Chaperonina (Galician Wikipedia)

Analysis of information sources in references of the Wikipedia article "Chaperonina" in Galician language version.

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12nih.gov

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2harvard.edu

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1web.archive.org

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1hhmi.org

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archive.org

Fenton WA, Horwich AL (maio de 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Q. Rev. Biophys. 36 (2): 229–56. PMID 14686103. doi:10.1017/S0033583503003883.

doi.org

dx.doi.org

Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (outubro de 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature 371 (6498): 578–86. Bibcode:1994Natur.371..578B. PMID 7935790. doi:10.1038/371578a0.
Conway de Macario E, Yohda M, Macario AJ, Robb FT (2019-03-15). "Bridging human chaperonopathies and microbial chaperonins". Communications Biology 2 (1): 103. PMC 6420498. PMID 30911678. doi:10.1038/s42003-019-0318-5.
Ansari MY, Mande SC (2018). "A Glimpse Into the Structure and Function of Atypical Type I Chaperonins". Frontiers in Molecular Biosciences 5: 31. PMC 5904260. PMID 29696145. doi:10.3389/fmolb.2018.00031.
Willison, KR (5 de outubro de 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. PMID 30291170. doi:10.1042/BCJ20170378. hdl:10044/1/63924.
Fenton WA, Horwich AL (maio de 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Q. Rev. Biophys. 36 (2): 229–56. PMID 14686103. doi:10.1017/S0033583503003883.
Kusmierczyk AR, Martin J (maio de 2003). "Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis.". Biochem. J. 371 (3): 669–673. PMC 1223359. PMID 12628000. doi:10.1042/BJ20030230.
Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M (27 de abril de 2020). "Structure and conformational cycle of a bacteriophage-encoded chaperonin". PLOS ONE 15 (4): e0230090. Bibcode:2020PLoSO..1530090B. PMC 7185714. PMID 32339190. doi:10.1371/journal.pone.0230090.
Hartl, FU; Hayer-Hartl, M (2009). "Converging concepts of protein folding in vitro and in vivo". Nature Structural & Molecular Biology 16 (6): 574–581. PMID 19491934. doi:10.1038/nsmb.1591.
Apetri, AC; Horwich, AL (2008). "Chaperonin chamber accelerates protein folding through passive action of preventing aggregation". Proceedings of the National Academy of Sciences 105 (45): 17351–17355. PMC 2579888. PMID 18987317. doi:10.1073/pnas.0809794105.
Kmiecik, S; Kolinski, A (2011). "Simulation of Chaperonin Effect on Protein Folding: A Shift from Nucleation–Condensation to Framework Mechanism". Journal of the American Chemical Society 133 (26): 10283–10289. PMC 3132998. PMID 21618995. doi:10.1021/ja203275f.
Chakraborty, K; Chatila, M; Sinha, J; Shi, Q; Poschner, BC; Sikor, M; Jiang, G; Lamb, DC; Hartl, FU; Hayer-Hartl, M (2010). "Chaperonin-Catalyzed Rescue of Kinetically Trapped States in Protein Folding". Cell 142 (1): 112–122. PMID 20603018. doi:10.1016/j.cell.2010.05.027.
Todd, MJ; Lorimer, GH; Thirumalai, D. (1996). "Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.". Proceedings of the National Academy of Sciences 93 (9): 4030–4035. ISSN 0027-8424. PMC 39481. doi:10.1073/pnas.93.9.4030.

handle.net

hdl.handle.net

Willison, KR (5 de outubro de 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. PMID 30291170. doi:10.1042/BCJ20170378. hdl:10044/1/63924.

harvard.edu

adsabs.harvard.edu

Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (outubro de 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature 371 (6498): 578–86. Bibcode:1994Natur.371..578B. PMID 7935790. doi:10.1038/371578a0.
Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M (27 de abril de 2020). "Structure and conformational cycle of a bacteriophage-encoded chaperonin". PLOS ONE 15 (4): e0230090. Bibcode:2020PLoSO..1530090B. PMC 7185714. PMID 32339190. doi:10.1371/journal.pone.0230090.

