DOI: 10.1006/jsbi.1998.4060. GroEL/GroES: Structure and Function of a Two-Stroke Folding Machine

GroEL/GroES: Structure and Function of a Two-Stroke Folding Machine

10.1006/jsbi.1998.4060

Crossref journal-article

Elsevier BV

Journal of Structural Biology (78)

Bibliography

Xu, Z., & Sigler, P. B. (1998). GroEL/GroES: Structure and Function of a Two-Stroke Folding Machine. Journal of Structural Biology, 124(2â3), 129â141.

Authors 2

Zhaohui Xu (first)
Paul B. Sigler (additional)

References 63 Referenced 94

10.1126/science.181.4096.223 / Science / Principles that govern the folding of protein chains by Anfinsen (1973)
10.1073/pnas.92.26.12021 / Proc. Natl. Acad. Sci. USA / The protein-folding activity of chaperonins correlates with the symmetric GroEL1472 by Azem (1995)
10.1126/science.7913553 / Science / Characterization of a functional GroEL1472 by Azem (1994)
10.1016/S0021-9258(19)50496-3 / J. Biol. Chem. / Positive cooperativity in the functioning of molecular chaperone GroEL by Bochkareva (1992)
10.1038/nsb0296-170 / Nat. Struct. Biol. / The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S by Boisvert (1996)
10.1038/nsb1295-1083 / Nat. Struct. Biol. / Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution by Braig (1995)
10.1038/371578a0 / Nature / The crystal structure of the bacterial chaperonin GroEL at 2.8 Å by Braig (1994)
10.1073/pnas.90.9.3978 / Proc. Natl. Acad. Sci. USA / A polypeptide bound by the chaperonin GroEL is localized within a central cavity by Braig (1993)
10.1021/bi00220a020 / Biochemistry / GroE facilitates refolding of citrate synthase by suppressing aggregation by Buchner (1991)
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)
10.1016/S0021-9258(18)67256-4 / J. Biol. Chem. / Purification and properties of the GroES morphogenetic protein ofEscherichia 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)
10.1038/337620a0 / Nature / Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria by Cheng (1989)
10.1016/S0092-8674(00)81152-6 / Cell / Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT by Ditzel (1998)
{'key': '10.1006/jsbi.1998.4060_SB984060RF16', 'series-title': 'The Chaperonins', 'author': 'Ellis', 'year': '1996'} / The Chaperonins by Ellis (1996)
10.1128/jb.171.3.1379-1385.1989 / J. Bacteriol. / The GroES and GroEL heat shock gene products ofEscherichia coli 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)
10.1016/0092-8674(92)90622-J / Cell / A cytoplasmic chaperonin that catalyzes beta-actin folding by Gao (1992)
10.1038/342884a0 / Nature / Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends upon two chaperonin proteins and MgATP by Goloubinoff (1989)
10.1016/0014-5793(91)80878-7 / FEBS Lett. / Cooperativity in ATP hydrolysis by GroEL is increased by GroES by Gray (1991)
10.1038/381571a0 / Nature / Molecular chaperones in cellular protein folding by Hartl (1996)
10.1038/nsb0795-587 / Nat. Struct. Biol. / Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding by Hlodan (1995)
10.1016/0092-8674(93)90470-B / Cell / Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL by Horwich (1993)
10.1038/379037a0 / Nature / The crystal structure of the GroES co-chaperonin at 2.8 Å resolution by Hunt (1996)
10.1016/0014-5793(92)80240-H / FEBS Lett. / Structure of holo-chaperonin studied with electron microscopy. Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each by Ishii (1992)
10.1021/bi00044a037 / Biochemistry / Nature and consequences of GroEL–protein interactions by Itzhaki (1995)
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)
