DOI: 10.1006/jmbi.1999.3138. A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL 1 1Edited by A. R. Fersht

A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL 1 1Edited by A. R. Fersht

10.1006/jmbi.1999.3138

Crossref journal-article

Elsevier BV

Journal of Molecular Biology (78)

Bibliography

Cliff, M. J., Kad, N. M., Hay, N., Lund, P. A., Webb, M. R., Burston, S. G., & Clarke, A. R. (1999). A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL 1 1Edited by A. R. Fersht. Journal of Molecular Biology, 293(3), 667â684.

Authors 7

Matthew J Cliff (first)
Neil M Kad (additional)
Nicky Hay (additional)
Peter A Lund (additional)
Martin R Webb (additional)
Steven G Burston (additional)
Anthony R Clarke (additional)

References 54 Referenced 68

10.1021/bi00102a010 / Biochemistry / Binding of a chaperonin to the folding intermediates of lactate dehydrogenase by Badcoe (1991)
10.1016/S0021-9258(18)35659-X / J. Biol. Chem. / Positive cooperativity in the functioning of molecular chaperone GroEL by Bochkareva (1992)
10.1038/nsb0296-170 / Nature Struct. Biol. / The 2.4 Å crystal-structure of the bacterial chaperonin GroEL complexed with ATP-γ-S by Boisvert (1996)
10.1038/371578a0 / Nature / The crystal-structure of the bacterial chaperonin GroEL at 2.8-Å by Braig (1994)
10.1021/bi00193a013 / Biochemistry / Direct, real-time measurement of rapid inorganic-phosphate release using a novel fluorescent probe and its application to actomyosin subfragment-1 ATPase by Brune (1994)
10.1073/pnas.94.8.3571 / Proc. Natl Acad. Sci. USA / A structural model for GroEL-polypeptide recognition by Buckle (1997)
10.1006/jmbi.1995.0285 / J. Mol. Biol. / The origins and consequences of asymmetry in the chaperonin reaction cycle by Burston (1995)
10.1038/383096a0 / Nature / Release of both native and nonnative proteins from a cis-only GroEL ternary complex by Burston (1996)
10.1016/S0021-9258(18)67256-4 / J. Biol. Chem. / Purification and properties of the GroES morphogenetic protein of Escherichia coli by Chandrasekhar (1986)
10.1038/371261a0 / Nature / Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy by Chen (1994)
10.1016/S0959-440X(96)80093-5 / Curr. Opin. Struct. Biol. / Molecular chaperones in protein folding and translocation by Clarke (1996)
10.1073/pnas.93.9.4509 / Proc. Natl Acad. Sci. USA / Towards a mechanism for GroEL.GroES chaperone activity by Corrales (1996)
{'key': '10.1006/jmbi.1999.3138_BIB13', 'series-title': 'HMSO Report AERE-R 11771', 'article-title': 'FACSIMILE program', 'author': 'Curtis', 'year': '1985'} / HMSO Report AERE-R 11771 / FACSIMILE program by Curtis (1985)
10.1073/pnas.88.10.4472 / Proc. Natl Acad. Sci. USA / Application of linear free energy relations to protein conformational changes by Eaton (1991)
10.1128/jb.171.3.1379-1385.1989 / J. Bacteriol. / The GroES and GroEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures by Fayet (1989)
10.1002/pro.5560060401 / Protein Sci. / GroEL-mediated protein folding by Fenton (1997)
10.1038/371614a0 / Nature / Residues in chaperonin GroEL required for polypeptide binding and release by Fenton (1994)
10.1074/jbc.271.50.31989 / J. Biol. Chem. / Intrinsic fluorescence studies of the chaperonin groEL containing single Tyr→Trp replacements reveal ligand induced conformational changes by Gibbons (1996)
10.1016/0014-5793(91)80878-7 / FEBS Letters / Cooperativity in ATP hydrolysis by GroEL is increased by GroES by Gray (1991)
10.1126/science.7638601 / Science / Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein-folding by Hayer-Hartl (1995)
10.1002/j.1460-2075.1996.tb00999.x / EMBO J. / Mechanism of chaperonin action by Hayer-Hartl (1996)
10.1038/333330a0 / Nature / Homologous plant and bacterial proteins chaperone oligomeric protein assembly by Hemmingsen (1988)
10.1016/0022-2836(79)90502-3 / J. Mol. Biol. / Purification and properties of groE, a host protein involved in bacteriophage assembly by Hendrix (1979)
