메뉴 건너뛰기




Volumn 8, Issue 6, 2012, Pages

The role of non-native interactions in the folding of knotted proteins

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; COARSE-GRAINED MODELING; ENZYMES; STOCHASTIC MODELS;

EID: 84864054045     PISSN: 1553734X     EISSN: 15537358     Source Type: Journal    
DOI: 10.1371/journal.pcbi.1002504     Document Type: Article
Times cited : (53)

References (55)
  • 3
    • 0028421135 scopus 로고
    • Are there knots in proteins?
    • Mansfield ML, (1994) Are there knots in proteins? Nature Struct Biol 1: 213-214.
    • (1994) Nature Struct Biol , vol.1 , pp. 213-214
    • Mansfield, M.L.1
  • 5
    • 0034710671 scopus 로고    scopus 로고
    • A deeply knotted protein structure and how it might fold
    • Taylor WR, (2000) A deeply knotted protein structure and how it might fold. Nature 406: 916-919.
    • (2000) Nature , vol.406 , pp. 916-919
    • Taylor, W.R.1
  • 7
    • 0036774065 scopus 로고    scopus 로고
    • The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot
    • Michel G, Sauve V, Larocque R, Li Y, Matte A, Cygler M, (2002) The structure of the RlmB 23S rRNA methyltransferase reveals a new methyltransferase fold with a unique knot. Structure 10: 1303-1315.
    • (2002) Structure , vol.10 , pp. 1303-1315
    • Michel, G.1    Sauve, V.2    Larocque, R.3    Li, Y.4    Matte, A.5    Cygler, M.6
  • 8
    • 0037413604 scopus 로고    scopus 로고
    • A tangled problem
    • Taylor WR, Lin K, (2003) A tangled problem. Nature 421: 25.
    • (2003) Nature , vol.421 , pp. 25
    • Taylor, W.R.1    Lin, K.2
  • 9
    • 33646904782 scopus 로고    scopus 로고
    • Statistics of knots, geometry of conformations, and evolution of proteins
    • Lua RC, Grosberg AY, (2006) Statistics of knots, geometry of conformations, and evolution of proteins. PLoS Comput Biol 2: e45.
    • (2006) PLoS Comput Biol , vol.2
    • Lua, R.C.1    Grosberg, A.Y.2
  • 10
    • 0039051533 scopus 로고
    • Knotting problems in biology
    • In: Bellman RE, editors, Providence, Rhode Island, American Mathematical Society
    • Delbruck M, (1962) Knotting problems in biology. In: Bellman RE, editors. Mathematical Problems in the Biological Sciences Proceedings of Symposia in Applied Mathematics 14 Providence, Rhode Island American Mathematical Society: 55-63.
    • (1962) Mathematical Problems in the Biological Sciences , vol.14 , pp. 55-63
    • Delbruck, M.1
  • 16
    • 0023044418 scopus 로고
    • On the topology of a polymer ring
    • Michels JPG, Wiegel FW, (1986) On the topology of a polymer ring. Proc R Soc Lond A403: 269-284.
    • (1986) Proc R Soc Lond , vol.A403 , pp. 269-284
    • Michels, J.P.G.1    Wiegel, F.W.2
  • 17
    • 79955651124 scopus 로고    scopus 로고
    • Polymers with spatial or topological constraints: Theoretical and computational results
    • Micheletti C, Marenduzzo D, Orlandini E, (2011) Polymers with spatial or topological constraints: Theoretical and computational results. Phys Rep 504: 1.
