GroEL (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "GroEL" in English language version.

refsWebsite

Global rank English rank

34nih.gov

4^th place

27doi.org

2^nd place

11semanticscholar.org

11^th place

8^th place

5harvard.edu

18^th place

17^th place

2ensembl.org

1,626^th place

1,007^th place

2uni-muenchen.de

3,337^th place

3,444^th place

1cambridge.org

305^th place

264^th place

1rcsb.org

8,838^th place

8,783^rd place

1worldcat.org

5^th place

cambridge.org (Global: 305^th place; English: 264^th place)

journals.cambridge.org

Ranford JC, et al. (September 2000). "Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones". Expert Rev Mol Med. 2 (8): 1–17. doi:10.1017/S1462399400002015. PMID 14585136. S2CID 38110138.

doi.org (Global: 2^nd place; English: 2^nd place)

Zeilstra-Ryalls J, Fayet O, Georgopoulos C (1991). "The universally conserved GroE (Hsp60) chaperonins". Annu. Rev. Microbiol. 45: 301–25. doi:10.1146/annurev.mi.45.100191.001505. PMID 1683763.
Gupta RS (January 1995). "Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells". Mol. Microbiol. 15 (1): 1–11. doi:10.1111/j.1365-2958.1995.tb02216.x. PMID 7752884.
Itoh H, Komatsuda A, Ohtani H, et al. (December 2002). "Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration". Eur. J. Biochem. 269 (23): 5931–8. doi:10.1046/j.1432-1033.2002.03317.x. PMID 12444982.
Cheng MY, Hartl FU, Horwich AL (November 1990). "The mitochondrial chaperonin hsp60 is required for its own assembly". Nature. 348 (6300): 455–8. Bibcode:1990Natur.348..455C. doi:10.1038/348455a0. PMID 1978929. S2CID 28394330.
Fenton WA, et al. (October 1994). "Residues in chaperonin GroEL required for polypeptide binding and release". Nature. 371 (6498): 614–9. Bibcode:1994Natur.371..614F. doi:10.1038/371614a0. PMID 7935796. S2CID 23840816.
Habich C, et al. (March 2007). "Heat shock protein 60: regulatory role on innate immune cells". Cell. Mol. Life Sci. 64 (6): 742–51. doi:10.1007/s00018-007-6413-7. PMC 11138415. PMID 17221165. S2CID 24067484.
Ranford JC, et al. (September 2000). "Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones". Expert Rev Mol Med. 2 (8): 1–17. doi:10.1017/S1462399400002015. PMID 14585136. S2CID 38110138.
PDB: 1SRV; Walsh MA, et al. (June 1999). "Taking MAD to the extreme: ultrafast protein structure determination". Acta Crystallogr. D. 55 (6): 1168–73. Bibcode:1999AcCrD..55.1168W. doi:10.1107/S0907444999003698. PMID 10329779.
Johnson RB, et al. (2003). "Cloning and characterization of the yeast chaperonin HSP60 gene". Genetics. 84 (2): 295–300. doi:10.1016/0378-1119(89)90503-9. PMID 2575559.
Koll H, et al. (March 1992). "Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space" (PDF). Cell. 68 (6): 1163–75. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. S2CID 7430067.
Kaufman, B. A. (2003). "A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae". The Journal of Cell Biology. 163 (3): 457–461. doi:10.1083/jcb.200306132. ISSN 0021-9525. PMC 2173642. PMID 14597775.
Koll H, et al. (1992). "Antifolding Activity of HSP60 Couples Protein Import into the Mitochondrial Matrix with Export to the Intermembrane Space" (PDF). Cell. 68 (6): 1163–75. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. S2CID 7430067.
Itoh H, et al. (December 2002). "Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration". Eur. J. Biochem. 269 (23): 5931–8. doi:10.1046/j.1432-1033.2002.03317.x. PMID 12444982.