10.1016/0968-0004(94)90058-2 / Trends Biochem. Sci. / Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains by Kim (1994)
10.1002/j.1460-2075.1990.tb07403.x / EMBO J. / TheEscherichia coli by Laminet (1990)
10.1038/364255a0 / Nature / Characterization of a functionally important mobile domain of GroES by Landry (1993)
10.1002/j.1460-2075.1992.tb05581.x / EMBO J. / Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity by Langer (1992)
10.1038/358249a0 / Nature / T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol by Lewis (1992)
10.1074/jbc.270.3.1011 / J. Biol. Chem. / The hydrophobic nature of GroEL–substrate binding by Lin (1995)
10.1038/41892 / Nature / Folding with a two-stroke motor by Lorimer (1997)
10.1073/pnas.95.15.8502 / Proc. Natl. Acad. Sci. USA / The allosteric mechanism of the chaperonin GroEL: A dynamic analysis by Ma (1998)
10.1126/science.271.5246.203 / Science / Structure of the heat shock protein chaperonin-10 ofMycobacterium leprae by Mande (1996)
10.1038/352036a0 / Nature / Chaperonin-mediated protein folding at the surface of groEL through a ‘molten globule’-like intermediate by Martin (1991)
10.1038/379420a0 / Nature / Protein folding in the central cavity of the GroEL–GroES chaperonin complex by Mayhew (1996)
10.1074/jbc.271.45.28229 / J. Biol. Chem. / GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps by Murai (1996)
10.1002/j.1460-2075.1991.tb07695.x / EMBO J. / A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria by Phipps (1991)
10.1006/jmbi.1995.0399 / J. Mol. Biol. / Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds by Ranson (1995)
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)
10.1038/353025b0 / Nature / Binding of chaperonins by Saibil (1991)
10.1126/science.7913554 / Science / Symmetric complexes of GroE chaperonins as part of the functional cycle by Schmidt (1994)
10.1016/S0076-6879(98)90025-8 / Methods Enzymol. / Molecular chaperones and their interactions investigated by analytical ultracentrifugation and other methodologies by Schonfeld (1998)
10.1016/S0969-2126(96)00011-1 / Structure / Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering by Thiyagarajan (1996)
10.1073/pnas.78.3.1629 / Proc. Natl. Acad. Sci. USA / Identification of a secondEscherichia coli by Tilly (1981)
10.1126/science.7913555 / Science / Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding by Todd (1994)
10.1021/bi00084a024 / Biochemistry / Hydrolysis of adenosine 5′-triphosphate byEscherichia coli by Todd (1993)
10.1038/354490a0 / Nature / A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1 by Trent (1991)
10.1021/bi00476a003 / Biochemistry / Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (GroEL) are K+ by Viitanen (1990)
10.1073/pnas.93.18.9425 / Proc. Natl. Acad. Sci. USA / A thermodynamic coupling mechanism for GroEL-mediated unfolding by Walter (1996)
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)
10.1016/0092-8674(94)90533-9 / Cell / GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms by Weissman (1994)
10.1016/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 by Xu (1997)
10.1038/358245a0 / Nature / TCP1 complex is a molecular chaperone in tublin biogenesis by Yaffe (1992)
10.1006/jmbi.1996.0028 / J. Mol. Biol. / Allosteric control by ATP of non-folded protein binding to GroEL by Yifrach (1996)
10.1021/bi00016a001 / Biochemistry / Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL by Yifrach (1995)
10.1126/science.271.5249.642 / Science / Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB by Zahn (1996)

