897
    • McNulty, B.C.1    Young, G.B.2    Pielak, G.J.3
  • 55
    • 79951841821 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on an intrinsically disordered protein characterized by small-angle neutron scattering with contrast matching
    • D. Johansen, C.M.J. Jeffries, B. Hammouda, J. Trewhella, and D.P. Goldenberg Effects of macromolecular crowding on an intrinsically disordered protein characterized by small-angle neutron scattering with contrast matching Biophys. J. 100 2011 1120 1128
    • (2011) Biophys. J. , vol.100 , pp. 1120-1128
    • Johansen, D.1    Jeffries, C.M.J.2    Hammouda, B.3    Trewhella, J.4    Goldenberg, D.P.5
  • 57
    • 77953376172 scopus 로고    scopus 로고
    • Compression of random coils due to macromolecular crowding: Scaling effects
    • C. Le Coeur, J. Teixeira, P. Busch, and S. Longeville Compression of random coils due to macromolecular crowding: scaling effects Phys. Rev. E 81 2010 061914
    • (2010) Phys. Rev. e , vol.81 , pp. 061914
    • Le Coeur, C.1    Teixeira, J.2    Busch, P.3    Longeville, S.4
  • 58
    • 77955044557 scopus 로고    scopus 로고
    • Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state
    • J. Hong, and L.M. Gierasch Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state J. Am. Chem. Soc. 132 2010 10445 10452
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10445-10452
    • Hong, J.1    Gierasch, L.M.2
  • 60
    • 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
  • 61
    • 0027724892 scopus 로고
    • Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator
    • K.T. Hughes, K.L. Gillen, M.J. Semon, and J.E. Karlinsey Sensing structural intermediates in bacterial flagellar assembly by export of a negative regulator Science 262 1993 1277 1280
    • (1993) Science , vol.262 , pp. 1277-1280
    • Hughes, K.T.1    Gillen, K.L.2    Semon, M.J.3    Karlinsey, J.E.4
  • 62
    • 0030980926 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28
    • G.W. Daughdrill, M.S. Chadsey, J.E. Karlinsey, K.T. Hughes, and F.W. Dahlquist The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28 Nat. Struct. Biol. 4 1997 285 291
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 285-291
    • Daughdrill, G.W.1    Chadsey, M.S.2    Karlinsey, J.E.3    Hughes, K.T.4    Dahlquist, F.W.5
  • 63
    • 0032570318 scopus 로고    scopus 로고
    • The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations
    • G.W. Daughdrill, L.J. Hanely, and F.W. Dahlquist The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations Biochemistry 37 1998 1076 1082
    • (1998) Biochemistry , vol.37 , pp. 1076-1082
    • Daughdrill, G.W.1    Hanely, L.J.2    Dahlquist, F.W.3
  • 64
    • 1842766125 scopus 로고    scopus 로고
    • Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation
    • M.K. Sorenson, S.S. Ray, and S.A. Darst Crystal structure of the flagellar sigma/anti-sigma complex sigma(28)/FlgM reveals an intact sigma factor in an inactive conformation Mol. Cell 14 2004 127 138
    • (2004) Mol. Cell , vol.14 , pp. 127-138
    • Sorenson, M.K.1    Ray, S.S.2    Darst, S.A.3
  • 66
    • 67649635978 scopus 로고    scopus 로고
    • Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity
    • T. Vavouri, J.I. Semple, R. Garcia-Verdugo, and B. Lehner Intrinsic protein disorder and interaction promiscuity are widely associated with dosage sensitivity Cell 138 2009 198 208
    • (2009) Cell , vol.138 , pp. 198-208
    • Vavouri, T.1    Semple, J.I.2    Garcia-Verdugo, R.3    Lehner, B.4
  • 67
    • 57149116929 scopus 로고    scopus 로고
    • Tight regulation of unstructured proteins: From transcript synthesis to protein degradation
    • J. Gsponer, M.E. Futschik, S.A. Teichmann, and M.M. Babu Tight regulation of unstructured proteins: from transcript synthesis to protein degradation Science 322 2008 1365 1368
    • (2008) Science , vol.322 , pp. 1365-1368
    • Gsponer, J.1    Futschik, M.E.2    Teichmann, S.A.3    Babu, M.M.4
