Chaperonin (English Wikipedia)

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

refsWebsite

Global rank English rank

30nih.gov

4^th place

21doi.org

2^nd place

10semanticscholar.org

11^th place

8^th place

6harvard.edu

18^th place

17^th place

1web.archive.org

1^st place

1hhmi.org

low place

1handle.net

102^nd place

76^th place

1msu.ru

1,129^th place

6,103^rd place

doi.org

Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature. 371 (6498): 578–86. Bibcode:1994Natur.371..578B. doi:10.1038/371578a0. PMID 7935790. S2CID 4341993.
Conway de Macario E, Yohda M, Macario AJ, Robb FT (2019-03-15). "Bridging human chaperonopathies and microbial chaperonins". Communications Biology. 2 (1): 103. doi:10.1038/s42003-019-0318-5. PMC 6420498. PMID 30911678.
Ansari MY, Mande SC (2018). "A Glimpse Into the Structure and Function of Atypical Type I Chaperonins". Frontiers in Molecular Biosciences. 5: 31. doi:10.3389/fmolb.2018.00031. PMC 5904260. PMID 29696145.
Willison, KR (5 October 2018). "The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring". The Biochemical Journal. 475 (19): 3009–3034. doi:10.1042/BCJ20170378. hdl:10044/1/63924. PMID 30291170. S2CID 52923821.
Fenton WA, Horwich AL (May 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Quarterly Reviews of Biophysics. 36 (2): 229–56. doi:10.1017/S0033583503003883. PMID 14686103. S2CID 10328521.
Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, et al. (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature. 333 (6171): 330–4. Bibcode:1988Natur.333..330H. doi:10.1038/333330a0. PMID 2897629. S2CID 4325057.
Prasad TK, Stewart CR (March 1992). "cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock". Plant Molecular Biology. 18 (5): 873–85. doi:10.1007/BF00019202. PMID 1349837. S2CID 40768099.
Schmidt A, Schiesswohl M, Völker U, Hecker M, Schumann W (June 1992). "Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis". Journal of Bacteriology. 174 (12): 3993–9. doi:10.1128/jb.174.12.3993-3999.1992. PMC 206108. PMID 1350777.
Hindersson P, Høiby N, Bangsborg J (January 1991). "Sequence analysis of the Legionella micdadei groELS operon". FEMS Microbiology Letters. 61 (1): 31–8. doi:10.1111/j.1574-6968.1991.tb04317.x. PMID 1672279.
Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature. 371 (6498): 578–86. Bibcode:1994Natur.371..578B. doi:10.1038/371578a0. PMID 7935790. S2CID 4341993.
Zang Y, Jin M, Wang H, Cui Z, Kong L, Liu C, Cong Y (December 2016). "Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM". Nature Structural & Molecular Biology. 23 (12). Springer Science and Business Media LLC: 1083–1091. doi:10.1038/nsmb.3309. PMID 27775711. S2CID 12001964.
Kusmierczyk AR, Martin J (May 2003). "Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis". The Biochemical Journal. 371 (Pt 3): 669–73. doi:10.1042/BJ20030230. PMC 1223359. PMID 12628000.
Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M (27 April 2020). "Structure and conformational cycle of a bacteriophage-encoded chaperonin". PLOS ONE. 15 (4): e0230090. Bibcode:2020PLoSO..1530090B. doi:10.1371/journal.pone.0230090. PMC 7185714. PMID 32339190.
Hartl FU, Hayer-Hartl M (June 2009). "Converging concepts of protein folding in vitro and in vivo". Nature Structural & Molecular Biology. 16 (6): 574–81. doi:10.1038/nsmb.1591. PMID 19491934. S2CID 205522841.
Apetri AC, Horwich AL (November 2008). "Chaperonin chamber accelerates protein folding through passive action of preventing aggregation". Proceedings of the National Academy of Sciences of the United States of America. 105 (45): 17351–5. Bibcode:2008PNAS..10517351A. doi:10.1073/pnas.0809794105. PMC 2579888. PMID 18987317.
Kmiecik S, Kolinski A (July 2011). "Simulation of chaperonin effect on protein folding: a shift from nucleation-condensation to framework mechanism". Journal of the American Chemical Society. 133 (26): 10283–9. doi:10.1021/ja203275f. PMC 3132998. PMID 21618995.
Chakraborty K, Chatila M, Sinha J, Shi Q, Poschner BC, Sikor M, et al. (July 2010). "Chaperonin-catalyzed rescue of kinetically trapped states in protein folding". Cell. 142 (1): 112–22. doi:10.1016/j.cell.2010.05.027. PMID 20603018. S2CID 3859016.
Todd MJ, Lorimer GH, Thirumalai D (April 1996). "Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism". Proceedings of the National Academy of Sciences of the United States of America. 93 (9): 4030–5. Bibcode:1996PNAS...93.4030T. doi:10.1073/pnas.93.9.4030. PMC 39481. PMID 8633011.
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.
Bukau B, Horwich AL (February 1998). "The Hsp70 and Hsp60 chaperone machines". Cell. 92 (3): 351–66. doi:10.1016/S0092-8674(00)80928-9. PMID 9476895. S2CID 16526409.
Gor D, Mayfield JE (February 1992). "Cloning and nucleotide sequence of the Brucella abortus groE operon". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1130 (1): 120–2. doi:10.1016/0167-4781(92)90476-g. PMID 1347461.