Dates

Type	When
Created	22 years, 11 months ago (Sept. 18, 2002, 2:57 p.m.)
Deposited	1 year, 10 months ago (Nov. 2, 2023, 8:36 a.m.)
Indexed	2 months ago (July 4, 2025, 7:03 a.m.)
Issued	26 years, 9 months ago (Dec. 1, 1998)
Published	26 years, 9 months ago (Dec. 1, 1998)
Published Print	26 years, 9 months ago (Dec. 1, 1998)

Funders 0

None

BibTeX

@article{Xu_1998, title={GroEL/GroES: Structure and Function of a Two-Stroke Folding Machine}, volume={124}, ISSN={1047-8477}, url={http://dx.doi.org/10.1006/jsbi.1998.4060}, DOI={10.1006/jsbi.1998.4060}, number={2–3}, journal={Journal of Structural Biology}, publisher={Elsevier BV}, author={Xu, Zhaohui and Sigler, Paul B.}, year={1998}, month=dec, pages={129–141} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2025,
        7,
        4
      ]
    ],
    "date-time": "2025-07-04T11:03:55Z",
    "timestamp": 1751627035208
  },
  "reference-count": 63,
  "publisher": "Elsevier BV",
  "issue": "2-3",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            1998,
            12,
            1
          ]
        ],
        "date-time": "1998-12-01T00:00:00Z",
        "timestamp": 912470400000
      },
      "content-version": "tdm",
      "delay-in-days": 0,
      "URL": "https://www.elsevier.com/tdm/userlicense/1.0/"
    },
    {
      "start": {
        "date-parts": [
          [
            2002,
            5,
            25
          ]
        ],
        "date-time": "2002-05-25T00:00:00Z",
        "timestamp": 1022284800000
      },
      "content-version": "vor",
      "delay-in-days": 1271,
      "URL": "http://creativecommons.org/licenses/by-nc-nd/4.0/"
    }
  ],
  "content-domain": {
    "domain": [
      "elsevier.com",
      "sciencedirect.com"
    ],
    "crossmark-restriction": true
  },
  "published-print": {
    "date-parts": [
      [
        1998,
        12
      ]
    ]
  },
  "DOI": "10.1006/jsbi.1998.4060",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2002,
        9,
        18
      ]
    ],
    "date-time": "2002-09-18T18:57:36Z",
    "timestamp": 1032375456000
  },
  "page": "129-141",
  "update-policy": "http://dx.doi.org/10.1016/elsevier_cm_policy",
  "source": "Crossref",
  "is-referenced-by-count": 94,
  "title": "GroEL/GroES: Structure and Function of a Two-Stroke Folding Machine",
  "prefix": "10.1016",
  "volume": "124",
  "author": [
    {
      "given": "Zhaohui",
      "family": "Xu",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Paul B.",
      "family": "Sigler",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "78",
  "reference": [
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF1",
      "doi-asserted-by": "crossref",
      "first-page": "223",
      "DOI": "10.1126/science.181.4096.223",
      "article-title": "Principles that govern the folding of protein chains",
      "volume": "181",
      "author": "Anfinsen",
      "year": "1973",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF2",
      "doi-asserted-by": "crossref",
      "first-page": "12021",
      "DOI": "10.1073/pnas.92.26.12021",
      "article-title": "The protein-folding activity of chaperonins correlates with the symmetric GroEL1472",
      "volume": "92",
      "author": "Azem",
      "year": "1995",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF3",
      "doi-asserted-by": "crossref",
      "first-page": "653",
      "DOI": "10.1126/science.7913553",
      "article-title": "Characterization of a functional GroEL1472",
      "volume": "265",
      "author": "Azem",
      "year": "1994",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF4",
      "doi-asserted-by": "crossref",
      "first-page": "6796",
      "DOI": "10.1016/S0021-9258(19)50496-3",
      "article-title": "Positive cooperativity in the functioning of molecular chaperone GroEL",
      "volume": "267",
      "author": "Bochkareva",
      "year": "1992",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF5",
      "doi-asserted-by": "crossref",
      "first-page": "170",
      "DOI": "10.1038/nsb0296-170",
      "article-title": "The 2.4 \u00c5 crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S",
      "volume": "3",
      "author": "Boisvert",
      "year": "1996",
      "journal-title": "Nat. Struct. Biol."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF6",
      "doi-asserted-by": "crossref",
      "first-page": "1083",
      "DOI": "10.1038/nsb1295-1083",
      "article-title": "Conformational variability in the refined structure of the chaperonin GroEL at 2.8 \u00c5 resolution",
      "volume": "2",