10.1016/0022-2836(79)90501-1 / J. Mol. Biol. / Isolation and characterisation of the host protein GroE involved in bacteriophage lambda assembly by Hohn (1979)
10.1098/rstb.1993.0030 / Phil. Trans. Roy. Soc. ser. B / Protein folding in the cell - functions of two families of molecular chaperone, hsp60 and TF-TCP1 by Horwich (1993)
10.1016/S0378-1119(97)00087-5 / Gene / Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37 °C but not 43 °C by Ivic (1997)
10.1021/bi00061a013 / Biochemistry / Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle - implications for the mechanism of assisted protein folding by Jackson (1993)
10.1006/jmbi.1998.1704 / J. Mol. Biol. / Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings by Kad (1998)
10.1021/bi00865a047 / Biochemistry / Comparison of experimental binding data and theoretical models in proteins containing subunits by Koshland (1966)
10.1073/pnas.93.5.1977 / Proc. Natl Acad. Sci. USA / Nucleotide binding-promoted conformational changes release a non-native polypeptide from the Escherichia coli chaperonin GroEL by Lin (1996)
10.1038/41892 / Nature / Protein folding - folding with a two-stroke motor by Lorimer (1997)
10.1038/379420a0 / Nature / Protein-folding in the central cavity of the GroEL-GroES chaperonin complex by Mayhew (1996)
10.1016/S0022-2836(65)80285-6 / J. Mol. Biol. / On the nature of allosteric transitions by Monod (1965)
10.1006/jmbi.1995.0399 / J. Mol. Biol. / Chaperonins can catalyze the reversal of early aggregation steps when a protein misfolds by Ranson (1995)
10.1006/jmbi.1996.0815 / J. Mol. Biol. / Binding, encapsulation and ejection by Ranson (1997)
10.1016/S0092-8674(00)81342-2 / Cell / The chaperonin ATPase cycle - mechanism of allosteric switching and movements of substrate-binding domains in GroEL by Roseman (1996)
10.1038/42047 / Nature / Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL by Rye (1997)
10.1016/S0092-8674(00)80742-4 / Cell / GroEL-GroES cycling by Rye (1999)
10.1038/353025b0 / Nature / Binding of chaperonins by Saibil (1991)
10.1126/science.7913554 / Science / Symmetrical complexes of GroE chaperonins as part of the functional cycle by Schmidt (1994)
10.1126/science.284.5415.822 / Science / Chaperonin function by Shtilerman (1999)
10.1146/annurev.biochem.67.1.581 / Annu. Rev. Biochem. / Structure and function in GroEL-mediated protein folding by Sigler (1998)
10.1074/jbc.270.37.21517 / J. Biol. Chem. / Interactions between the GroE chaperonins and rhodanese-multiple intermediates and release and binding by Smith (1995)
10.1042/bj3000651 / Biochem. J. / Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10 by Staniforth (1994)
10.1126/science.7913555 / Science / Dynamics of the chaperonin ATPase cycle - implications for facilitated protein-folding by Todd (1994)
10.1038/14918 / Nature Struct. Biol. / Thinking outside the box by Wang (1999)
10.1016/0092-8674(94)90533-9 / Cell / GroEL-mediated protein-folding proceeds by multiple rounds of binding and release of nonnative forms by Weissman (1994)
10.1016/0092-8674(95)90098-5 / Cell / Mechanism of GroEL action - productive release of polypeptide from a sequestered position under GroES by Weissman (1995)
10.1016/S0092-8674(00)81293-3 / Cell / Characterization of the active intermediate of a GroEL-GroES-mediated protein-folding reaction by Weissman (1996)
10.1038/41944 / Nature / The crystal structure of the asymmetric GroEL-GroES-(ADP)(7) chaperonin complex by Xu (1997)
10.1006/jmbi.1994.1667 / J. Mol. Biol. / Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196→Ala by Yifrach (1994)
10.1021/bi00016a001 / Biochemistry / Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL by Yifrach (1995)
10.1021/bi980370o / Biochemistry / Transient kinetic analysis of adenosine 5′-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL by Yifrach (1998)
10.1073/pnas.93.26.15024 / Proc. Natl Acad. Sci. USA / Chaperone activity and structure of monomeric polypeptide binding domains of GroEL by Zahn (1996)

