Chaperone (protein) (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Chaperone (protein)" in English language version.

refsWebsite

Global rank English rank

54nih.gov

4^th place

35doi.org

2^nd place

13semanticscholar.org

11^th place

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10harvard.edu

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2handle.net

102^nd place

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1acs.org

1,248^th place

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1archive.org

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1web.archive.org

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1vub.ac.be

low place

1umich.edu

459^th place

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1archive.today

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acs.org

pubs.acs.org

[Chaperone Action at the Single-Molecule Level http://pubs.acs.org/doi/abs/10.1021/cr400326k]

archive.org

Ellis RJ (2007). "Protein Misassembly". Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks. Advances in Experimental Medicine and Biology. Vol. 594. New York, N.Y.: Sprinter Science+Business Media, LLC ; Austin, Tex.: Landes Bioscience/Eurekah.com. pp. 1–13. doi:10.1007/978-0-387-39975-1_1. ISBN 978-0-387-39974-4. PMID 17205670.

archive.today

Soluble complexes of target proteins and peptidyl prolyl isomerase ...

doi.org

Richardson RT, Alekseev OM, Grossman G, Widgren EE, Thresher R, Wagner EJ, et al. (July 2006). "Nuclear autoantigenic sperm protein (NASP), a linker histone chaperone that is required for cell proliferation". The Journal of Biological Chemistry. 281 (30): 21526–34. doi:10.1074/jbc.M603816200. PMID 16728391.
Alekseev OM, Richardson RT, Alekseev O, O'Rand MG (May 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. doi:10.1186/1477-7827-7-45. PMC 2686705. PMID 19439102.
Ellis RJ, van der Vies SM (1991). "Molecular chaperones". Annual Review of Biochemistry. 60: 321–347. doi:10.1146/annurev.bi.60.070191.001541. PMID 1679318.
Bascos NA, Landry SJ (December 2019). "A History of Molecular Chaperone Structures in the Protein Data Bank". International Journal of Molecular Sciences. 20 (24): 6195. doi:10.3390/ijms20246195. PMC 6940948. PMID 31817979.
Hoffmann JH, Linke K, Graf PC, Lilie H, Jakob U (January 2004). "Identification of a redox-regulated chaperone network". The EMBO Journal. 23 (1): 160–8. doi:10.1038/sj.emboj.7600016. PMC 1271656. PMID 14685279.
Nillegoda NB, Kirstein J, Szlachcic A, Berynskyy M, Stank A, Stengel F, et al. (August 2015). "Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation". Nature. 524 (7564): 247–51. Bibcode:2015Natur.524..247N. doi:10.1038/nature14884. PMC 4830470. PMID 26245380.
Balchin D, Hayer-Hartl M, Hartl FU (July 2016). "In vivo aspects of protein folding and quality control". Science. 353 (6294): aac4354. doi:10.1126/science.aac4354. hdl:11858/00-001M-0000-002B-0856-C. PMID 27365453. S2CID 5174431.
