메뉴 건너뛰기




Volumn 6, Issue 4, 2008, Pages 681-691

Search for folding initiation sites from amino acid sequence

Author keywords

Amyloid fibril; Amyloidogenic regions; Folding nucleus; Protein folding; Protein misfolding; Transition state

Indexed keywords

AMINO ACID; AMYLOID; AMYLOID PROTEIN; APOMYOGLOBIN; RIBONUCLEASE A;

EID: 51749109104     PISSN: 02197200     EISSN: None     Source Type: Journal    
DOI: 10.1142/S021972000800362X     Document Type: Conference Paper
Times cited : (6)

References (41)
  • 1
    • 0024358426 scopus 로고
    • Mapping the transition state and pathway of protein folding by protein engineering
    • Matouschek A, Kellis JT Jr, Serrano L, Fersht AR, Mapping the transition state and pathway of protein folding by protein engineering, Nature 340(6229): 122-126, 1989.
    • (1989) Nature , vol.340 , Issue.6229 , pp. 122-126
    • Matouschek, A.1    Kellis Jr, J.T.2    Serrano, L.3    Fersht, A.R.4
  • 2
    • 0025698613 scopus 로고
    • Transient folding intermediates characterized by protein engineering
    • Matouschek A, Kellis JT Jr, Serrano L, Bycroft M, Fersht AR, Transient folding intermediates characterized by protein engineering, Nature 346(6283):440-445, 1990.
    • (1990) Nature , vol.346 , Issue.6283 , pp. 440-445
    • Matouschek, A.1    Kellis Jr, J.T.2    Serrano, L.3    Bycroft, M.4    Fersht, A.R.5
  • 3
    • 0037818986 scopus 로고
    • The proteins of the mammalian epidermis
    • Rudall KM, The proteins of the mammalian epidermis, Adv Protein Chem 7:253-290, 1952.
    • (1952) Adv Protein Chem , vol.7 , pp. 253-290
    • Rudall, K.M.1
  • 8
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • FandrichM, Fletcher MA, Dobson CM, Amyloid fibrils from muscle myoglobin, Nature 410(6825):165-166, 2001.
    • (2001) Nature , vol.410 , Issue.6825 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 9
    • 0028958601 scopus 로고
    • Characterizing transition states in protein folding: An essential step in the puzzle
    • Fersht AR, Characterizing transition states in protein folding: An essential step in the puzzle, Curr Opin Struct Biol 5 (1):79-84, 1995.
    • (1995) Curr Opin Struct Biol , vol.5 , Issue.1 , pp. 79-84
    • Fersht, A.R.1
  • 10
    • 0031043161 scopus 로고    scopus 로고
    • Nucleation mechanisms in protein folding
    • Fersht AR, Nucleation mechanisms in protein folding, Curr Opin Struct Biol 7(1):3-9, 1997.
    • (1997) Curr Opin Struct Biol , vol.7 , Issue.1 , pp. 3-9
    • Fersht, A.R.1
  • 11
    • 0029670994 scopus 로고    scopus 로고
    • Conserved residues and the mechanism of protein folding
    • Shakhnovich E, Abkevich V, Ptitsyn O, Conserved residues and the mechanism of protein folding, Nature 379(6560):96-98, 1996.
    • (1996) Nature , vol.379 , Issue.6560 , pp. 96-98
    • Shakhnovich, E.1    Abkevich, V.2    Ptitsyn, O.3
  • 12
    • 0031867090 scopus 로고    scopus 로고
    • A strategy for detecting the conservation of folding-nucleus residues in protein superfamilies
    • Michnick SW, Shakhnovich E, A strategy for detecting the conservation of folding-nucleus residues in protein superfamilies, Fold Des 3 (4):239-251, 1998.
    • (1998) Fold Des , vol.3 , Issue.4 , pp. 239-251
    • Michnick, S.W.1    Shakhnovich, E.2
  • 13
    • 0029981188 scopus 로고    scopus 로고
    • Structure of the transition state for folding of a protein derived from experiment and simulation
    • Daggett V, Li A, Itzhaki LS, Otzen DE, Fersht AR, Structure of the transition state for folding of a protein derived from experiment and simulation, J Mol Biol 257(2):430-440, 1996.
    • (1996) J Mol Biol , vol.257 , Issue.2 , pp. 430-440
    • Daggett, V.1    Li, A.2    Itzhaki, L.S.3    Otzen, D.E.4    Fersht, A.R.5
  • 14
    • 0029124153 scopus 로고
    • Acid and thermal denaturation of barnase investigated by molecular dynamics simulations
    • Caflisch A, Karplus M, Acid and thermal denaturation of barnase investigated by molecular dynamics simulations, J Mol Biol 252 (5):672-708, 1995.
    • (1995) J Mol Biol , vol.252 , Issue.5 , pp. 672-708
    • Caflisch, A.1    Karplus, M.2
  • 16
    • 0033613131 scopus 로고    scopus 로고
    • A theoretical search for folding/ unfolding nuclei in three-dimensional protein structures