Dates

Type	When
Created	22 years, 10 months ago (Oct. 7, 2002, 12:17 p.m.)
Deposited	2 years, 4 months ago (April 4, 2023, 10:15 a.m.)
Indexed	1 month ago (July 24, 2025, 7:26 a.m.)
Issued	25 years, 10 months ago (Oct. 1, 1999)
Published	25 years, 10 months ago (Oct. 1, 1999)
Published Print	25 years, 10 months ago (Oct. 1, 1999)

Funders 0

None

BibTeX

@article{Cliff_1999, title={A kinetic analysis of the nucleotide-induced allosteric transitions of GroEL 1 1Edited by A. R. Fersht}, volume={293}, ISSN={0022-2836}, url={http://dx.doi.org/10.1006/jmbi.1999.3138}, DOI={10.1006/jmbi.1999.3138}, number={3}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Cliff, Matthew J and Kad, Neil M and Hay, Nicky and Lund, Peter A and Webb, Martin R and Burston, Steven G and Clarke, Anthony R}, year={1999}, month=oct, pages={667–684} }

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      "article-title": "The 2.4 \u00c5 crystal-structure of the bacterial chaperonin GroEL complexed with ATP-\u03b3-S",
      "volume": "3",
      "author": "Boisvert",
      "year": "1996",
      "journal-title": "Nature Struct. Biol."
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      "first-page": "578",
      "DOI": "10.1038/371578a0",
      "article-title": "The crystal-structure of the bacterial chaperonin GroEL at 2.8-\u00c5",
      "volume": "371",
      "author": "Braig",
      "year": "1994",
      "journal-title": "Nature"
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    {
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      "first-page": "8262",
      "DOI": "10.1021/bi00193a013",
      "article-title": "Direct, real-time measurement of rapid inorganic-phosphate release using a novel fluorescent probe and its application to actomyosin subfragment-1 ATPase",
      "volume": "33",
      "author": "Brune",
      "year": "1994",
      "journal-title": "Biochemistry"
    },
    {
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      "first-page": "3571",
      "DOI": "10.1073/pnas.94.8.3571",
      "article-title": "A structural model for GroEL-polypeptide recognition",
      "volume": "94",
      "author": "Buckle",
      "year": "1997",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB7",
      "doi-asserted-by": "crossref",
      "first-page": "138",
      "DOI": "10.1006/jmbi.1995.0285",
      "article-title": "The origins and consequences of asymmetry in the chaperonin reaction cycle",
      "volume": "249",
      "author": "Burston",
      "year": "1995",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB8",
      "doi-asserted-by": "crossref",
      "first-page": "96",
      "DOI": "10.1038/383096a0",
      "article-title": "Release of both native and nonnative proteins from a cis-only GroEL ternary complex",
      "volume": "383",
      "author": "Burston",
      "year": "1996",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB9",
      "doi-asserted-by": "crossref",
      "first-page": "2414",
      "DOI": "10.1016/S0021-9258(18)67256-4",
      "article-title": "Purification and properties of the GroES morphogenetic protein of Escherichia coli",
      "volume": "261",
      "author": "Chandrasekhar",
      "year": "1986",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB10",
      "doi-asserted-by": "crossref",
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      "DOI": "10.1038/371261a0",
      "article-title": "Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy",
      "volume": "371",
      "author": "Chen",
      "year": "1994",
      "journal-title": "Nature"
    },
    {
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      "doi-asserted-by": "crossref",
      "first-page": "43",
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      "article-title": "Molecular chaperones in protein folding and translocation",
      "volume": "6",
      "author": "Clarke",
      "year": "1996",
      "journal-title": "Curr. Opin. Struct. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB12",
      "doi-asserted-by": "crossref",
      "first-page": "4509",
      "DOI": "10.1073/pnas.93.9.4509",
      "article-title": "Towards a mechanism for GroEL.GroES chaperone activity",
      "volume": "93",
      "author": "Corrales",
      "year": "1996",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB13",
      "series-title": "HMSO Report AERE-R 11771",
      "article-title": "FACSIMILE program",
      "author": "Curtis",
      "year": "1985"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB14",
      "doi-asserted-by": "crossref",
      "first-page": "4472",
      "DOI": "10.1073/pnas.88.10.4472",
      "article-title": "Application of linear free energy relations to protein conformational changes",