van den Berg B, Wain R, Dobson CM, Ellis RJ (August 2000). "Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell". The EMBO Journal. 19 (15): 3870–5. doi:10.1093/emboj/19.15.3870. PMC 306593. PMID 10921869.
van den Berg B, Ellis RJ, Dobson CM (December 1999). "Effects of macromolecular crowding on protein folding and aggregation". The EMBO Journal. 18 (24): 6927–33. doi:10.1093/emboj/18.24.6927. PMC 1171756. PMID 10601015.
Ellis RJ, Minton AP (May 2006). "Protein aggregation in crowded environments". Biological Chemistry. 387 (5): 485–97. doi:10.1515/BC.2006.064. PMID 16740119. S2CID 7336464.
Martin J, Hartl FU (February 1997). "The effect of macromolecular crowding on chaperonin-mediated protein folding". Proceedings of the National Academy of Sciences of the United States of America. 94 (4): 1107–12. Bibcode:1997PNAS...94.1107M. doi:10.1073/pnas.94.4.1107. PMC 19752. PMID 9037014.
Ellis RJ (2007). "Protein Misassembly". Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks. Advances in Experimental Medicine and Biology. Vol. 594. New York, N.Y.: Sprinter Science+Business Media, LLC ; Austin, Tex.: Landes Bioscience/Eurekah.com. pp. 1–13. doi:10.1007/978-0-387-39975-1_1. ISBN 978-0-387-39974-4. PMID 17205670.
Pauwels K, Van Molle I, Tommassen J, Van Gelder P (May 2007). "Chaperoning Anfinsen: the steric foldases" (PDF). Molecular Microbiology. 64 (4): 917–22. doi:10.1111/j.1365-2958.2007.05718.x. PMID 17501917. S2CID 6435829. Archived from the original (PDF) on 2012-05-23.
Zhou J, Xu Z (October 2005). "The structural view of bacterial translocation-specific chaperone SecB: implications for function" (PDF). Molecular Microbiology. 58 (2): 349–57. doi:10.1111/j.1365-2958.2005.04842.x. hdl:2027.42/74325. PMID 16194224. S2CID 33227532.
Specht S, Miller SB, Mogk A, Bukau B (14 November 2011). "Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae". J. Cell Biol. 195 (4): 617–29. doi:10.1083/jcb.201106037. PMC 3257523. PMID 22065637.
Ojha J, Masilamoni G, Dunlap D, Udoff RA, Cashikar AG (August 2011). "Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism". Mol. Cell. Biol. 31 (15): 3146–57. doi:10.1128/MCB.01187-10. PMC 3147607. PMID 21670152.
Mannini B, Cascella R, Zampagni M, van Waarde-Verhagen M, Meehan S, Roodveldt C, Campioni S, Boninsegna M, Penco A, Relini A, Kampinga HH, Dobson CM, Wilson MR, Cecchi C, Chiti F (31 July 2012). "Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers". Proc. Natl. Acad. Sci. USA. 109 (31): 12479–84. Bibcode:2012PNAS..10912479M. doi:10.1073/pnas.1117799109. PMC 3411936. PMID 22802614.
Sadigh-Eteghad S, Majdi A, Talebi M, Mahmoudi J, Babri S (May 2015). "Regulation of nicotinic acetylcholine receptors in Alzheimer׳s disease: a possible role of chaperones". European Journal of Pharmacology. 755: 34–41. doi:10.1016/j.ejphar.2015.02.047. PMID 25771456. S2CID 31929001.
Salamanca HH, Antonyak MA, Cerione RA, Shi H, Lis JT (2014). "Inhibiting heat shock factor 1 in human cancer cells with a potent RNA aptamer". PLOS ONE. 9 (5): e96330. Bibcode:2014PLoSO...996330S. doi:10.1371/journal.pone.0096330. PMC 4011729. PMID 24800749.