Hansen JJ, Bross P, Westergaard M, et al. (January 2003). "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter". Hum. Genet. 112 (1): 71–7. doi:10.1007/s00439-002-0837-9. PMID 12483302. S2CID 25856774.
Vargas-Parada L, Solis C (2001). "Heat Shock and stress response of Taenia solium and T. crassiceps". Parasitology. 122 (5): 583–8. doi:10.1017/s0031182001007764. PMID 11393832. S2CID 41092962.
Calabrese V, Mancuso C, Ravagna A, et al. (May 2007). "In vivo induction of heat shock proteins in the substantia nigra following L-DOPA administration is associated with increased activity of mitochondrial complex I and nitrosative stress in rats: regulation by glutathione redox state". J. Neurochem. 101 (3): 709–17. doi:10.1111/j.1471-4159.2006.04367.x. PMID 17241115. S2CID 6512400.
Rossi MR, Somji S, Garrett SH, Sens MA, Nath J, Sens DA (December 2002). "Expression of hsp 27, hsp 60, hsc 70, and hsp 70 stress response genes in cultured human urothelial cells (UROtsa) exposed to lethal and sublethal concentrations of sodium arsenite". Environ. Health Perspect. 110 (12): 1225–32. doi:10.1289/ehp.021101225. PMC 1241110. PMID 12460802.
Cappello F, Di Stefano A, David S, et al. (November 2006). "Hsp60 and Hsp10 down-regulation predicts bronchial epithelial carcinogenesis in smokers with chronic obstructive pulmonary disease". Cancer. 107 (10): 2417–24. doi:10.1002/cncr.22265. PMID 17048249.
Urushibara M, Kageyama Y, Akashi T, et al. (January 2007). "HSP60 may predict good pathological response to neoadjuvant chemoradiotherapy in bladder cancer". Jpn. J. Clin. Oncol. 37 (1): 56–61. doi:10.1093/jjco/hyl121. PMID 17095522.
Lebret T, Watson RW, Molinié V, et al. (September 2003). "Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma". Cancer. 98 (5): 970–7. doi:10.1002/cncr.11594. PMID 12942564. S2CID 30820581.
Horwich AL, Fenton WA, Chapman E, Farr GW (2007). "Two families of chaperonin: physiology and mechanism". Annu. Rev. Cell Dev. Biol. 23: 115–45. doi:10.1146/annurev.cellbio.23.090506.123555. PMID 17489689.
Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S (Apr 1999). "Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells". EMBO J. 18 (8): 2040–8. doi:10.1093/emboj/18.8.2040. PMC 1171288. PMID 10205158.
Lee KH, Kim HS, Jeong HS, Lee YS (Oct 2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli". Biochem. Biophys. Res. Commun. 298 (2): 216–24. doi:10.1016/S0006-291X(02)02423-3. PMID 12387818.
Xanthoudakis S, Roy S, Rasper D, Hennessey T, Aubin Y, Cassady R, Tawa P, Ruel R, Rosen A, Nicholson DW (Apr 1999). "Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis". EMBO J. 18 (8): 2049–56. doi:10.1093/emboj/18.8.2049. PMC 1171289. PMID 10205159.
Mayhew M, da Silva AC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU (Feb 1996). "Protein folding in the central cavity of the GroEL-GroES chaperonin complex". Nature. 379 (6564): 420–6. Bibcode:1996Natur.379..420M. doi:10.1038/379420a0. PMID 8559246. S2CID 4310511.
Edgar RS, Epstein RH (February 1965). "The genetics of a bacterial virus". Scientific American. 212 (2): 70–8. Bibcode:1965SciAm.212b..70E. doi:10.1038/scientificamerican0265-70. PMID 14272117.
Snustad DP (August 1968). "Dominance interactions in Escherichia coli cells mixedly infected with bacteriophage T4D wild-type and amber mutants and their possible implications as to type of gene-product function: catalytic vs. stoichiometric". Virology. 35 (4): 550–63. doi:10.1016/0042-6822(68)90285-7. PMID 4878023.