      "volume": "88",
      "author": "Eaton",
      "year": "1991",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB15",
      "doi-asserted-by": "crossref",
      "first-page": "1379",
      "DOI": "10.1128/jb.171.3.1379-1385.1989",
      "article-title": "The GroES and GroEL heat shock gene products of Escherichia coli are essential for bacterial growth at all temperatures",
      "volume": "171",
      "author": "Fayet",
      "year": "1989",
      "journal-title": "J. Bacteriol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB16",
      "doi-asserted-by": "crossref",
      "first-page": "743",
      "DOI": "10.1002/pro.5560060401",
      "article-title": "GroEL-mediated protein folding",
      "volume": "6",
      "author": "Fenton",
      "year": "1997",
      "journal-title": "Protein Sci."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB17",
      "doi-asserted-by": "crossref",
      "first-page": "614",
      "DOI": "10.1038/371614a0",
      "article-title": "Residues in chaperonin GroEL required for polypeptide binding and release",
      "volume": "371",
      "author": "Fenton",
      "year": "1994",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB18",
      "doi-asserted-by": "crossref",
      "first-page": "31989",
      "DOI": "10.1074/jbc.271.50.31989",
      "article-title": "Intrinsic fluorescence studies of the chaperonin groEL containing single Tyr\u2192Trp replacements reveal ligand induced conformational changes",
      "volume": "271",
      "author": "Gibbons",
      "year": "1996",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB19",
      "doi-asserted-by": "crossref",
      "first-page": "254",
      "DOI": "10.1016/0014-5793(91)80878-7",
      "article-title": "Cooperativity in ATP hydrolysis by GroEL is increased by GroES",
      "volume": "292",
      "author": "Gray",
      "year": "1991",
      "journal-title": "FEBS Letters"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB20",
      "doi-asserted-by": "crossref",
      "first-page": "836",
      "DOI": "10.1126/science.7638601",
      "article-title": "Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein-folding",
      "volume": "269",
      "author": "Hayer-Hartl",
      "year": "1995",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB21",
      "doi-asserted-by": "crossref",
      "first-page": "6111",
      "DOI": "10.1002/j.1460-2075.1996.tb00999.x",
      "article-title": "Mechanism of chaperonin action",
      "volume": "15",
      "author": "Hayer-Hartl",
      "year": "1996",
      "journal-title": "EMBO J."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB22",
      "doi-asserted-by": "crossref",
      "first-page": "330",
      "DOI": "10.1038/333330a0",
      "article-title": "Homologous plant and bacterial proteins chaperone oligomeric protein assembly",
      "volume": "333",
      "author": "Hemmingsen",
      "year": "1988",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB23",
      "doi-asserted-by": "crossref",
      "first-page": "375",
      "DOI": "10.1016/0022-2836(79)90502-3",
      "article-title": "Purification and properties of groE, a host protein involved in bacteriophage assembly",
      "volume": "129",
      "author": "Hendrix",
      "year": "1979",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB24",
      "doi-asserted-by": "crossref",
      "first-page": "359",
      "DOI": "10.1016/0022-2836(79)90501-1",
      "article-title": "Isolation and characterisation of the host protein GroE involved in bacteriophage lambda assembly",
      "volume": "129",
      "author": "Hohn",
      "year": "1979",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB25",
      "doi-asserted-by": "crossref",
      "first-page": "313",
      "DOI": "10.1098/rstb.1993.0030",
      "article-title": "Protein folding in the cell - functions of two families of molecular chaperone, hsp60 and TF-TCP1",
      "volume": "339",
      "author": "Horwich",
      "year": "1993",
      "journal-title": "Phil. Trans. Roy. Soc. ser. B"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB26",
      "doi-asserted-by": "crossref",
      "first-page": "1",
      "DOI": "10.1016/S0378-1119(97)00087-5",
      "article-title": "Deletion of Escherichia coli groEL is complemented by a Rhizobium leguminosarum groEL homologue at 37 \u00b0C but not 43 \u00b0C",
      "volume": "194",
      "author": "Ivic",
      "year": "1997",
      "journal-title": "Gene"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB27",
      "doi-asserted-by": "crossref",
      "first-page": "2554",
      "DOI": "10.1021/bi00061a013",
      "article-title": "Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle - implications for the mechanism of assisted protein folding",