    • Galzitskaya OV, Finkelstein AV, A theoretical search for folding/ unfolding nuclei in three-dimensional protein structures, Proc Natl Acad Sci USA 96(20):11299-11304, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.20 , pp. 11299-11304
    • Galzitskaya, O.V.1    Finkelstein, A.V.2
  • 17
    • 0033613255 scopus 로고    scopus 로고
    • Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures
    • Alm E, Baker D, Prediction of protein-folding mechanisms from free-energy landscapes derived from native structures, Proc Natl Acad Sci USA 96(20):11305-11310, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.20 , pp. 11305-11310
    • Alm, E.1    Baker, D.2
  • 18
    • 0033613165 scopus 로고    scopus 로고
    • A simple model for calculating the kinetics of protein folding from three-dimensional structures
    • Munoz V, Eaton WA, A simple model for calculating the kinetics of protein folding from three-dimensional structures, Proc Natl Acad Sci USA 96(20):11311-11316, 1999.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.20 , pp. 11311-11316
    • Munoz, V.1    Eaton, W.A.2
  • 20
    • 0036295640 scopus 로고    scopus 로고
    • Sensitivity of folding pathway to the details of amino-acid sequence
    • Galzitskaya OV, Sensitivity of folding pathway to the details of amino-acid sequence, Mol Biol (Mosk) 36(3):386-390, 2002.
    • (2002) Mol Biol (Mosk) , vol.36 , Issue.3 , pp. 386-390
    • Galzitskaya, O.V.1
  • 21
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE, Intrinsically unstructured proteins and their functions, Nat Rev Mol Cell Biol 6(3):197-208, 2005.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 22
    • 0345304461 scopus 로고    scopus 로고
    • Origin of unusual φ-values in protein folding: Evidence against specific nucleation sites
    • Sánchez IE, Kiefhaber T, Origin of unusual φ-values in protein folding: Evidence against specific nucleation sites, J Mol Biol 334(5):1077-1085, 2003.
    • (2003) J Mol Biol , vol.334 , Issue.5 , pp. 1077-1085
    • Sánchez, I.E.1    Kiefhaber, T.2
  • 23
    • 33748349224 scopus 로고    scopus 로고
    • The role of hydrophobic interactions in initiation and propagation of protein folding
    • Dyson HJ, Wright PE, Scheraga HA, The role of hydrophobic interactions in initiation and propagation of protein folding, Proc Natl Acad Sci USA 103(35):13057-13061, 2006.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.35 , pp. 13057-13061
    • Dyson, H.J.1    Wright, P.E.2    Scheraga, H.A.3
  • 24
    • 33748314477 scopus 로고    scopus 로고
    • High polar content of long buried blocks of sequence in protein domains suggests selection against amyloidogenic non-polar sequences
    • Patki AU, Hausrath AC, Cordes MH, High polar content of long buried blocks of sequence in protein domains suggests selection against amyloidogenic non-polar sequences, J Mol Biol 362 (4):800-809, 2006.
    • (2006) J Mol Biol , vol.362 , Issue.4 , pp. 800-809
    • Patki, A.U.1    Hausrath, A.C.2    Cordes, M.H.3
  • 25
    • 33845990277 scopus 로고    scopus 로고
    • Prediction of amyloidogenic and disordered regions in protein chains
    • Galzitskaya OV, Garbuzynskiy SO, Lobanov MY, Prediction of amyloidogenic and disordered regions in protein chains, PLoS Comput Biol 2 (12):e177, 2006.
    • (2006) PLoS Comput Biol , vol.2 , Issue.12
    • Galzitskaya, O.V.1    Garbuzynskiy, S.O.2    Lobanov, M.Y.3
  • 26
    • 33747845657 scopus 로고    scopus 로고
    • Entropic criteria for protein folding derived from recurrences: Six residues patch as the basic protein word
    • Zbilut JP, Chua GH, Krishnan A, Bossa C, Colafranceschi M, Giuliani A, Entropic criteria for protein folding derived from recurrences: Six residues patch as the basic protein word, FEBS Lett 580 (20):4861-4864, 2006.
    • (2006) FEBS Lett , vol.580 , Issue.20 , pp. 4861-4864
    • Zbilut, J.P.1    Chua, G.H.2    Krishnan, A.3    Bossa, C.4    Colafranceschi, M.5    Giuliani, A.6
  • 29
    • 33745712610 scopus 로고    scopus 로고
    • Galzitskaya OV, Garbuzynskiy SO, Lobanov MY, is it possible to predict amyloidogenic regions from sequence alone?, J Bioinform Comput Biol 4(2):373-388, 2006.