ensembl.org (Global: 1,626^th place; English: 1,007^th place)

May2017.archive.ensembl.org

GRCh38: Ensembl release 89: ENSG00000144381 – Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000025980 – Ensembl, May 2017

harvard.edu (Global: 18^th place; English: 17^th place)

ui.adsabs.harvard.edu

Cheng MY, Hartl FU, Horwich AL (November 1990). "The mitochondrial chaperonin hsp60 is required for its own assembly". Nature. 348 (6300): 455–8. Bibcode:1990Natur.348..455C. doi:10.1038/348455a0. PMID 1978929. S2CID 28394330.
Fenton WA, et al. (October 1994). "Residues in chaperonin GroEL required for polypeptide binding and release". Nature. 371 (6498): 614–9. Bibcode:1994Natur.371..614F. doi:10.1038/371614a0. PMID 7935796. S2CID 23840816.
PDB: 1SRV; Walsh MA, et al. (June 1999). "Taking MAD to the extreme: ultrafast protein structure determination". Acta Crystallogr. D. 55 (6): 1168–73. Bibcode:1999AcCrD..55.1168W. doi:10.1107/S0907444999003698. PMID 10329779.
Mayhew M, da Silva AC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU (Feb 1996). "Protein folding in the central cavity of the GroEL-GroES chaperonin complex". Nature. 379 (6564): 420–6. Bibcode:1996Natur.379..420M. doi:10.1038/379420a0. PMID 8559246. S2CID 4310511.
Edgar RS, Epstein RH (February 1965). "The genetics of a bacterial virus". Scientific American. 212 (2): 70–8. Bibcode:1965SciAm.212b..70E. doi:10.1038/scientificamerican0265-70. PMID 14272117.

nih.gov (Global: 4^th place; English: 4^th place)