  • 68
    • 0032190622 scopus 로고    scopus 로고
    • The flagellar anti-sigma factor FlgM actively dissociates Salmonella typhimurium sigma28 RNA polymerase holoenzyme
    • M.S. Chadsey, J.E. Karlinsey, and K.T. Hughes The flagellar anti-sigma factor FlgM actively dissociates Salmonella typhimurium sigma28 RNA polymerase holoenzyme Genes Dev. 12 1998 3123 3136
    • (1998) Genes Dev. , vol.12 , pp. 3123-3136
    • Chadsey, M.S.1    Karlinsey, J.E.2    Hughes, K.T.3
  • 69
    • 77950158041 scopus 로고    scopus 로고
    • Generalized fundamental measure theory for atomistic modeling of macromolecular crowding
    • S. Qin, and H.X. Zhou Generalized fundamental measure theory for atomistic modeling of macromolecular crowding Phys. Rev. E 81 2010 031919
    • (2010) Phys. Rev. e , vol.81 , pp. 031919
    • Qin, S.1    Zhou, H.X.2
  • 70
    • 0023758314 scopus 로고
    • Effects of macromolecular crowding on the association of E. coli ribosomal particles
    • S.B. Zimmerman, and S.O. Trach Effects of macromolecular crowding on the association of E. coli ribosomal particles Nucleic Acids Res. 16 1988 6309 6326
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6309-6326
    • Zimmerman, S.B.1    Trach, S.O.2
  • 71
    • 0024992188 scopus 로고
    • "Macromolecular crowding": Thermodynamic consequences for protein-protein interactions within the T4 DNA replication complex
    • T.C. Jarvis, D.M. Ring, S.S. Daube, and P.H. von Hippel "Macromolecular crowding": thermodynamic consequences for protein-protein interactions within the T4 DNA replication complex J. Biol. Chem. 265 1990 15160 15167
    • (1990) J. Biol. Chem. , vol.265 , pp. 15160-15167
    • Jarvis, T.C.1    Ring, D.M.2    Daube, S.S.3    Von Hippel, P.H.4
  • 72
    • 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
  • 73
    • 68949110044 scopus 로고    scopus 로고
    • Atomistic modeling of macromolecular crowding predicts modest increases in protein folding and binding stability
    • S. Qin, and H.-X. Zhou Atomistic modeling of macromolecular crowding predicts modest increases in protein folding and binding stability Biophys. J. 97 2009 12 19
    • (2009) Biophys. J. , vol.97 , pp. 12-19
    • Qin, S.1    Zhou, H.-X.2
  • 74
    • 77956645458 scopus 로고    scopus 로고
    • Macromolecular crowding converts the human recombinant PrPC to the soluble neurotoxic beta-oligomers
    • L.Q. Huang, R. Jin, J.R. Li, K. Luo, T. Huang, D. Wu, W.X. Wang, R. Chen, and G.F. Xiao Macromolecular crowding converts the human recombinant PrPC to the soluble neurotoxic beta-oligomers FASEB J. 24 2010 3536 3543
    • (2010) FASEB J. , vol.24 , pp. 3536-3543
    • Huang, L.Q.1    Jin, R.2    Li, J.R.3    Luo, K.4    Huang, T.5    Wu, D.6    Wang, W.X.7    Chen, R.8    Xiao, G.F.9
  • 76
    • 22144435939 scopus 로고    scopus 로고
    • Protein self-association induced by macromolecular crowding: A quantitative analysis by magnetic relaxation dispersion
    • K. Snoussi, and B. Halle Protein self-association induced by macromolecular crowding: a quantitative analysis by magnetic relaxation dispersion Biophys. J. 88 2005 2855 2866
    • (2005) Biophys. J. , vol.88 , pp. 2855-2866
    • Snoussi, K.1    Halle, B.2
  • 77
    • 79953697415 scopus 로고    scopus 로고
    • Macromolecular crowding extended to a heptameric system: The co-chaperonin protein 10
    • X. Aguilar, C.F. Weise, T. Sparrman, M. Wolf-Watz, and P. Wittung-Stafshede Macromolecular crowding extended to a heptameric system: the co-chaperonin protein 10 Biochemistry 50 2011 3034 3044
    • (2011) Biochemistry , vol.50 , pp. 3034-3044
    • Aguilar, X.1    Weise, C.F.2    Sparrman, T.3    Wolf-Watz, M.4    Wittung-Stafshede, P.5
  • 78
    • 79551676332 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on the inhibition of virus assembly and virus-cell receptor recognition