handle.net

hdl.handle.net

Willison, KR (5 October 2018). "The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring". The Biochemical Journal. 475 (19): 3009–3034. doi:10.1042/BCJ20170378. hdl:10044/1/63924. PMID 30291170. S2CID 52923821.

harvard.edu

ui.adsabs.harvard.edu

Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature. 371 (6498): 578–86. Bibcode:1994Natur.371..578B. doi:10.1038/371578a0. PMID 7935790. S2CID 4341993.
Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, et al. (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature. 333 (6171): 330–4. Bibcode:1988Natur.333..330H. doi:10.1038/333330a0. PMID 2897629. S2CID 4325057.
Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature. 371 (6498): 578–86. Bibcode:1994Natur.371..578B. doi:10.1038/371578a0. PMID 7935790. S2CID 4341993.
Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M (27 April 2020). "Structure and conformational cycle of a bacteriophage-encoded chaperonin". PLOS ONE. 15 (4): e0230090. Bibcode:2020PLoSO..1530090B. doi:10.1371/journal.pone.0230090. PMC 7185714. PMID 32339190.
Apetri AC, Horwich AL (November 2008). "Chaperonin chamber accelerates protein folding through passive action of preventing aggregation". Proceedings of the National Academy of Sciences of the United States of America. 105 (45): 17351–5. Bibcode:2008PNAS..10517351A. doi:10.1073/pnas.0809794105. PMC 2579888. PMID 18987317.
Todd MJ, Lorimer GH, Thirumalai D (April 1996). "Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism". Proceedings of the National Academy of Sciences of the United States of America. 93 (9): 4030–5. Bibcode:1996PNAS...93.4030T. doi:10.1073/pnas.93.9.4030. PMC 39481. PMID 8633011.

hhmi.org

"Howard Hughes Investigators: Arthur L. Horwich, M.D." Archived from the original on 2019-07-26. Retrieved 2011-09-12.

msu.ru

protein.bio.msu.ru

Marusich EI, Kurochkina LP, Mesyanzhinov VV (April 1998). "Chaperones in bacteriophage T4 assembly". Biochemistry (Moscow). 63 (4): 399–406. PMID 9556522.