    • Galzitskaya OV, Garbuzynskiy SO, Lobanov MY, is it possible to predict amyloidogenic regions from sequence alone?, J Bioinform Comput Biol 4(2):373-388, 2006.
  • 31
    • 0024293204 scopus 로고
    • Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding
    • Wright PE, Dyson HJ, Lerner RA, Conformation of peptide fragments of proteins in aqueous solution: Implications for initiation of protein folding, Biochemistry 27(19):7167-7175, 1988.
    • (1988) Biochemistry , vol.27 , Issue.19 , pp. 7167-7175
    • Wright, P.E.1    Dyson, H.J.2    Lerner, R.A.3
  • 32
    • 0025370815 scopus 로고
    • Dominant forces on protein folding
    • Dill KA, Dominant forces on protein folding, Biochemistry 29 (31):7133-7155, 1990.
    • (1990) Biochemistry , vol.29 , Issue.31 , pp. 7133-7155
    • Dill, K.A.1
  • 33
    • 0242321015 scopus 로고    scopus 로고
    • Role of the B helix in early folding events in apomyoglobin: Evidence from site-directed mutagenesis for native-like long range interactions
    • Nishimura C, Wright PE, Dyson HJ, Role of the B helix in early folding events in apomyoglobin: Evidence from site-directed mutagenesis for native-like long range interactions, J Mol Biol 334 (2):293-307, 2003.
    • (2003) J Mol Biol , vol.334 , Issue.2 , pp. 293-307
    • Nishimura, C.1    Wright, P.E.2    Dyson, H.J.3
  • 34
    • 22444443996 scopus 로고    scopus 로고
    • Sequence determinants of a protein folding pathway
    • Nishimura C, Lietzow MA, Dyson HJ, Wright PE, Sequence determinants of a protein folding pathway, J Mol Biol 351(2):383-392, 2005.
    • (2005) J Mol Biol , vol.351 , Issue.2 , pp. 383-392
    • Nishimura, C.1    Lietzow, M.A.2    Dyson, H.J.3    Wright, P.E.4
  • 35
    • 33947091990 scopus 로고
    • A method for predicting nucleation sites for protein folding based on hydrophobic contacts
    • Matheson RR Jr, Scheraga HA, A method for predicting nucleation sites for protein folding based on hydrophobic contacts, Macromolecules 11:819-829, 1978.
    • (1978) Macromolecules , vol.11 , pp. 819-829
    • Matheson Jr, R.R.1    Scheraga, H.A.2
  • 36
    • 0019052221 scopus 로고
    • Hydrophobic basis of packing in globular proteins
    • Rose GD, Roy S, Hydrophobic basis of packing in globular proteins, Proc Natl Acad Sci USA 77(8):4643-4647, 1980.
    • (1980) Proc Natl Acad Sci USA , vol.77 , Issue.8 , pp. 4643-4647
    • Rose, G.D.1    Roy, S.2
  • 37
    • 0017474001 scopus 로고
    • Hypothesis about the mechanism of protein folding
    • Tanaka S, Scheraga HA, Hypothesis about the mechanism of protein folding, Macromolecules 10(2):291-304, 1977.
    • (1977) Macromolecules , vol.10 , Issue.2 , pp. 291-304
    • Tanaka, S.1    Scheraga, H.A.2
  • 38
    • 0018589605 scopus 로고
    • A possible folding pathway of bovine pancreatic RNase
    • Nemethy G, Scheraga HA, A possible folding pathway of bovine pancreatic RNase, Proc Natl Acad Sci USA 76(12):6050-6054, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , Issue.12 , pp. 6050-6054
    • Nemethy, G.1    Scheraga, H.A.2
  • 39
    • 0022092307 scopus 로고    scopus 로고
    • Gerritsen M, Chou KC, Nemethy G, Scheraga HA, Energetics of multihelix interactions in protein folding: Application to myoglobin, Biopolymers 24(7):1271-1291, 1985. Erraturn 24:2177, 2005.
    • Gerritsen M, Chou KC, Nemethy G, Scheraga HA, Energetics of multihelix interactions in protein folding: Application to myoglobin, Biopolymers 24(7):1271-1291, 1985. Erraturn 24:2177, 2005.
  • 40
    • 0025186451 scopus 로고
    • Structural characterization of a partly folded apomyoglobin intermediate
    • Hughson FM, Wright PE, Baldwin RL, Structural characterization of a partly folded apomyoglobin intermediate, Science 249 (4976):1544-1548, 1990.
    • (1990) Science , vol.249 , Issue.4976 , pp. 1544-1548
    • Hughson, F.M.1    Wright, P.E.2    Baldwin, R.L.3
  • 41
    • 0027749370 scopus 로고
    • Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
    • Jennings PA, Wright PE, Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin, Science 262 (5135):892-896, 1993.
    • (1993) Science , vol.262 , Issue.5135 , pp. 892-896
    • Jennings, P.A.1    Wright, P.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.