      "author": "Braig",
      "year": "1995",
      "journal-title": "Nat. Struct. Biol."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF7",
      "doi-asserted-by": "crossref",
      "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"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF8",
      "doi-asserted-by": "crossref",
      "first-page": "3978",
      "DOI": "10.1073/pnas.90.9.3978",
      "article-title": "A polypeptide bound by the chaperonin GroEL is localized within a central cavity",
      "volume": "90",
      "author": "Braig",
      "year": "1993",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF9",
      "doi-asserted-by": "crossref",
      "first-page": "1586",
      "DOI": "10.1021/bi00220a020",
      "article-title": "GroE facilitates refolding of citrate synthase by suppressing aggregation",
      "volume": "30",
      "author": "Buchner",
      "year": "1991",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF10",
      "doi-asserted-by": "crossref",
      "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/jsbi.1998.4060_SB984060RF11",
      "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/jsbi.1998.4060_SB984060RF12",
      "doi-asserted-by": "crossref",
      "first-page": "12414",
      "DOI": "10.1016/S0021-9258(18)67256-4",
      "article-title": "Purification and properties of the GroES morphogenetic protein ofEscherichia coli",
      "volume": "261",
      "author": "Chandrasekhar",
      "year": "1986",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF13",
      "doi-asserted-by": "crossref",
      "first-page": "261",
      "DOI": "10.1038/371261a0",
      "article-title": "Location of a folding protein and shape changes in GroEL\u2013GroES complexes imaged by cryo-electron microscopy",
      "volume": "371",
      "author": "Chen",
      "year": "1994",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF14",
      "doi-asserted-by": "crossref",
      "first-page": "620",
      "DOI": "10.1038/337620a0",
      "article-title": "Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria",
      "volume": "337",
      "author": "Cheng",
      "year": "1989",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF15",
      "doi-asserted-by": "crossref",
      "first-page": "125",
      "DOI": "10.1016/S0092-8674(00)81152-6",
      "article-title": "Crystal structure of the thermosome, the archaeal chaperonin and homolog of CCT",
      "volume": "93",
      "author": "Ditzel",
      "year": "1998",
      "journal-title": "Cell"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF16",
      "series-title": "The Chaperonins",
      "author": "Ellis",
      "year": "1996"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF17",
      "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 ofEscherichia coli",
      "volume": "171",
      "author": "Fayet",
      "year": "1989",
      "journal-title": "J. Bacteriol."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF18",
      "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/jsbi.1998.4060_SB984060RF19",
      "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/jsbi.1998.4060_SB984060RF20",
      "doi-asserted-by": "crossref",
      "first-page": "1043",
      "DOI": "10.1016/0092-8674(92)90622-J",
      "article-title": "A cytoplasmic chaperonin that catalyzes beta-actin folding",
      "volume": "69",
      "author": "Gao",
      "year": "1992",
      "journal-title": "Cell"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF21",
      "doi-asserted-by": "crossref",
      "first-page": "884",
      "DOI": "10.1038/342884a0",
      "article-title": "Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends upon two chaperonin proteins and MgATP",
      "volume": "342",
      "author": "Goloubinoff",
      "year": "1989",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF22",
      "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 Lett."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF23",
      "doi-asserted-by": "crossref",
      "first-page": "571",
      "DOI": "10.1038/381571a0",
      "article-title": "Molecular chaperones in cellular protein folding",
      "volume": "381",
      "author": "Hartl",
      "year": "1996",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF24",
      "doi-asserted-by": "crossref",
      "first-page": "587",
      "DOI": "10.1038/nsb0795-587",
      "article-title": "Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding",
      "volume": "2",
      "author": "Hlodan",
      "year": "1995",