    • (2011) Phys Rep , vol.504 , pp. 1
    • Micheletti, C.1    Marenduzzo, D.2    Orlandini, E.3
  • 18
    • 76149131390 scopus 로고    scopus 로고
    • DNA-DNA interactions in bacteriophage capsids are responsible for the observed DNA knotting
    • Marenduzzo D, Orlandini E, Stasiak A, Sumners DW, Tubiana L, et al. (2009) DNA-DNA interactions in bacteriophage capsids are responsible for the observed DNA knotting. Proc Natl Acad Sci U S A 106: 22269-22274.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 22269-22274
    • Marenduzzo, D.1    Orlandini, E.2    Stasiak, A.3    Sumners, D.W.4    Tubiana, L.5
  • 19
    • 34248570354 scopus 로고    scopus 로고
    • Protein knots and fold complexity: some new twists
    • Taylor WR, (2007) Protein knots and fold complexity: some new twists. Comput Biol Chem 31: 151-162.
    • (2007) Comput Biol Chem , vol.31 , pp. 151-162
    • Taylor, W.R.1
  • 20
    • 84856113243 scopus 로고    scopus 로고
    • Knot formation in newly translated proteins is spontaneous and accelerated by chaperonins
    • Mallam AL, Jackson SE, (2012) Knot formation in newly translated proteins is spontaneous and accelerated by chaperonins. Nat Chem Biol 8: 147-53.
    • (2012) Nat Chem Biol , vol.8 , pp. 147-153
    • Mallam, A.L.1    Jackson, S.E.2
  • 22
    • 36549032188 scopus 로고    scopus 로고
    • Knotted and topologically complex proteins as models for studying folding and stability
    • Yeates TO, Norcross TS, King NP, (2007) Knotted and topologically complex proteins as models for studying folding and stability. Curr Opin Chem Biol 11: 595-603.
    • (2007) Curr Opin Chem Biol , vol.11 , pp. 595-603
    • Yeates, T.O.1    Norcross, T.S.2    King, N.P.3
  • 23
    • 58149174188 scopus 로고    scopus 로고
    • How does a knotted protein fold?
    • Mallam AL, (2009) How does a knotted protein fold? FEBS J 276: 365-375.
    • (2009) FEBS J , vol.276 , pp. 365-375
    • Mallam, A.L.1
  • 24
    • 78651511523 scopus 로고    scopus 로고
    • Structures and folding pathways of topologically knotted proteins
    • Virnau P, Mallam A, Jackson S, (2011) Structures and folding pathways of topologically knotted proteins. J Phys: Condens Matter 23: 33101-33118.
    • (2011) J Phys: Condens Matter , vol.23 , pp. 33101-33118
    • Virnau, P.1    Mallam, A.2    Jackson, S.3
  • 25
    • 77957259237 scopus 로고    scopus 로고
    • Slipknotting upon native-like loop formation in a trefoil knot protein
    • Noel JK, Sulkowska JI, Onuchic J, (2010) Slipknotting upon native-like loop formation in a trefoil knot protein. Proc Natl Acad Sci U S A 107: 15403-15408.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 15403-15408
    • Noel, J.K.1    Sulkowska, J.I.2    Onuchic, J.3
  • 26
    • 33749347406 scopus 로고    scopus 로고
    • Intricate knots in proteins: function and evolution
    • Virnau P, Mirny LA, Kardar M, (2006) Intricate knots in proteins: function and evolution. PLoS Comput Biol 2: e122.
    • (2006) PLoS Comput Biol , vol.2
    • Virnau, P.1    Mirny, L.A.2    Kardar, M.3
  • 27
    • 78049235694 scopus 로고    scopus 로고
    • Knotted vs. unknotted proteins: evidence of knot-promoting loops
    • Potestio R, Micheletti C, Orland H, (2010) Knotted vs. unknotted proteins: evidence of knot-promoting loops. PLoS Comput Biol 6: e1000864.
    • (2010) PLoS Comput Biol , vol.6
    • Potestio, R.1    Micheletti, C.2    Orland, H.3
  • 28
    • 79251514279 scopus 로고    scopus 로고
    • Protein folding: To knot or not to knot?
    • Shakhnovich E, (2011) Protein folding: To knot or not to knot? Nat Mater 10: 84-6.