nih.gov

pubmed.ncbi.nlm.nih.gov

Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature. 371 (6498): 578–86. Bibcode:1994Natur.371..578B. doi:10.1038/371578a0. PMID 7935790. S2CID 4341993.
Conway de Macario E, Yohda M, Macario AJ, Robb FT (2019-03-15). "Bridging human chaperonopathies and microbial chaperonins". Communications Biology. 2 (1): 103. doi:10.1038/s42003-019-0318-5. PMC 6420498. PMID 30911678.
Ansari MY, Mande SC (2018). "A Glimpse Into the Structure and Function of Atypical Type I Chaperonins". Frontiers in Molecular Biosciences. 5: 31. doi:10.3389/fmolb.2018.00031. PMC 5904260. PMID 29696145.
Willison, KR (5 October 2018). "The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring". The Biochemical Journal. 475 (19): 3009–3034. doi:10.1042/BCJ20170378. hdl:10044/1/63924. PMID 30291170. S2CID 52923821.
Fenton WA, Horwich AL (May 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Quarterly Reviews of Biophysics. 36 (2): 229–56. doi:10.1017/S0033583503003883. PMID 14686103. S2CID 10328521.
Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, et al. (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature. 333 (6171): 330–4. Bibcode:1988Natur.333..330H. doi:10.1038/333330a0. PMID 2897629. S2CID 4325057.
Prasad TK, Stewart CR (March 1992). "cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock". Plant Molecular Biology. 18 (5): 873–85. doi:10.1007/BF00019202. PMID 1349837. S2CID 40768099.
Schmidt A, Schiesswohl M, Völker U, Hecker M, Schumann W (June 1992). "Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis". Journal of Bacteriology. 174 (12): 3993–9. doi:10.1128/jb.174.12.3993-3999.1992. PMC 206108. PMID 1350777.
Hindersson P, Høiby N, Bangsborg J (January 1991). "Sequence analysis of the Legionella micdadei groELS operon". FEMS Microbiology Letters. 61 (1): 31–8. doi:10.1111/j.1574-6968.1991.tb04317.x. PMID 1672279.
Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature. 371 (6498): 578–86. Bibcode:1994Natur.371..578B. doi:10.1038/371578a0. PMID 7935790. S2CID 4341993.
Zang Y, Jin M, Wang H, Cui Z, Kong L, Liu C, Cong Y (December 2016). "Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM". Nature Structural & Molecular Biology. 23 (12). Springer Science and Business Media LLC: 1083–1091. doi:10.1038/nsmb.3309. PMID 27775711. S2CID 12001964.
Kusmierczyk AR, Martin J (May 2003). "Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis". The Biochemical Journal. 371 (Pt 3): 669–73. doi:10.1042/BJ20030230. PMC 1223359. PMID 12628000.
Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M (27 April 2020). "Structure and conformational cycle of a bacteriophage-encoded chaperonin". PLOS ONE. 15 (4): e0230090. Bibcode:2020PLoSO..1530090B. doi:10.1371/journal.pone.0230090. PMC 7185714. PMID 32339190.
Hartl FU, Hayer-Hartl M (June 2009). "Converging concepts of protein folding in vitro and in vivo". Nature Structural & Molecular Biology. 16 (6): 574–81. doi:10.1038/nsmb.1591. PMID 19491934. S2CID 205522841.
Apetri AC, Horwich AL (November 2008). "Chaperonin chamber accelerates protein folding through passive action of preventing aggregation". Proceedings of the National Academy of Sciences of the United States of America. 105 (45): 17351–5. Bibcode:2008PNAS..10517351A. doi:10.1073/pnas.0809794105. PMC 2579888. PMID 18987317.
Kmiecik S, Kolinski A (July 2011). "Simulation of chaperonin effect on protein folding: a shift from nucleation-condensation to framework mechanism". Journal of the American Chemical Society. 133 (26): 10283–9. doi:10.1021/ja203275f. PMC 3132998. PMID 21618995.
Chakraborty K, Chatila M, Sinha J, Shi Q, Poschner BC, Sikor M, et al. (July 2010). "Chaperonin-catalyzed rescue of kinetically trapped states in protein folding". Cell. 142 (1): 112–22. doi:10.1016/j.cell.2010.05.027. PMID 20603018. S2CID 3859016.
Todd MJ, Lorimer GH, Thirumalai D (April 1996). "Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism". Proceedings of the National Academy of Sciences of the United States of America. 93 (9): 4030–5. Bibcode:1996PNAS...93.4030T. doi:10.1073/pnas.93.9.4030. PMC 39481. PMID 8633011.
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.
Marusich EI, Kurochkina LP, Mesyanzhinov VV (April 1998). "Chaperones in bacteriophage T4 assembly". Biochemistry (Moscow). 63 (4): 399–406. PMID 9556522.
Bukau B, Horwich AL (February 1998). "The Hsp70 and Hsp60 chaperone machines". Cell. 92 (3): 351–66. doi:10.1016/S0092-8674(00)80928-9. PMID 9476895. S2CID 16526409.
Gor D, Mayfield JE (February 1992). "Cloning and nucleotide sequence of the Brucella abortus groE operon". Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression. 1130 (1): 120–2. doi:10.1016/0167-4781(92)90476-g. PMID 1347461.