Finka A, Goloubinoff P (September 2013). "Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis". Cell Stress & Chaperones. 18 (5): 591–605. doi:10.1007/s12192-013-0413-3. PMC 3745260. PMID 23430704.
Ruoppolo M, Orrù S, Talamo F, Ljung J, Pirneskoski A, Kivirikko KI, et al. (May 2003). "Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A". Protein Science. 12 (5): 939–52. doi:10.1110/ps.0242803. PMC 2323865. PMID 12717017.
Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L (February 2002). "TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain". Proceedings of the National Academy of Sciences of the United States of America. 99 (4): 1954–9. Bibcode:2002PNAS...99.1954F. doi:10.1073/pnas.042699099. PMC 122301. PMID 11842220.
Smith, Tracy (1 December 1999). "The discovery of chaperonins". Nature Structural Biology. 6 (12): 1090. doi:10.1038/70015. PMID 10581544. S2CID 6158370.
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.
Yochem, J; Uchida, H; Sunshine, M; Saito, H; Georgopoulos, CP; Feiss, M (4 August 1978). "Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication". Molecular & General Genetics. 164 (1): 9–14. doi:10.1007/BF00267593. PMID 360041. S2CID 28144214.
Mayer MP, Bukau B (March 2005). "Hsp70 chaperones: cellular functions and molecular mechanism". Cellular and Molecular Life Sciences. 62 (6): 670–84. doi:10.1007/s00018-004-4464-6. PMC 2773841. PMID 15770419.
Vaughan CK, Gohlke U, Sobott F, Good VM, Ali MM, Prodromou C, et al. (September 2006). "Structure of an Hsp90-Cdc37-Cdk4 complex". Molecular Cell. 23 (5): 697–707. doi:10.1016/j.molcel.2006.07.016. PMC 5704897. PMID 16949366.
Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, et al. (April 2006). "Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex". Nature. 440 (7087): 1013–7. Bibcode:2006Natur.440.1013A. doi:10.1038/nature04716. PMC 5703407. PMID 16625188.
Terasawa K, Minami M, Minami Y (April 2005). "Constantly updated knowledge of Hsp90". Journal of Biochemistry. 137 (4): 443–7. doi:10.1093/jb/mvi056. PMID 15858167.
Pearl LH, Prodromou C (2006). "Structure and mechanism of the Hsp90 molecular chaperone machinery". Annual Review of Biochemistry. 75: 271–94. doi:10.1146/annurev.biochem.75.103004.142738. PMID 16756493.
Laskey RA, Honda BM, Mills AD, Finch JT (October 1978). "Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA". Nature. 275 (5679): 416–20. Bibcode:1978Natur.275..416L. doi:10.1038/275416a0. PMID 692721. S2CID 2535641.
Ellis J (1987). "Proteins as molecular chaperones". Nature. 328 (6129): 378–9. Bibcode:1987Natur.328..378E. doi:10.1038/328378a0. PMID 3112578. S2CID 4337273.
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.
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. Bibcode:1989Natur.342..884G. doi:10.1038/342884a0. PMID 10532860. S2CID 4319510.
Taylor JP (August 2015). "Multisystem proteinopathy: intersecting genetics in muscle, bone, and brain degeneration". Neurology. 85 (8): 658–60. doi:10.1212/WNL.0000000000001862. PMID 26208960. S2CID 42203997.

