Chaperona (Galician Wikipedia)

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

refsWebsite

Global rank Galician rank

25doi.org

2^nd place

7^th place

24nih.gov

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3archive.org

6^th place

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2web.archive.org

1^st place

2elsevier.com

610^th place

214^th place

1cirp.es

low place

189^th place

1vub.ac.be

low place

1pnas.org

1,293^rd place

271^st place

1archive.today

14^th place

30^th place

1patentstorm.us

low place

1annualreviews.org

3,867^th place

801^st place

annualreviews.org

arjournals.annualreviews.org

Pearl LH, Prodromou C (2006). "Structure and mechanism of the Hsp90 molecular chaperone machinery". Annu. Rev. Biochem. 75: 271–94. PMID 16756493. doi:10.1146/annurev.biochem.75.103004.142738. Arquivado dende o orixinal o 18 de outubro de 2019. Consultado o 24 de decembro de 2012.

archive.org

Ellis RJ (2006). "Molecular chaperones: assisting assembly in addition to folding". Trends in Biochemical Sciences 31 (7): 395–401. PMID 16716593. doi:10.1016/j.tibs.2006.05.001.
Ellis RJ, van der Vies SM (1991). "Molecular chaperones". Annu. Rev. Biochem. 60: 321–47. PMID 1679318. doi:10.1146/annurev.bi.60.070191.001541.
Fenton WA, Horwich AL (2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Q. Rev. Biophys. 36 (2): 229–56. PMID 14686103. doi:10.1017/S0033583503003883.

archive.today

"Soluble complexes of target proteins and peptidyl prolyl isomerase ...". Arquivado dende o orixinal o 21 de abril de 2013. Consultado o 24 de decembro de 2012.

cirp.es

Coordinadores: Jaime Gómez Márquez, Ana Mª Viñas Díaz e Manuel González González. Redactores: David Villar Docampo e Luís Vale Ferreira. Revisores lingüísticos: Víctor Fresco e Mª Liliana Martínez Calvo. (2010). Dicionario de bioloxía galego-castelán-inglés. (PDF). Xunta de Galicia. p. 44. ISBN 978-84-453-4973-1.