      "journal-title": "Nat. Struct. Biol."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF25",
      "doi-asserted-by": "crossref",
      "first-page": "909",
      "DOI": "10.1016/0092-8674(93)90470-B",
      "article-title": "Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL",
      "volume": "74",
      "author": "Horwich",
      "year": "1993",
      "journal-title": "Cell"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF26",
      "doi-asserted-by": "crossref",
      "first-page": "37",
      "DOI": "10.1038/379037a0",
      "article-title": "The crystal structure of the GroES co-chaperonin at 2.8 \u00c5 resolution",
      "volume": "379",
      "author": "Hunt",
      "year": "1996",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF27",
      "doi-asserted-by": "crossref",
      "first-page": "169",
      "DOI": "10.1016/0014-5793(92)80240-H",
      "article-title": "Structure of holo-chaperonin studied with electron microscopy. Oligomeric cpn10 on top of two layers of cpn60 rings with two stripes each",
      "volume": "299",
      "author": "Ishii",
      "year": "1992",
      "journal-title": "FEBS Lett."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF28",
      "doi-asserted-by": "crossref",
      "first-page": "14581",
      "DOI": "10.1021/bi00044a037",
      "article-title": "Nature and consequences of GroEL\u2013protein interactions",
      "volume": "34",
      "author": "Itzhaki",
      "year": "1995",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF29",
      "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/jsbi.1998.4060_SB984060RF30",
      "doi-asserted-by": "crossref",
      "first-page": "543",
      "DOI": "10.1016/0968-0004(94)90058-2",
      "article-title": "Cystosolic chaperonin subunits have a conserved ATPase domain but diverged polypeptide-binding domains",
      "volume": "19",
      "author": "Kim",
      "year": "1994",
      "journal-title": "Trends Biochem. Sci."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF31",
      "doi-asserted-by": "crossref",
      "first-page": "2315",
      "DOI": "10.1002/j.1460-2075.1990.tb07403.x",
      "article-title": "TheEscherichia coli",
      "volume": "9",
      "author": "Laminet",
      "year": "1990",
      "journal-title": "EMBO J."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF32",
      "doi-asserted-by": "crossref",
      "first-page": "255",
      "DOI": "10.1038/364255a0",
      "article-title": "Characterization of a functionally important mobile domain of GroES",
      "volume": "364",
      "author": "Landry",
      "year": "1993",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF33",
      "doi-asserted-by": "crossref",
      "first-page": "4757",
      "DOI": "10.1002/j.1460-2075.1992.tb05581.x",
      "article-title": "Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity",
      "volume": "11",
      "author": "Langer",
      "year": "1992",
      "journal-title": "EMBO J."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF34",
      "doi-asserted-by": "crossref",
      "first-page": "249",
      "DOI": "10.1038/358249a0",
      "article-title": "T-complex polypeptide-1 is a subunit of a heteromeric particle in the eukaryotic cytosol",
      "volume": "358",
      "author": "Lewis",
      "year": "1992",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF35",
      "doi-asserted-by": "crossref",
      "first-page": "1011",
      "DOI": "10.1074/jbc.270.3.1011",
      "article-title": "The hydrophobic nature of GroEL\u2013substrate binding",
      "volume": "270",
      "author": "Lin",
      "year": "1995",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF36",
      "doi-asserted-by": "crossref",
      "first-page": "720",
      "DOI": "10.1038/41892",
      "article-title": "Folding with a two-stroke motor",
      "volume": "388",
      "author": "Lorimer",
      "year": "1997",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF37",
      "doi-asserted-by": "crossref",
      "first-page": "8502",
      "DOI": "10.1073/pnas.95.15.8502",
      "article-title": "The allosteric mechanism of the chaperonin GroEL: A dynamic analysis",
      "volume": "95",
      "author": "Ma",
      "year": "1998",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF38",
      "doi-asserted-by": "crossref",
      "first-page": "203",
      "DOI": "10.1126/science.271.5246.203",
      "article-title": "Structure of the heat shock protein chaperonin-10 ofMycobacterium leprae",
      "volume": "271",
      "author": "Mande",