pubmed.ncbi.nlm.nih.gov

Zeilstra-Ryalls J, Fayet O, Georgopoulos C (1991). "The universally conserved GroE (Hsp60) chaperonins". Annu. Rev. Microbiol. 45: 301–25. doi:10.1146/annurev.mi.45.100191.001505. PMID 1683763.
Gupta RS (January 1995). "Evolution of the chaperonin families (Hsp60, Hsp10 and Tcp-1) of proteins and the origin of eukaryotic cells". Mol. Microbiol. 15 (1): 1–11. doi:10.1111/j.1365-2958.1995.tb02216.x. PMID 7752884.
Itoh H, Komatsuda A, Ohtani H, et al. (December 2002). "Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration". Eur. J. Biochem. 269 (23): 5931–8. doi:10.1046/j.1432-1033.2002.03317.x. PMID 12444982.
Cheng MY, Hartl FU, Horwich AL (November 1990). "The mitochondrial chaperonin hsp60 is required for its own assembly". Nature. 348 (6300): 455–8. Bibcode:1990Natur.348..455C. doi:10.1038/348455a0. PMID 1978929. S2CID 28394330.
Fenton WA, et al. (October 1994). "Residues in chaperonin GroEL required for polypeptide binding and release". Nature. 371 (6498): 614–9. Bibcode:1994Natur.371..614F. doi:10.1038/371614a0. PMID 7935796. S2CID 23840816.
Habich C, et al. (March 2007). "Heat shock protein 60: regulatory role on innate immune cells". Cell. Mol. Life Sci. 64 (6): 742–51. doi:10.1007/s00018-007-6413-7. PMC 11138415. PMID 17221165. S2CID 24067484.
Ranford JC, et al. (September 2000). "Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones". Expert Rev Mol Med. 2 (8): 1–17. doi:10.1017/S1462399400002015. PMID 14585136. S2CID 38110138.
PDB: 1SRV; Walsh MA, et al. (June 1999). "Taking MAD to the extreme: ultrafast protein structure determination". Acta Crystallogr. D. 55 (6): 1168–73. Bibcode:1999AcCrD..55.1168W. doi:10.1107/S0907444999003698. PMID 10329779.
Johnson RB, et al. (2003). "Cloning and characterization of the yeast chaperonin HSP60 gene". Genetics. 84 (2): 295–300. doi:10.1016/0378-1119(89)90503-9. PMID 2575559.
Koll H, et al. (March 1992). "Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space" (PDF). Cell. 68 (6): 1163–75. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. S2CID 7430067.
Kaufman, B. A. (2003). "A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae". The Journal of Cell Biology. 163 (3): 457–461. doi:10.1083/jcb.200306132. ISSN 0021-9525. PMC 2173642. PMID 14597775.
Koll H, et al. (1992). "Antifolding Activity of HSP60 Couples Protein Import into the Mitochondrial Matrix with Export to the Intermembrane Space" (PDF). Cell. 68 (6): 1163–75. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. S2CID 7430067.
Itoh H, et al. (December 2002). "Mammalian HSP60 is quickly sorted into the mitochondria under conditions of dehydration". Eur. J. Biochem. 269 (23): 5931–8. doi:10.1046/j.1432-1033.2002.03317.x. PMID 12444982.
Hansen JJ, Bross P, Westergaard M, et al. (January 2003). "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter". Hum. Genet. 112 (1): 71–7. doi:10.1007/s00439-002-0837-9. PMID 12483302. S2CID 25856774.
Vargas-Parada L, Solis C (2001). "Heat Shock and stress response of Taenia solium and T. crassiceps". Parasitology. 122 (5): 583–8. doi:10.1017/s0031182001007764. PMID 11393832. S2CID 41092962.
Calabrese V, Mancuso C, Ravagna A, et al. (May 2007). "In vivo induction of heat shock proteins in the substantia nigra following L-DOPA administration is associated with increased activity of mitochondrial complex I and nitrosative stress in rats: regulation by glutathione redox state". J. Neurochem. 101 (3): 709–17. doi:10.1111/j.1471-4159.2006.04367.x. PMID 17241115. S2CID 6512400.
Rossi MR, Somji S, Garrett SH, Sens MA, Nath J, Sens DA (December 2002). "Expression of hsp 27, hsp 60, hsc 70, and hsp 70 stress response genes in cultured human urothelial cells (UROtsa) exposed to lethal and sublethal concentrations of sodium arsenite". Environ. Health Perspect. 110 (12): 1225–32. doi:10.1289/ehp.021101225. PMC 1241110. PMID 12460802.
Cappello F, Di Stefano A, David S, et al. (November 2006). "Hsp60 and Hsp10 down-regulation predicts bronchial epithelial carcinogenesis in smokers with chronic obstructive pulmonary disease". Cancer. 107 (10): 2417–24. doi:10.1002/cncr.22265. PMID 17048249.
Urushibara M, Kageyama Y, Akashi T, et al. (January 2007). "HSP60 may predict good pathological response to neoadjuvant chemoradiotherapy in bladder cancer". Jpn. J. Clin. Oncol. 37 (1): 56–61. doi:10.1093/jjco/hyl121. PMID 17095522.
Lebret T, Watson RW, Molinié V, et al. (September 2003). "Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma". Cancer. 98 (5): 970–7. doi:10.1002/cncr.11594. PMID 12942564. S2CID 30820581.
Horwich AL, Fenton WA, Chapman E, Farr GW (2007). "Two families of chaperonin: physiology and mechanism". Annu. Rev. Cell Dev. Biol. 23: 115–45. doi:10.1146/annurev.cellbio.23.090506.123555. PMID 17489689.
Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S (Apr 1999). "Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells". EMBO J. 18 (8): 2040–8. doi:10.1093/emboj/18.8.2040. PMC 1171288. PMID 10205158.
Lee KH, Kim HS, Jeong HS, Lee YS (Oct 2002). "Chaperonin GroESL mediates the protein folding of human liver mitochondrial aldehyde dehydrogenase in Escherichia coli". Biochem. Biophys. Res. Commun. 298 (2): 216–24. doi:10.1016/S0006-291X(02)02423-3. PMID 12387818.
Xanthoudakis S, Roy S, Rasper D, Hennessey T, Aubin Y, Cassady R, Tawa P, Ruel R, Rosen A, Nicholson DW (Apr 1999). "Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis". EMBO J. 18 (8): 2049–56. doi:10.1093/emboj/18.8.2049. PMC 1171289. PMID 10205159.
Mayhew M, da Silva AC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU (Feb 1996). "Protein folding in the central cavity of the GroEL-GroES chaperonin complex". Nature. 379 (6564): 420–6. Bibcode:1996Natur.379..420M. doi:10.1038/379420a0. PMID 8559246. S2CID 4310511.
Edgar RS, Epstein RH (February 1965). "The genetics of a bacterial virus". Scientific American. 212 (2): 70–8. Bibcode:1965SciAm.212b..70E. doi:10.1038/scientificamerican0265-70. PMID 14272117.
Snustad DP (August 1968). "Dominance interactions in Escherichia coli cells mixedly infected with bacteriophage T4D wild-type and amber mutants and their possible implications as to type of gene-product function: catalytic vs. stoichiometric". Virology. 35 (4): 550–63. doi:10.1016/0042-6822(68)90285-7. PMID 4878023.