    • (2011) Nat Mater , vol.10 , pp. 84-86
    • Shakhnovich, E.1
  • 29
    • 13844255609 scopus 로고    scopus 로고
    • Folding studies on a knotted protein
    • Mallam AL, Jackson SE, (2005) Folding studies on a knotted protein. J Mol Biol 346: 1409-1421.
    • (2005) J Mol Biol , vol.346 , pp. 1409-1421
    • Mallam, A.L.1    Jackson, S.E.2
  • 30
    • 33745163582 scopus 로고    scopus 로고
    • Probing Nature's knots: the folding pathway of a knotted homodimeric protein
    • Mallam AL, Jackson SE, (2006) Probing Nature's knots: the folding pathway of a knotted homodimeric protein. J Mol Biol 359: 1420-1436.
    • (2006) J Mol Biol , vol.359 , pp. 1420-1436
    • Mallam, A.L.1    Jackson, S.E.2
  • 31
    • 33846362515 scopus 로고    scopus 로고
    • A comparison of the folding of two knotted proteins: YbeA and YibK
    • Mallam AL, Jackson SE, (2006) A comparison of the folding of two knotted proteins: YbeA and YibK. J Mol Biol 366: 650-665.
    • (2006) J Mol Biol , vol.366 , pp. 650-665
    • Mallam, A.L.1    Jackson, S.E.2
  • 32
    • 44449146446 scopus 로고    scopus 로고
    • Knotted fusion proteins reveal unexpected possibilities in protein folding
    • Mallam AL, Jackson SE, (2008) Knotted fusion proteins reveal unexpected possibilities in protein folding. Mol Cell 30: 642-648.
    • (2008) Mol Cell , vol.30 , pp. 642-648
    • Mallam, A.L.1    Jackson, S.E.2
  • 34
    • 77952415889 scopus 로고    scopus 로고
    • Experimental detection of knotted conformations in denaturated proteins
    • Mallam AL, Rogers JM, Jackson SE, (2010) Experimental detection of knotted conformations in denaturated proteins. Proc Natl Acad Sci U S A 107: 8189-8194.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 8189-8194
    • Mallam, A.L.1    Rogers, J.M.2    Jackson, S.E.3
  • 38
  • 39
    • 70349983270 scopus 로고    scopus 로고
    • MISTRAL: a tool for energy-based multiple structural alignment of proteins
    • Micheletti C, Orland H, (2009) MISTRAL: a tool for energy-based multiple structural alignment of proteins. Bioinformatics 25: 2663-2669.
    • (2009) Bioinformatics , vol.25 , pp. 2663-2669
    • Micheletti, C.1    Orland, H.2
  • 41
    • 0000635457 scopus 로고
    • Fast Monte Carlo algorithms for knotted polymers
    • Quake SR, (1995) Fast Monte Carlo algorithms for knotted polymers. Phys Rev E 52: 1176-1180.
    • (1995) Phys Rev E , vol.52 , pp. 1176-1180
    • Quake, S.R.1
  • 44
    • 75749153687 scopus 로고    scopus 로고
    • Coordinate-dependent diffusion in protein folding
    • Best RB, Hummer G, (2010) Coordinate-dependent diffusion in protein folding. Proc Natl Acad Sci U S A 107: 1088-1093.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1088-1093
    • Best, R.B.1    Hummer, G.2
  • 45
    • 37549009571 scopus 로고    scopus 로고
    • Coarse-grained models for simulations of multi-protein complexes: application to ubiquitin binding
    • Kim YC, Hummer G, (2008) Coarse-grained models for simulations of multi-protein complexes: application to ubiquitin binding. J Mol Biol 375: 1416-1433.
    • (2008) J Mol Biol , vol.375 , pp. 1416-1433
    • Kim, Y.C.1    Hummer, G.2
  • 46
    • 0029919190 scopus 로고    scopus 로고
    • Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term for simulation and threading
    • Miyazawa S, Jernigan RL, (1996) Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term for simulation and threading. J Mol Biol 256: 623-644.