doi.org

dx.doi.org

Richardson RT; Alekseev OM; Grossman G; et al. (2006). "Nuclear Autoantigenic Sperm Protein (NASP), a Linker Histone Chaperone That is Required for Cell Proliferation". Journal of Biological Chemistry 281 (30): 21526–34. PMID 16728391. doi:10.1074/jbc.M603816200.
Alekseev OM, Richardson RT, Alekseev O, O'Rand MG (2009). "Analysis of gene expression profiles in HeLa cells in response to overexpression or siRNA-mediated depletion of NASP". Reproductive Biology and Endocrinology 7: 45. PMC 2686705. PMID 19439102. doi:10.1186/1477-7827-7-45.
Ellis RJ (2006). "Molecular chaperones: assisting assembly in addition to folding". Trends in Biochemical Sciences 31 (7): 395–401. PMID 16716593. doi:10.1016/j.tibs.2006.05.001.
Kris Pauwels and other (2007). "Chaperoning Anfinsen:The Steric Foldases" (PDF). Molecular Microbiology 64 (4): 917. doi:10.1111/j.1365-2958.2007.05718.x. Arquivado dende o orixinal (PDF) o 23 de maio de 2012. Consultado o 24 de decembro de 2012.
Ellis RJ, van der Vies SM (1991). "Molecular chaperones". Annu. Rev. Biochem. 60: 321–47. PMID 1679318. doi:10.1146/annurev.bi.60.070191.001541.
van den Berg B, Wain R, Dobson CM, Ellis RJ (2000). "Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell". EMBO J. 19 (15): 3870–5. PMC 306593. PMID 10921869. doi:10.1093/emboj/19.15.3870.
van den Berg B, Ellis RJ, Dobson CM (1999). "Effects of macromolecular crowding on protein folding and aggregation". EMBO J. 18 (24): 6927–33. PMC 1171756. PMID 10601015. doi:10.1093/emboj/18.24.6927.
Ellis RJ, Minton AP (2006). "Protein aggregation in crowded environments". Biol. Chem. 387 (5): 485–97. PMID 16740119. doi:10.1515/BC.2006.064.
Martin J, Hartl FU (1997). "The effect of macromolecular crowding on chaperonin-mediated protein folding". Proc. Natl. Acad. Sci. U.S.A. 94 (4): 1107–12. PMC 19752. PMID 9037014. doi:10.1073/pnas.94.4.1107.
Ellis RJ (2007). "Protein misassembly: macromolecular crowding and molecular chaperones". Adv. Exp. Med. Biol. Advances in Experimental Medicine and Biology 594: 1–13. ISBN 978-0-387-39974-4. PMID 17205670. doi:10.1007/978-0-387-39975-1_1.
Zhou J, Xu Z (2005). "The structural view of bacterial translocation-specific chaperone SecB: implications for function". Molecular Microbiology 58 (2): 349–57. PMID 16194224. doi:10.1111/j.1365-2958.2005.04842.x.
Ruoppolo M, Orrù S, Talamo F, Ljung J, Pirneskoski A, Kivirikko KI, Marino G, Koivunen P (2003). "Mutations in domain a′ of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A". Protein Sci. 12 (5): 939–52. PMC 2323865. PMID 12717017. doi:10.1110/ps.0242803.
Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L (2002). "TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain". Proc. Natl. Acad. Sci. U.S.A. 99 (4): 1954–9. PMC 122301. PMID 11842220. doi:10.1073/pnas.042699099.
Fenton WA, Horwich AL (2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Q. Rev. Biophys. 36 (2): 229–56. PMID 14686103. doi:10.1017/S0033583503003883.
Koll H, Guiard B, Rassow J; et al. (1992). "Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space". Cell 68 (6): 1163–75. PMID 1347713. doi:10.1016/0092-8674(92)90086-R.
Mayer MP, Bukau B (2005). "Hsp70 chaperones: Cellular functions and molecular mechanism". Cell. Mol. Life Sci. 62 (6): 670–84. PMC 2773841. PMID 15770419. doi:10.1007/s00018-004-4464-6.
Vaughan CK; Gohlke U; Sobott F; et al. (2006). "Structure of an Hsp90-Cdc37-Cdk4 complex". Mol. Cell 23 (5): 697–707. PMID 16949366. doi:10.1016/j.molcel.2006.07.016.
Ali MM; Roe SM; Vaughan CK; et al. (2006). "Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex". Nature 440 (7087): 1013–7. PMID 16625188. doi:10.1038/nature04716.
Terasawa K, Minami M, Minami Y (2005). "Constantly updated knowledge of Hsp90". J. Biochem. (Tokyo) 137 (4): 443–7. PMID 15858167. doi:10.1093/jb/mvi056.
Pearl LH, Prodromou C (2006). "Structure and mechanism of the Hsp90 molecular chaperone machinery". Annu. Rev. Biochem. 75: 271–94. PMID 16756493. doi:10.1146/annurev.biochem.75.103004.142738. Arquivado dende o orixinal o 18 de outubro de 2019. Consultado o 24 de decembro de 2012.
Ellis RJ (1996). "Discovery of molecular chaperones". Cell Stress Chaperones 1 (3): 155–60. PMC 248474. PMID 9222600. doi:10.1379/1466-1268(1996)001<0155:DOMC>2.3.CO;2.
Laskey RA, Honda BM, Mills AD, Finch JT (1978). "Nucleosomes are assembled by an acidic protein that binds histones and transfers them to DNA". Nature 275 (5679): 416–20. PMID 692721. doi:10.1038/275416a0.
Ellis J (1987). "Proteins as molecular chaperones". Nature 328 (6129): 378–9. PMID 3112578. doi:10.1038/328378a0.
Hemmingsen SM; Woolford C; van der Vies SM; et al. (1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature 333 (6171): 330–4. PMID 2897629. doi:10.1038/333330a0.
Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH (1989). "Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP". Nature 342 (6252): 884–9. PMID 10532860. doi:10.1038/342884a0.