      "year": "1996",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF39",
      "doi-asserted-by": "crossref",
      "first-page": "36",
      "DOI": "10.1038/352036a0",
      "article-title": "Chaperonin-mediated protein folding at the surface of groEL through a \u2018molten globule\u2019-like intermediate",
      "volume": "352",
      "author": "Martin",
      "year": "1991",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF40",
      "doi-asserted-by": "crossref",
      "first-page": "420",
      "DOI": "10.1038/379420a0",
      "article-title": "Protein folding in the central cavity of the GroEL\u2013GroES chaperonin complex",
      "volume": "379",
      "author": "Mayhew",
      "year": "1996",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF41",
      "doi-asserted-by": "crossref",
      "first-page": "28229",
      "DOI": "10.1074/jbc.271.45.28229",
      "article-title": "GroEL locked in a closed conformation by an interdomain cross-link can bind ATP and polypeptide but cannot process further reaction steps",
      "volume": "261",
      "author": "Murai",
      "year": "1996",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF42",
      "doi-asserted-by": "crossref",
      "first-page": "1711",
      "DOI": "10.1002/j.1460-2075.1991.tb07695.x",
      "article-title": "A novel ATPase complex selectively accumulated upon heat shock is a major cellular component of thermophilic archaebacteria",
      "volume": "10",
      "author": "Phipps",
      "year": "1991",
      "journal-title": "EMBO J."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF43",
      "doi-asserted-by": "crossref",
      "first-page": "581",
      "DOI": "10.1006/jmbi.1995.0399",
      "article-title": "Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds",
      "volume": "250",
      "author": "Ranson",
      "year": "1995",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF44",
      "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/jsbi.1998.4060_SB984060RF45",
      "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/jsbi.1998.4060_SB984060RF46",
      "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/jsbi.1998.4060_SB984060RF47",
      "doi-asserted-by": "crossref",
      "first-page": "656",
      "DOI": "10.1126/science.7913554",
      "article-title": "Symmetric complexes of GroE chaperonins as part of the functional cycle",
      "volume": "265",
      "author": "Schmidt",
      "year": "1994",
      "journal-title": "Science"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF48",
      "doi-asserted-by": "crossref",
      "first-page": "269",
      "DOI": "10.1016/S0076-6879(98)90025-8",
      "article-title": "Molecular chaperones and their interactions investigated by analytical ultracentrifugation and other methodologies",
      "volume": "290",
      "author": "Schonfeld",
      "year": "1998",
      "journal-title": "Methods Enzymol."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF49",
      "doi-asserted-by": "crossref",
      "first-page": "79",
      "DOI": "10.1016/S0969-2126(96)00011-1",
      "article-title": "Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering",
      "volume": "4",
      "author": "Thiyagarajan",
      "year": "1996",
      "journal-title": "Structure"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF50",
      "doi-asserted-by": "crossref",
      "first-page": "1629",
      "DOI": "10.1073/pnas.78.3.1629",
      "article-title": "Identification of a secondEscherichia coli",
      "volume": "78",
      "author": "Tilly",
      "year": "1981",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF51",
      "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/jsbi.1998.4060_SB984060RF52",
      "doi-asserted-by": "crossref",
      "first-page": "8560",
      "DOI": "10.1021/bi00084a024",
      "article-title": "Hydrolysis of adenosine 5\u2032-triphosphate byEscherichia coli",
      "volume": "32",
      "author": "Todd",
      "year": "1993",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF53",
      "doi-asserted-by": "crossref",
      "first-page": "490",
      "DOI": "10.1038/354490a0",
      "article-title": "A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1",
      "volume": "354",
      "author": "Trent",
      "year": "1991",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF54",
      "doi-asserted-by": "crossref",
      "first-page": "5665",
      "DOI": "10.1021/bi00476a003",
      "article-title": "Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (GroEL) are K+",
      "volume": "29",
      "author": "Viitanen",