      "volume": "32",
      "author": "Jackson",
      "year": "1993",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB28",
      "doi-asserted-by": "crossref",
      "first-page": "267",
      "DOI": "10.1006/jmbi.1998.1704",
      "article-title": "Asymmetry, commitment and inhibition in the GroE ATPase cycle impose alternating functions on the two GroEL rings",
      "volume": "278",
      "author": "Kad",
      "year": "1998",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB29",
      "doi-asserted-by": "crossref",
      "first-page": "365",
      "DOI": "10.1021/bi00865a047",
      "article-title": "Comparison of experimental binding data and theoretical models in proteins containing subunits",
      "volume": "5",
      "author": "Koshland",
      "year": "1966",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB30",
      "doi-asserted-by": "crossref",
      "first-page": "1977",
      "DOI": "10.1073/pnas.93.5.1977",
      "article-title": "Nucleotide binding-promoted conformational changes release a non-native polypeptide from the Escherichia coli chaperonin GroEL",
      "volume": "93",
      "author": "Lin",
      "year": "1996",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB31",
      "doi-asserted-by": "crossref",
      "first-page": "720",
      "DOI": "10.1038/41892",
      "article-title": "Protein folding - folding with a two-stroke motor",
      "volume": "388",
      "author": "Lorimer",
      "year": "1997",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB32",
      "doi-asserted-by": "crossref",
      "first-page": "420",
      "DOI": "10.1038/379420a0",
      "article-title": "Protein-folding in the central cavity of the GroEL-GroES chaperonin complex",
      "volume": "379",
      "author": "Mayhew",
      "year": "1996",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB33",
      "doi-asserted-by": "crossref",
      "first-page": "88",
      "DOI": "10.1016/S0022-2836(65)80285-6",
      "article-title": "On the nature of allosteric transitions",
      "volume": "12",
      "author": "Monod",
      "year": "1965",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB34",
      "doi-asserted-by": "crossref",
      "first-page": "581",
      "DOI": "10.1006/jmbi.1995.0399",
      "article-title": "Chaperonins can catalyze the reversal of early aggregation steps when a protein misfolds",
      "volume": "250",
      "author": "Ranson",
      "year": "1995",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB35",
      "doi-asserted-by": "crossref",
      "first-page": "656",
      "DOI": "10.1006/jmbi.1996.0815",
      "article-title": "Binding, encapsulation and ejection",
      "volume": "266",
      "author": "Ranson",
      "year": "1997",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB36",
      "doi-asserted-by": "crossref",
      "first-page": "241",
      "DOI": "10.1016/S0092-8674(00)81342-2",
      "article-title": "The chaperonin ATPase cycle - mechanism of allosteric switching and movements of substrate-binding domains in GroEL",
      "volume": "87",
      "author": "Roseman",
      "year": "1996",
      "journal-title": "Cell"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB37",
      "doi-asserted-by": "crossref",
      "first-page": "792",
      "DOI": "10.1038/42047",
      "article-title": "Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL",
      "volume": "388",
      "author": "Rye",
      "year": "1997",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB38",
      "doi-asserted-by": "crossref",
      "first-page": "325",
      "DOI": "10.1016/S0092-8674(00)80742-4",
      "article-title": "GroEL-GroES cycling",
      "volume": "97",
      "author": "Rye",
      "year": "1999",
      "journal-title": "Cell"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB39",
      "doi-asserted-by": "crossref",
      "first-page": "25",
      "DOI": "10.1038/353025b0",
      "article-title": "Binding of chaperonins",
      "volume": "353",
      "author": "Saibil",
      "year": "1991",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB40",
      "doi-asserted-by": "crossref",
      "first-page": "656",
      "DOI": "10.1126/science.7913554",
      "article-title": "Symmetrical complexes of GroE chaperonins as part of the functional cycle",
      "volume": "265",
      "author": "Schmidt",
      "year": "1994",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB41",
      "doi-asserted-by": "crossref",
      "first-page": "822",
      "DOI": "10.1126/science.284.5415.822",
      "article-title": "Chaperonin function",
      "volume": "284",
      "author": "Shtilerman",
      "year": "1999",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB42",