    • (1996) J Mol Biol , vol.256 , pp. 623-644
    • Miyazawa, S.1    Jernigan, R.L.2
  • 48
    • 0042510944 scopus 로고    scopus 로고
    • Contact order revisited: influence of protein size on the folding rate
    • Ivankov DN, Garbuzynskiy SO, Alm E, Plaxco KW, Baker D, et al. (2003) Contact order revisited: influence of protein size on the folding rate. Protein Sci 12: 2057-2062.
    • (2003) Protein Sci , vol.12 , pp. 2057-2062
    • Ivankov, D.N.1    Garbuzynskiy, S.O.2    Alm, E.3    Plaxco, K.W.4    Baker, D.5
  • 49
    • 0036785556 scopus 로고    scopus 로고
    • The origins of the asymmetry in the folding transition states of protein L and protein G
    • Karanicolas J, Brooks CL, (2002) The origins of the asymmetry in the folding transition states of protein L and protein G. Protein Sci 11: 2351-2361.
    • (2002) Protein Sci , vol.11 , pp. 2351-2361
    • Karanicolas, J.1    Brooks, C.L.2
  • 50
    • 0024034830 scopus 로고
    • Monte Carlo simulation of lattice models for macromolecules
    • Kremer K, Binder K, (1988) Monte Carlo simulation of lattice models for macromolecules. Comput Phys Rep 7: 259-310.
    • (1988) Comput Phys Rep , vol.7 , pp. 259-310
    • Kremer, K.1    Binder, K.2
  • 51
    • 5944256461 scopus 로고
    • The pivot algorithm: a highly efficient Monte Carlo method for the self-avoiding walk
    • Madras N, Sokal AE, (1988) The pivot algorithm: a highly efficient Monte Carlo method for the self-avoiding walk. J Stat Phys 50: 109-186.
    • (1988) J Stat Phys , vol.50 , pp. 109-186
    • Madras, N.1    Sokal, A.E.2
  • 52
    • 33748875167 scopus 로고    scopus 로고
    • Monte Carlo vs molecular dynamics for conformational sampling
    • Jorgensen WL, Tirado-Rives J, (1996) Monte Carlo vs molecular dynamics for conformational sampling. J Phys Chem 100: 14508-14513.
    • (1996) J Phys Chem , vol.100 , pp. 14508-14513
    • Jorgensen, W.L.1    Tirado-Rives, J.2
  • 53
    • 84855303314 scopus 로고    scopus 로고
    • Profiling the arc entanglement of compact ring polymers: a comparison of different arc-closure schemes with applications to knot localization
    • Tubiana L, Orlandini E, Micheletti C, (2011) Profiling the arc entanglement of compact ring polymers: a comparison of different arc-closure schemes with applications to knot localization. Prog Theor Phys 191: 192-204.
    • (2011) Prog Theor Phys , vol.191 , pp. 192-204
    • Tubiana, L.1    Orlandini, E.2    Micheletti, C.3
  • 54
    • 13244258252 scopus 로고    scopus 로고
    • Linear Random Knots and their Scaling Behaviour
    • Millett K, Dobay A, Stasiak A, (2005) Linear Random Knots and their Scaling Behaviour. Macromolecules 38: 601-606.
    • (2005) Macromolecules , vol.38 , pp. 601-606
    • Millett, K.1    Dobay, A.2    Stasiak, A.3
  • 55
    • 80054948313 scopus 로고    scopus 로고
    • Multiscale entanglement in ring polymers under spherical confinement
    • Tubiana L, Orlandini E, Micheletti C, (2011) Multiscale entanglement in ring polymers under spherical confinement. Phys Rev Lett 107: 188302.
    • (2011) Phys Rev Lett , vol.107 , pp. 188302
    • Tubiana, L.1    Orlandini, E.2    Micheletti, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.