ncbi.nlm.nih.gov

"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Habich C, et al. (March 2007). "Heat shock protein 60: regulatory role on innate immune cells". Cell. Mol. Life Sci. 64 (6): 742–51. doi:10.1007/s00018-007-6413-7. PMC 11138415. PMID 17221165. S2CID 24067484.
Kaufman, B. A. (2003). "A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae". The Journal of Cell Biology. 163 (3): 457–461. doi:10.1083/jcb.200306132. ISSN 0021-9525. PMC 2173642. PMID 14597775.
Rossi MR, Somji S, Garrett SH, Sens MA, Nath J, Sens DA (December 2002). "Expression of hsp 27, hsp 60, hsc 70, and hsp 70 stress response genes in cultured human urothelial cells (UROtsa) exposed to lethal and sublethal concentrations of sodium arsenite". Environ. Health Perspect. 110 (12): 1225–32. doi:10.1289/ehp.021101225. PMC 1241110. PMID 12460802.
Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S (Apr 1999). "Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of jurkat cells". EMBO J. 18 (8): 2040–8. doi:10.1093/emboj/18.8.2040. PMC 1171288. PMID 10205158.
Xanthoudakis S, Roy S, Rasper D, Hennessey T, Aubin Y, Cassady R, Tawa P, Ruel R, Rosen A, Nicholson DW (Apr 1999). "Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis". EMBO J. 18 (8): 2049–56. doi:10.1093/emboj/18.8.2049. PMC 1171289. PMID 10205159.

rcsb.org (Global: 8,838^th place; English: 8,783^rd place)

PDB: 1SRV; Walsh MA, et al. (June 1999). "Taking MAD to the extreme: ultrafast protein structure determination". Acta Crystallogr. D. 55 (6): 1168–73. Bibcode:1999AcCrD..55.1168W. doi:10.1107/S0907444999003698. PMID 10329779.

semanticscholar.org (Global: 11^th place; English: 8^th place)