    • V. Rincon, R. Bocanegra, A. Rodriguez-Huete, G. Rivas, and M.G. Mateu Effects of macromolecular crowding on the inhibition of virus assembly and virus-cell receptor recognition Biophys. J. 100 2011 738 746
    • (2011) Biophys. J. , vol.100 , pp. 738-746
    • Rincon, V.1    Bocanegra, R.2    Rodriguez-Huete, A.3    Rivas, G.4    Mateu, M.G.5
  • 79
    • 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
  • 80
    • 33646536078 scopus 로고    scopus 로고
    • The influence of macromolecular crowding on HIV-1 protease internal dynamics
    • D.D. Minh, C.E. Chang, J. Trylska, V. Tozzini, and J.A. McCammon The influence of macromolecular crowding on HIV-1 protease internal dynamics J. Am. Chem. Soc. 128 2006 6006 6007
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 6006-6007
    • Minh, D.D.1    Chang, C.E.2    Trylska, J.3    Tozzini, V.4    McCammon, J.A.5
  • 81
    • 78650080825 scopus 로고    scopus 로고
    • Macromolecular crowding effects on protein-protein binding affinity and specificity
    • Y.C. Kim, R.B. Best, and J. Mittal Macromolecular crowding effects on protein-protein binding affinity and specificity J. Chem. Phys. 133 2010 205101
    • (2010) J. Chem. Phys. , vol.133 , pp. 205101
    • Kim, Y.C.1    Best, R.B.2    Mittal, J.3
  • 82
    • 77049106311 scopus 로고    scopus 로고
    • Dependence of protein folding stability and dynamics on the density and composition of macromolecular crowders
    • J. Mittal, and R.B. Best Dependence of protein folding stability and dynamics on the density and composition of macromolecular crowders Biophys. J. 98 2010 315 320
    • (2010) Biophys. J. , vol.98 , pp. 315-320
    • Mittal, J.1    Best, R.B.2
  • 83
    • 77149164191 scopus 로고    scopus 로고
    • Method to predict crowding effects by postprocessing molecular dynamics trajectories: Application to the flap dynamics of HIV-1 protease
    • S. Qin, D.D. Minh, J.A. McCammon, and H.X. Zhou Method to predict crowding effects by postprocessing molecular dynamics trajectories: application to the flap dynamics of HIV-1 protease J. Phys. Chem. Lett. 1 2010 107 110
    • (2010) J. Phys. Chem. Lett. , vol.1 , pp. 107-110
    • Qin, S.1    Minh, D.D.2    McCammon, J.A.3    Zhou, H.X.4
  • 84
    • 77950792003 scopus 로고    scopus 로고
    • Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm
    • S.R. McGuffee, and A.H. Elcock Diffusion, crowding & protein stability in a dynamic molecular model of the bacterial cytoplasm PLoS Comput. Biol. 6 2010 e1000694
    • (2010) PLoS Comput. Biol. , vol.6 , pp. 1000694
    • McGuffee, S.R.1    Elcock, A.H.2
  • 85
    • 84855848788 scopus 로고    scopus 로고
    • Variable interactions between protein crowders and biomolecular solutes are important in understanding cellular crowding
    • M. Feig, and Y. Sugita Variable interactions between protein crowders and biomolecular solutes are important in understanding cellular crowding J. Phys. Chem. B. 116 2012 599 605
    • (2012) J. Phys. Chem. B. , vol.116 , pp. 599-605
    • Feig, M.1    Sugita, Y.2
  • 86
    • 84876055112 scopus 로고    scopus 로고
    • Folding free energy surfaces of three small proteins under crowding: Validation of the postprocessing method by direct simulation
    • S. Qin, J. Mittal, and H.X. Zhou Folding free energy surfaces of three small proteins under crowding: validation of the postprocessing method by direct simulation Phys. Biol. 10 2013
    • (2013) Phys. Biol. , vol.10
    • Qin, S.1    Mittal, J.2    Zhou, H.X.3
  • 87
    • 77952775472 scopus 로고    scopus 로고
    • The folding transition-state ensemble of a four-helix bundle protein: Helix propensity as a determinant and macromolecular crowding as a probe
    • H. Tjong, and H.X. Zhou The folding transition-state ensemble of a four-helix bundle protein: helix propensity as a determinant and macromolecular crowding as a probe Biophys. J. 98 2010 2273 2280
    • (2010) Biophys. J. , vol.98 , pp. 2273-2280
    • Tjong, H.1    Zhou, H.X.2


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