elsevier.com

linkinghub.elsevier.com

Koll H, Guiard B, Rassow J; et al. (1992). "Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space". Cell 68 (6): 1163–75. PMID 1347713. doi:10.1016/0092-8674(92)90086-R.
Vaughan CK; Gohlke U; Sobott F; et al. (2006). "Structure of an Hsp90-Cdc37-Cdk4 complex". Mol. Cell 23 (5): 697–707. PMID 16949366. doi:10.1016/j.molcel.2006.07.016.

nih.gov

ncbi.nlm.nih.gov

Richardson RT; Alekseev OM; Grossman G; et al. (2006). "Nuclear Autoantigenic Sperm Protein (NASP), a Linker Histone Chaperone That is Required for Cell Proliferation". Journal of Biological Chemistry 281 (30): 21526–34. PMID 16728391. doi:10.1074/jbc.M603816200.
Alekseev OM, Richardson RT, Alekseev O, O'Rand MG (2009). "Analysis of gene expression profiles in HeLa cells in response to overexpression or siRNA-mediated depletion of NASP". Reproductive Biology and Endocrinology 7: 45. PMC 2686705. PMID 19439102. doi:10.1186/1477-7827-7-45.
Ellis RJ (2006). "Molecular chaperones: assisting assembly in addition to folding". Trends in Biochemical Sciences 31 (7): 395–401. PMID 16716593. doi:10.1016/j.tibs.2006.05.001.
Ellis RJ, van der Vies SM (1991). "Molecular chaperones". Annu. Rev. Biochem. 60: 321–47. PMID 1679318. doi:10.1146/annurev.bi.60.070191.001541.
van den Berg B, Wain R, Dobson CM, Ellis RJ (2000). "Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell". EMBO J. 19 (15): 3870–5. PMC 306593. PMID 10921869. doi:10.1093/emboj/19.15.3870.
van den Berg B, Ellis RJ, Dobson CM (1999). "Effects of macromolecular crowding on protein folding and aggregation". EMBO J. 18 (24): 6927–33. PMC 1171756. PMID 10601015. doi:10.1093/emboj/18.24.6927.
Ellis RJ, Minton AP (2006). "Protein aggregation in crowded environments". Biol. Chem. 387 (5): 485–97. PMID 16740119. doi:10.1515/BC.2006.064.
Martin J, Hartl FU (1997). "The effect of macromolecular crowding on chaperonin-mediated protein folding". Proc. Natl. Acad. Sci. U.S.A. 94 (4): 1107–12. PMC 19752. PMID 9037014. doi:10.1073/pnas.94.4.1107.
Ellis RJ (2007). "Protein misassembly: macromolecular crowding and molecular chaperones". Adv. Exp. Med. Biol. Advances in Experimental Medicine and Biology 594: 1–13. ISBN 978-0-387-39974-4. PMID 17205670. doi:10.1007/978-0-387-39975-1_1.
Zhou J, Xu Z (2005). "The structural view of bacterial translocation-specific chaperone SecB: implications for function". Molecular Microbiology 58 (2): 349–57. PMID 16194224. doi:10.1111/j.1365-2958.2005.04842.x.
Ruoppolo M, Orrù S, Talamo F, Ljung J, Pirneskoski A, Kivirikko KI, Marino G, Koivunen P (2003). "Mutations in domain a′ of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A". Protein Sci. 12 (5): 939–52. PMC 2323865. PMID 12717017. doi:10.1110/ps.0242803.
Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L (2002). "TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain". Proc. Natl. Acad. Sci. U.S.A. 99 (4): 1954–9. PMC 122301. PMID 11842220. doi:10.1073/pnas.042699099.
Fenton WA, Horwich AL (2003). "Chaperonin-mediated protein folding: fate of substrate polypeptide". Q. Rev. Biophys. 36 (2): 229–56. PMID 14686103. doi:10.1017/S0033583503003883.
Koll H, Guiard B, Rassow J; et al. (1992). "Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space". Cell 68 (6): 1163–75. PMID 1347713. doi:10.1016/0092-8674(92)90086-R.
Mayer MP, Bukau B (2005). "Hsp70 chaperones: Cellular functions and molecular mechanism". Cell. Mol. Life Sci. 62 (6): 670–84. PMC 2773841. PMID 15770419. doi:10.1007/s00018-004-4464-6.
Vaughan CK; Gohlke U; Sobott F; et al. (2006). "Structure of an Hsp90-Cdc37-Cdk4 complex". Mol. Cell 23 (5): 697–707. PMID 16949366. doi:10.1016/j.molcel.2006.07.016.
Ali MM; Roe SM; Vaughan CK; et al. (2006). "Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex". Nature 440 (7087): 1013–7. PMID 16625188. doi:10.1038/nature04716.
Terasawa K, Minami M, Minami Y (2005). "Constantly updated knowledge of Hsp90". J. Biochem. (Tokyo) 137 (4): 443–7. PMID 15858167. doi:10.1093/jb/mvi056.
Pearl LH, Prodromou C (2006). "Structure and mechanism of the Hsp90 molecular chaperone machinery". Annu. Rev. Biochem. 75: 271–94. PMID 16756493. doi:10.1146/annurev.biochem.75.103004.142738. Arquivado dende o orixinal o 18 de outubro de 2019. Consultado o 24 de decembro de 2012.
Ellis RJ (1996). "Discovery of molecular chaperones". Cell Stress Chaperones 1 (3): 155–60. PMC 248474. PMID 9222600. doi:10.1379/1466-1268(1996)001<0155:DOMC>2.3.CO;2.
Laskey RA, Honda BM, Mills AD, Finch JT (1978). "Nucleosomes are assembled by an acidic protein that binds histones and transfers them to DNA". Nature 275 (5679): 416–20. PMID 692721. doi:10.1038/275416a0.
Ellis J (1987). "Proteins as molecular chaperones". Nature 328 (6129): 378–9. PMID 3112578. doi:10.1038/328378a0.
Hemmingsen SM; Woolford C; van der Vies SM; et al. (1988). "Homologous plant and bacterial proteins chaperone oligomeric protein assembly". Nature 333 (6171): 330–4. PMID 2897629. doi:10.1038/333330a0.
Goloubinoff P, Christeller JT, Gatenby AA, Lorimer GH (1989). "Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfoleded state depends on two chaperonin proteins and Mg-ATP". Nature 342 (6252): 884–9. PMID 10532860. doi:10.1038/342884a0.