api.semanticscholar.org

Cheng MY, Hartl FU, Horwich AL (November 1990). "The mitochondrial chaperonin hsp60 is required for its own assembly". Nature. 348 (6300): 455–8. Bibcode:1990Natur.348..455C. doi:10.1038/348455a0. PMID 1978929. S2CID 28394330.
Fenton WA, et al. (October 1994). "Residues in chaperonin GroEL required for polypeptide binding and release". Nature. 371 (6498): 614–9. Bibcode:1994Natur.371..614F. doi:10.1038/371614a0. PMID 7935796. S2CID 23840816.
Habich C, et al. (March 2007). "Heat shock protein 60: regulatory role on innate immune cells". Cell. Mol. Life Sci. 64 (6): 742–51. doi:10.1007/s00018-007-6413-7. PMC 11138415. PMID 17221165. S2CID 24067484.
Ranford JC, et al. (September 2000). "Chaperonins are cell-signalling proteins: the unfolding biology of molecular chaperones". Expert Rev Mol Med. 2 (8): 1–17. doi:10.1017/S1462399400002015. PMID 14585136. S2CID 38110138.
Koll H, et al. (March 1992). "Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space" (PDF). Cell. 68 (6): 1163–75. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. S2CID 7430067.
Koll H, et al. (1992). "Antifolding Activity of HSP60 Couples Protein Import into the Mitochondrial Matrix with Export to the Intermembrane Space" (PDF). Cell. 68 (6): 1163–75. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. S2CID 7430067.
Hansen JJ, Bross P, Westergaard M, et al. (January 2003). "Genomic structure of the human mitochondrial chaperonin genes: HSP60 and HSP10 are localised head to head on chromosome 2 separated by a bidirectional promoter". Hum. Genet. 112 (1): 71–7. doi:10.1007/s00439-002-0837-9. PMID 12483302. S2CID 25856774.
Vargas-Parada L, Solis C (2001). "Heat Shock and stress response of Taenia solium and T. crassiceps". Parasitology. 122 (5): 583–8. doi:10.1017/s0031182001007764. PMID 11393832. S2CID 41092962.
Calabrese V, Mancuso C, Ravagna A, et al. (May 2007). "In vivo induction of heat shock proteins in the substantia nigra following L-DOPA administration is associated with increased activity of mitochondrial complex I and nitrosative stress in rats: regulation by glutathione redox state". J. Neurochem. 101 (3): 709–17. doi:10.1111/j.1471-4159.2006.04367.x. PMID 17241115. S2CID 6512400.
Lebret T, Watson RW, Molinié V, et al. (September 2003). "Heat shock proteins HSP27, HSP60, HSP70, and HSP90: expression in bladder carcinoma". Cancer. 98 (5): 970–7. doi:10.1002/cncr.11594. PMID 12942564. S2CID 30820581.
Mayhew M, da Silva AC, Martin J, Erdjument-Bromage H, Tempst P, Hartl FU (Feb 1996). "Protein folding in the central cavity of the GroEL-GroES chaperonin complex". Nature. 379 (6564): 420–6. Bibcode:1996Natur.379..420M. doi:10.1038/379420a0. PMID 8559246. S2CID 4310511.

uni-muenchen.de (Global: 3,337^th place; English: 3,444^th place)

epub.ub.uni-muenchen.de

Koll H, et al. (March 1992). "Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space" (PDF). Cell. 68 (6): 1163–75. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. S2CID 7430067.
Koll H, et al. (1992). "Antifolding Activity of HSP60 Couples Protein Import into the Mitochondrial Matrix with Export to the Intermembrane Space" (PDF). Cell. 68 (6): 1163–75. doi:10.1016/0092-8674(92)90086-R. PMID 1347713. S2CID 7430067.

worldcat.org (Global: 5^th place; English: 5^th place)

search.worldcat.org

Kaufman, B. A. (2003). "A function for the mitochondrial chaperonin Hsp60 in the structure and transmission of mitochondrial DNA nucleoids in Saccharomyces cerevisiae". The Journal of Cell Biology. 163 (3): 457–461. doi:10.1083/jcb.200306132. ISSN 0021-9525. PMC 2173642. PMID 14597775.

GroEL (English Wikipedia)

cambridge.org (Global: 305th place; English: 264th place)

journals.cambridge.org

doi.org (Global: 2nd place; English: 2nd place)

ensembl.org (Global: 1,626th place; English: 1,007th place)