      "year": "1990",
      "journal-title": "Biochemistry"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF55",
      "doi-asserted-by": "crossref",
      "first-page": "9425",
      "DOI": "10.1073/pnas.93.18.9425",
      "article-title": "A thermodynamic coupling mechanism for GroEL-mediated unfolding",
      "volume": "93",
      "author": "Walter",
      "year": "1996",
      "journal-title": "Proc. Natl. Acad. Sci. USA"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF56",
      "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/jsbi.1998.4060_SB984060RF57",
      "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/jsbi.1998.4060_SB984060RF58",
      "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\u2013GroES-mediated protein folding reaction",
      "volume": "84",
      "author": "Weissman",
      "year": "1996",
      "journal-title": "Cell"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF59",
      "doi-asserted-by": "crossref",
      "first-page": "741",
      "DOI": "10.1038/41944",
      "article-title": "The crystal structure of the asymmetric GroEL\u2013GroES\u2013(ADP)7",
      "volume": "388",
      "author": "Xu",
      "year": "1997",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF60",
      "doi-asserted-by": "crossref",
      "first-page": "245",
      "DOI": "10.1038/358245a0",
      "article-title": "TCP1 complex is a molecular chaperone in tublin biogenesis",
      "volume": "358",
      "author": "Yaffe",
      "year": "1992",
      "journal-title": "Nature"
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF61",
      "doi-asserted-by": "crossref",
      "first-page": "356",
      "DOI": "10.1006/jmbi.1996.0028",
      "article-title": "Allosteric control by ATP of non-folded protein binding to GroEL",
      "volume": "255",
      "author": "Yifrach",
      "year": "1996",
      "journal-title": "J. Mol. Biol."
    },
    {
      "key": "10.1006/jsbi.1998.4060_SB984060RF62",
      "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/jsbi.1998.4060_SB984060RF63",
      "doi-asserted-by": "crossref",
      "first-page": "642",
      "DOI": "10.1126/science.271.5249.642",
      "article-title": "Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB",
      "volume": "271",
      "author": "Zahn",
      "year": "1996",
      "journal-title": "Science"
    }
  ],
  "container-title": "Journal of Structural Biology",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.elsevier.com/content/article/PII:S1047847798940606?httpAccept=text/xml",
      "content-type": "text/xml",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://api.elsevier.com/content/article/PII:S1047847798940606?httpAccept=text/plain",
      "content-type": "text/plain",
      "content-version": "vor",
      "intended-application": "text-mining"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        11,
        2
      ]
    ],
    "date-time": "2023-11-02T12:36:32Z",
    "timestamp": 1698928592000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://linkinghub.elsevier.com/retrieve/pii/S1047847798940606"
    }
  },
  "subtitle": [],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        1998,
        12
      ]
    ]
  },
  "references-count": 63,
  "journal-issue": {
    "issue": "2-3",
    "published-print": {
      "date-parts": [
        [
          1998,
          12
        ]
      ]
    }
  },
  "alternative-id": [
    "S1047847798940606"
  ],
  "URL": "http://dx.doi.org/10.1006/jsbi.1998.4060",
  "relation": {},
  "ISSN": [
    "1047-8477"
  ],
  "subject": [],
  "container-title-short": "Journal of Structural Biology",
  "published": {
    "date-parts": [
      [
        1998,
        12
      ]
    ]
  },
  "assertion": [
    {
      "value": "Elsevier",
      "name": "publisher",
      "label": "This article is maintained by"
    },
    {
      "value": "GroEL/GroES: Structure and Function of a Two-Stroke Folding Machine",
      "name": "articletitle",
      "label": "Article Title"
    },
    {
      "value": "Journal of Structural Biology",
      "name": "journaltitle",
      "label": "Journal Title"
    },
    {
      "value": "https://doi.org/10.1006/jsbi.1998.4060",
      "name": "articlelink",
      "label": "CrossRef DOI link to publisher maintained version"
    },
    {
      "value": "converted-article",
      "name": "content_type",
      "label": "Content Type"
    },
    {
      "value": "Copyright \u00a9 1998 Academic Press. All rights reserved.",
      "name": "copyright",
      "label": "Copyright"
    }
  ]
}