ATP-Bound States of GroEL Captured by Cryo-Electron Microscopy
Tài liệu tham khảo
Boisvert, 1996, The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPgS, Nat. Struct. Biol., 3, 170, 10.1038/nsb0296-170
Böttcher, 1997, Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy, Nature, 386, 88, 10.1038/386088a0
Braig, 1994, The crystal structure of the bacterial chaperonin GroEL at 2.8 Å, Nature, 371, 578, 10.1038/371578a0
Bukau, 1998, The Hsp70 and Hsp60 chaperone machines, Cell, 92, 351, 10.1016/S0092-8674(00)80928-9
Burston, 1995, The origins and consequences of asymmetry in the chaperonin reaction cycle, J. Mol. Biol., 249, 138, 10.1006/jmbi.1995.0285
Burston, 1996, Release of both native and non-native proteins from a cis-only GroEL ternary complex, Nature, 383, 96, 10.1038/383096a0
Chandrasekhar, 1986, Purification and properties of the groES morphogenetic protein of Escherichia coli., J. Biol. Chem., 261, 12414, 10.1016/S0021-9258(18)67256-4
Chen, 2001, Folding of malate dehydrogenase inside the GroEL–GroES cavity, Nat. Struct. Biol., 8, 721, 10.1038/90443
Cliff, 1999, A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL, J. Mol. Biol., 293, 667, 10.1006/jmbi.1999.3138
Conway, 1997, Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy, Nature, 386, 91, 10.1038/386091a0
Crowther, 1996, MRC image processing programs, J. Struct. Biol., 116, 9, 10.1006/jsbi.1996.0003
Dubochet, 1988, Cryo-electron microscopy of vitrified specimens, Q. Rev. Biophys., 21, 129, 10.1017/S0033583500004297
Esnouf, 1997, An extensively modified version of Molscript that includes greatly enhanced coloring capabilities, J. Mol. Graph., 15, 132, 10.1016/S1093-3263(97)00021-1
Farr, 2000, Multivalent binding of non-native substrate proteins by the chaperonin GroEL, Cell, 100, 561, 10.1016/S0092-8674(00)80692-3
Fenton, 1994, Residues in chaperonin GroEL required for polypeptide binding and release, Nature, 371, 614, 10.1038/371614a0
Frank, 1996, SPIDER and WEB; processing and visualization of images in 3D electron microscopy and related fields, J. Struct. Biol., 116, 190, 10.1006/jsbi.1996.0030
Gray, 1991, Cooperativity in ATP hydrolysis by GroEL is increased by GroES, FEBS Lett., 292, 254, 10.1016/0014-5793(91)80878-7
Hartl, 1996, Molecular chaperones in cellular protein folding, Nature, 381, 571, 10.1038/381571a0
Jackson, 1993, Binding and hydrolysis of nucleotide1s in the chaperonin catalytic cycle, Biochemistry, 32, 2554, 10.1021/bi00061a013
Jones, 1991, Improved methods for building models in electron density maps and the location of errors in these models, Acta Crystallogr. A, 47, 110, 10.1107/S0108767390010224
Kad, 1998, Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings, J. Mol. Biol., 278, 267, 10.1006/jmbi.1998.1704
Kantrowitz, 1990, Escherichia coli aspartate transcarbamoylase, Trends Biochem. Sci., 15, 53, 10.1016/0968-0004(90)90176-C
Kraulis, 1991, Molscript - a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr., 24, 946, 10.1107/S0021889891004399
Ma, 2000, A dynamic model for the allosteric mechanism of GroEL, J. Mol. Biol., 302, 303, 10.1006/jmbi.2000.4014
Mayhew, 1996, Protein folding in the central cavity of the GroEL-GroES chaperonin complex, Nature, 379, 420, 10.1038/379420a0
Merritt, 1994, Raster3d version-2.0 - a program for photorealistic molecular graphics, Acta Crystallogr. D, 50, 869, 10.1107/S0907444994006396
Ranson, 1998, Chaperonins, Biochem. J., 333, 233, 10.1042/bj3330233
Roseman, 2000, Docking structures of domains into maps from cryo-electron microscopy using local correlation, Acta Crystallogr. D, 56, 1332, 10.1107/S0907444900010908
Roseman, 1996, The chaperonin ATPase cycle, Cell, 87, 241, 10.1016/S0092-8674(00)81342-2
Roseman, 2001, The ATP-bound state of the E. coli chaperonin GroEL studied by Cryo-Electron Microscopy, J. Struct. Biol., 135, 115, 10.1006/jsbi.2001.4374
Rye, 1997, Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL, Nature, 388, 792, 10.1038/42047
Rye, 1999, GroEL-GroES cycling, Cell, 97, 325, 10.1016/S0092-8674(00)80742-4
Shtilerman, 1999, Chaperonin function, Science, 284, 822, 10.1126/science.284.5415.822
Sigler, 1998, Structure and function in GroEL-mediated protein folding, Annu. Rev. Biochem., 67, 581, 10.1146/annurev.biochem.67.1.581
Staniforth, 1994, Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and GroES, Biochem. J., 300, 651, 10.1042/bj3000651
Todd, 1994, Dynamics of the chaperonin ATPase cycle, Science, 265, 659, 10.1126/science.7913555
van Heel, 1996, A new generation of the IMAGIC image processing system, J. Struct. Biol., 116, 17, 10.1006/jsbi.1996.0004
Wang, 1998, Energy transduction in the F1 motor of ATP synthase, Nature, 396, 279, 10.1038/24409
Weissman, 1995, Mechanism of GroEL action, Cell, 83, 577, 10.1016/0092-8674(95)90098-5
Weissman, 1996, Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction, Cell, 84, 481, 10.1016/S0092-8674(00)81293-3
White, 1997, Structural basis of allosteric changes in the GroEL mutant Arg197→Ala, Nat. Struct. Biol., 4, 690, 10.1038/nsb0997-690
Xu, 1997, The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex, Nature, 388, 741, 10.1038/41944
Yifrach, 1994, Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala, J. Mol. Biol., 243, 397, 10.1006/jmbi.1994.1667
Yifrach, 1995, Nested co-operativity in the ATPase activity of the oligomeric chaperonin GroEL, Biochemistry, 34, 5303, 10.1021/bi00016a001
Yifrach, 1998, Mapping the transition state of the allosteric pathway of GroEL by protein engineering, J. Am. Chem. Soc., 120, 13262, 10.1021/ja983136u
Yifrach, 1998, Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL, Biochemistry, 37, 7083, 10.1021/bi980370o