      "doi-asserted-by": "crossref",
      "first-page": "581",
      "DOI": "10.1146/annurev.biochem.67.1.581",
      "article-title": "Structure and function in GroEL-mediated protein folding",
      "volume": "67",
      "author": "Sigler",
      "year": "1998",
      "journal-title": "Annu. Rev. Biochem."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB43",
      "doi-asserted-by": "crossref",
      "first-page": "21517",
      "DOI": "10.1074/jbc.270.37.21517",
      "article-title": "Interactions between the GroE chaperonins and rhodanese-multiple intermediates and release and binding",
      "volume": "270",
      "author": "Smith",
      "year": "1995",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB44",
      "doi-asserted-by": "crossref",
      "first-page": "651",
      "DOI": "10.1042/bj3000651",
      "article-title": "Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10",
      "volume": "300",
      "author": "Staniforth",
      "year": "1994",
      "journal-title": "Biochem. J."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB45",
      "doi-asserted-by": "crossref",
      "first-page": "659",
      "DOI": "10.1126/science.7913555",
      "article-title": "Dynamics of the chaperonin ATPase cycle - implications for facilitated protein-folding",
      "volume": "265",
      "author": "Todd",
      "year": "1994",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB46",
      "doi-asserted-by": "crossref",
      "first-page": "597",
      "DOI": "10.1038/14918",
      "article-title": "Thinking outside the box",
      "volume": "6",
      "author": "Wang",
      "year": "1999",
      "journal-title": "Nature Struct. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB47",
      "doi-asserted-by": "crossref",
      "first-page": "693",
      "DOI": "10.1016/0092-8674(94)90533-9",
      "article-title": "GroEL-mediated protein-folding proceeds by multiple rounds of binding and release of nonnative forms",
      "volume": "78",
      "author": "Weissman",
      "year": "1994",
      "journal-title": "Cell"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB48",
      "doi-asserted-by": "crossref",
      "first-page": "577",
      "DOI": "10.1016/0092-8674(95)90098-5",
      "article-title": "Mechanism of GroEL action - productive release of polypeptide from a sequestered position under GroES",
      "volume": "83",
      "author": "Weissman",
      "year": "1995",
      "journal-title": "Cell"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB49",
      "doi-asserted-by": "crossref",
      "first-page": "481",
      "DOI": "10.1016/S0092-8674(00)81293-3",
      "article-title": "Characterization of the active intermediate of a GroEL-GroES-mediated protein-folding reaction",
      "volume": "84",
      "author": "Weissman",
      "year": "1996",
      "journal-title": "Cell"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB50",
      "doi-asserted-by": "crossref",
      "first-page": "741",
      "DOI": "10.1038/41944",
      "article-title": "The crystal structure of the asymmetric GroEL-GroES-(ADP)(7) chaperonin complex",
      "volume": "388",
      "author": "Xu",
      "year": "1997",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB51",
      "doi-asserted-by": "crossref",
      "first-page": "397",
      "DOI": "10.1006/jmbi.1994.1667",
      "article-title": "Two lines of allosteric communication in the oligomeric chaperonin GroEL are revealed by the single mutation Arg196\u2192Ala",
      "volume": "243",
      "author": "Yifrach",
      "year": "1994",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB52",
      "doi-asserted-by": "crossref",
      "first-page": "5303",
      "DOI": "10.1021/bi00016a001",
      "article-title": "Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL",
      "volume": "34",
      "author": "Yifrach",
      "year": "1995",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB53",
      "doi-asserted-by": "crossref",
      "first-page": "7083",
      "DOI": "10.1021/bi980370o",
      "article-title": "Transient kinetic analysis of adenosine 5\u2032-triphosphate binding-induced conformational changes in the allosteric chaperonin GroEL",
      "volume": "37",
      "author": "Yifrach",
      "year": "1998",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jmbi.1999.3138_BIB54",
      "doi-asserted-by": "crossref",
      "first-page": "15024",
      "DOI": "10.1073/pnas.93.26.15024",
      "article-title": "Chaperone activity and structure of monomeric polypeptide binding domains of GroEL",
      "volume": "93",
      "author": "Zahn",
      "year": "1996",
      "journal-title": "Proc. Natl Acad. Sci. USA"
    }
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