patentstorm.us

"Soluble complexes of target proteins and peptidyl prolyl isomerase ...". Arquivado dende o orixinal o 21 de abril de 2013. Consultado o 24 de decembro de 2012.

pnas.org

Martin J, Hartl FU (1997). "The effect of macromolecular crowding on chaperonin-mediated protein folding". Proc. Natl. Acad. Sci. U.S.A. 94 (4): 1107–12. PMC 19752. PMID 9037014. doi:10.1073/pnas.94.4.1107.

vub.ac.be

ultr23.vub.ac.be

Kris Pauwels and other (2007). "Chaperoning Anfinsen:The Steric Foldases" (PDF). Molecular Microbiology 64 (4): 917. doi:10.1111/j.1365-2958.2007.05718.x. Arquivado dende o orixinal (PDF) o 23 de maio de 2012. Consultado o 24 de decembro de 2012.

web.archive.org

Kris Pauwels and other (2007). "Chaperoning Anfinsen:The Steric Foldases" (PDF). Molecular Microbiology 64 (4): 917. doi:10.1111/j.1365-2958.2007.05718.x. Arquivado dende o orixinal (PDF) o 23 de maio de 2012. Consultado o 24 de decembro de 2012.
Pearl LH, Prodromou C (2006). "Structure and mechanism of the Hsp90 molecular chaperone machinery". Annu. Rev. Biochem. 75: 271–94. PMID 16756493. doi:10.1146/annurev.biochem.75.103004.142738. Arquivado dende o orixinal o 18 de outubro de 2019. Consultado o 24 de decembro de 2012.