hhmi.org

"Howard Hughes Investigators: Arthur L. Horwich, M.D.". Arquivado dende o orixinal o 26 de xullo de 2019. Consultado o 28 de decembro de 2018.

nih.gov

ncbi.nlm.nih.gov

Braig K, Otwinowski Z, Hegde R, Boisvert DC, Joachimiak A, Horwich AL, Sigler PB (outubro de 1994). "The crystal structure of the bacterial chaperonin GroEL at 2.8 A". Nature 371 (6498): 578–86. Bibcode:1994Natur.371..578B. PMID 7935790. doi:10.1038/371578a0.
Conway de Macario E, Yohda M, Macario AJ, Robb FT (2019-03-15). "Bridging human chaperonopathies and microbial chaperonins". Communications Biology 2 (1): 103. PMC 6420498. PMID 30911678. doi:10.1038/s42003-019-0318-5.
Ansari MY, Mande SC (2018). "A Glimpse Into the Structure and Function of Atypical Type I Chaperonins". Frontiers in Molecular Biosciences 5: 31. PMC 5904260. PMID 29696145. doi:10.3389/fmolb.2018.00031.
Willison, KR (5 de outubro de 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. PMID 30291170. doi:10.1042/BCJ20170378. hdl:10044/1/63924.
Fenton WA, Horwich AL (maio de 2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Q. Rev. Biophys. 36 (2): 229–56. PMID 14686103. doi:10.1017/S0033583503003883.
Kusmierczyk AR, Martin J (maio de 2003). "Nucleotide-dependent protein folding in the type II chaperonin from the mesophilic archaeon Methanococcus maripaludis.". Biochem. J. 371 (3): 669–673. PMC 1223359. PMID 12628000. doi:10.1042/BJ20030230.
Bracher A, Paul SS, Wang H, Wischnewski N, Hartl FU, Hayer-Hartl M (27 de abril de 2020). "Structure and conformational cycle of a bacteriophage-encoded chaperonin". PLOS ONE 15 (4): e0230090. Bibcode:2020PLoSO..1530090B. PMC 7185714. PMID 32339190. doi:10.1371/journal.pone.0230090.
Hartl, FU; Hayer-Hartl, M (2009). "Converging concepts of protein folding in vitro and in vivo". Nature Structural & Molecular Biology 16 (6): 574–581. PMID 19491934. doi:10.1038/nsmb.1591.
Apetri, AC; Horwich, AL (2008). "Chaperonin chamber accelerates protein folding through passive action of preventing aggregation". Proceedings of the National Academy of Sciences 105 (45): 17351–17355. PMC 2579888. PMID 18987317. doi:10.1073/pnas.0809794105.
Kmiecik, S; Kolinski, A (2011). "Simulation of Chaperonin Effect on Protein Folding: A Shift from Nucleation–Condensation to Framework Mechanism". Journal of the American Chemical Society 133 (26): 10283–10289. PMC 3132998. PMID 21618995. doi:10.1021/ja203275f.
Chakraborty, K; Chatila, M; Sinha, J; Shi, Q; Poschner, BC; Sikor, M; Jiang, G; Lamb, DC; Hartl, FU; Hayer-Hartl, M (2010). "Chaperonin-Catalyzed Rescue of Kinetically Trapped States in Protein Folding". Cell 142 (1): 112–122. PMID 20603018. doi:10.1016/j.cell.2010.05.027.
Todd, MJ; Lorimer, GH; Thirumalai, D. (1996). "Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.". Proceedings of the National Academy of Sciences 93 (9): 4030–4035. ISSN 0027-8424. PMC 39481. doi:10.1073/pnas.93.9.4030.

web.archive.org

"Howard Hughes Investigators: Arthur L. Horwich, M.D.". Arquivado dende o orixinal o 26 de xullo de 2019. Consultado o 28 de decembro de 2018.

worldcat.org

Todd, MJ; Lorimer, GH; Thirumalai, D. (1996). "Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism.". Proceedings of the National Academy of Sciences 93 (9): 4030–4035. ISSN 0027-8424. PMC 39481. doi:10.1073/pnas.93.9.4030.