ncbi.nlm.nih.gov

Conway de Macario E, Yohda M, Macario AJ, Robb FT (2019-03-15). "Bridging human chaperonopathies and microbial chaperonins". Communications Biology. 2 (1): 103. doi:10.1038/s42003-019-0318-5. PMC 6420498. PMID 30911678.
Ansari MY, Mande SC (2018). "A Glimpse Into the Structure and Function of Atypical Type I Chaperonins". Frontiers in Molecular Biosciences. 5: 31. doi:10.3389/fmolb.2018.00031. PMC 5904260. PMID 29696145.
Schmidt A, Schiesswohl M, Völker U, Hecker M, Schumann W (June 1992). "Cloning, sequencing, mapping, and transcriptional analysis of the groESL operon from Bacillus subtilis". Journal of Bacteriology. 174 (12): 3993–9. doi:10.1128/jb.174.12.3993-3999.1992. PMC 206108. PMID 1350777.
Kusmierczyk AR, Martin J (May 2003). "Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis". The Biochemical Journal. 371 (Pt 3): 669–73. doi:10.1042/BJ20030230. PMC 1223359. PMID 12628000.
Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M (27 April 2020). "Structure and conformational cycle of a bacteriophage-encoded chaperonin". PLOS ONE. 15 (4): e0230090. Bibcode:2020PLoSO..1530090B. doi:10.1371/journal.pone.0230090. PMC 7185714. PMID 32339190.
Apetri AC, Horwich AL (November 2008). "Chaperonin chamber accelerates protein folding through passive action of preventing aggregation". Proceedings of the National Academy of Sciences of the United States of America. 105 (45): 17351–5. Bibcode:2008PNAS..10517351A. doi:10.1073/pnas.0809794105. PMC 2579888. PMID 18987317.
Kmiecik S, Kolinski A (July 2011). "Simulation of chaperonin effect on protein folding: a shift from nucleation-condensation to framework mechanism". Journal of the American Chemical Society. 133 (26): 10283–9. doi:10.1021/ja203275f. PMC 3132998. PMID 21618995.
Todd MJ, Lorimer GH, Thirumalai D (April 1996). "Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism". Proceedings of the National Academy of Sciences of the United States of America. 93 (9): 4030–5. Bibcode:1996PNAS...93.4030T. doi:10.1073/pnas.93.9.4030. PMC 39481. PMID 8633011.

semanticscholar.org

api.semanticscholar.org

Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature. 371 (6498): 578–86. Bibcode:1994Natur.371..578B. doi:10.1038/371578a0. PMID 7935790. S2CID 4341993.
Willison, KR (5 October 2018). "The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring". The Biochemical Journal. 475 (19): 3009–3034. doi:10.1042/BCJ20170378. hdl:10044/1/63924. PMID 30291170. S2CID 52923821.
Fenton WA, Horwich AL (May 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Quarterly Reviews of Biophysics. 36 (2): 229–56. doi:10.1017/S0033583503003883. PMID 14686103. S2CID 10328521.
Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, et al. (May 1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature. 333 (6171): 330–4. Bibcode:1988Natur.333..330H. doi:10.1038/333330a0. PMID 2897629. S2CID 4325057.
Prasad TK, Stewart CR (March 1992). "cDNA clones encoding Arabidopsis thaliana and Zea mays mitochondrial chaperonin HSP60 and gene expression during seed germination and heat shock". Plant Molecular Biology. 18 (5): 873–85. doi:10.1007/BF00019202. PMID 1349837. S2CID 40768099.
Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (October 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature. 371 (6498): 578–86. Bibcode:1994Natur.371..578B. doi:10.1038/371578a0. PMID 7935790. S2CID 4341993.
Zang Y, Jin M, Wang H, Cui Z, Kong L, Liu C, Cong Y (December 2016). "Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM". Nature Structural & Molecular Biology. 23 (12). Springer Science and Business Media LLC: 1083–1091. doi:10.1038/nsmb.3309. PMID 27775711. S2CID 12001964.
Hartl FU, Hayer-Hartl M (June 2009). "Converging concepts of protein folding in vitro and in vivo". Nature Structural & Molecular Biology. 16 (6): 574–81. doi:10.1038/nsmb.1591. PMID 19491934. S2CID 205522841.
Chakraborty K, Chatila M, Sinha J, Shi Q, Poschner BC, Sikor M, et al. (July 2010). "Chaperonin-catalyzed rescue of kinetically trapped states in protein folding". Cell. 142 (1): 112–22. doi:10.1016/j.cell.2010.05.027. PMID 20603018. S2CID 3859016.
Bukau B, Horwich AL (February 1998). "The Hsp70 and Hsp60 chaperone machines". Cell. 92 (3): 351–66. doi:10.1016/S0092-8674(00)80928-9. PMID 9476895. S2CID 16526409.

web.archive.org

"Howard Hughes Investigators: Arthur L. Horwich, M.D." Archived from the original on 2019-07-26. Retrieved 2011-09-12.