handle.net

hdl.handle.net

Balchin D, Hayer-Hartl M, Hartl FU (July 2016). "In vivo aspects of protein folding and quality control". Science. 353 (6294): aac4354. doi:10.1126/science.aac4354. hdl:11858/00-001M-0000-002B-0856-C. PMID 27365453. S2CID 5174431.
Zhou J, Xu Z (October 2005). "The structural view of bacterial translocation-specific chaperone SecB: implications for function" (PDF). Molecular Microbiology. 58 (2): 349–57. doi:10.1111/j.1365-2958.2005.04842.x. hdl:2027.42/74325. PMID 16194224. S2CID 33227532.

harvard.edu

ui.adsabs.harvard.edu

Nillegoda NB, Kirstein J, Szlachcic A, Berynskyy M, Stank A, Stengel F, et al. (August 2015). "Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation". Nature. 524 (7564): 247–51. Bibcode:2015Natur.524..247N. doi:10.1038/nature14884. PMC 4830470. PMID 26245380.
Martin J, Hartl FU (February 1997). "The effect of macromolecular crowding on chaperonin-mediated protein folding". Proceedings of the National Academy of Sciences of the United States of America. 94 (4): 1107–12. Bibcode:1997PNAS...94.1107M. doi:10.1073/pnas.94.4.1107. PMC 19752. PMID 9037014.
Mannini B, Cascella R, Zampagni M, van Waarde-Verhagen M, Meehan S, Roodveldt C, Campioni S, Boninsegna M, Penco A, Relini A, Kampinga HH, Dobson CM, Wilson MR, Cecchi C, Chiti F (31 July 2012). "Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers". Proc. Natl. Acad. Sci. USA. 109 (31): 12479–84. Bibcode:2012PNAS..10912479M. doi:10.1073/pnas.1117799109. PMC 3411936. PMID 22802614.
Salamanca HH, Antonyak MA, Cerione RA, Shi H, Lis JT (2014). "Inhibiting heat shock factor 1 in human cancer cells with a potent RNA aptamer". PLOS ONE. 9 (5): e96330. Bibcode:2014PLoSO...996330S. doi:10.1371/journal.pone.0096330. PMC 4011729. PMID 24800749.
Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L (February 2002). "TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain". Proceedings of the National Academy of Sciences of the United States of America. 99 (4): 1954–9. Bibcode:2002PNAS...99.1954F. doi:10.1073/pnas.042699099. PMC 122301. PMID 11842220.
Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, et al. (April 2006). "Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex". Nature. 440 (7087): 1013–7. Bibcode:2006Natur.440.1013A. doi:10.1038/nature04716. PMC 5703407. PMID 16625188.
Laskey RA, Honda BM, Mills AD, Finch JT (October 1978). "Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA". Nature. 275 (5679): 416–20. Bibcode:1978Natur.275..416L. doi:10.1038/275416a0. PMID 692721. S2CID 2535641.
Ellis J (1987). "Proteins as molecular chaperones". Nature. 328 (6129): 378–9. Bibcode:1987Natur.328..378E. doi:10.1038/328378a0. PMID 3112578. S2CID 4337273.
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.
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. Bibcode:1989Natur.342..884G. doi:10.1038/342884a0. PMID 10532860. S2CID 4319510.

nih.gov

pubmed.ncbi.nlm.nih.gov

Richardson RT, Alekseev OM, Grossman G, Widgren EE, Thresher R, Wagner EJ, et al. (July 2006). "Nuclear autoantigenic sperm protein (NASP), a linker histone chaperone that is required for cell proliferation". The Journal of Biological Chemistry. 281 (30): 21526–34. doi:10.1074/jbc.M603816200. PMID 16728391.
Alekseev OM, Richardson RT, Alekseev O, O'Rand MG (May 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. doi:10.1186/1477-7827-7-45. PMC 2686705. PMID 19439102.
Ellis RJ, van der Vies SM (1991). "Molecular chaperones". Annual Review of Biochemistry. 60: 321–347. doi:10.1146/annurev.bi.60.070191.001541. PMID 1679318.
Bascos NA, Landry SJ (December 2019). "A History of Molecular Chaperone Structures in the Protein Data Bank". International Journal of Molecular Sciences. 20 (24): 6195. doi:10.3390/ijms20246195. PMC 6940948. PMID 31817979.
Hoffmann JH, Linke K, Graf PC, Lilie H, Jakob U (January 2004). "Identification of a redox-regulated chaperone network". The EMBO Journal. 23 (1): 160–8. doi:10.1038/sj.emboj.7600016. PMC 1271656. PMID 14685279.
Nillegoda NB, Kirstein J, Szlachcic A, Berynskyy M, Stank A, Stengel F, et al. (August 2015). "Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation". Nature. 524 (7564): 247–51. Bibcode:2015Natur.524..247N. doi:10.1038/nature14884. PMC 4830470. PMID 26245380.
Balchin D, Hayer-Hartl M, Hartl FU (July 2016). "In vivo aspects of protein folding and quality control". Science. 353 (6294): aac4354. doi:10.1126/science.aac4354. hdl:11858/00-001M-0000-002B-0856-C. PMID 27365453. S2CID 5174431.
van den Berg B, Wain R, Dobson CM, Ellis RJ (August 2000). "Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell". The EMBO Journal. 19 (15): 3870–5. doi:10.1093/emboj/19.15.3870. PMC 306593. PMID 10921869.
van den Berg B, Ellis RJ, Dobson CM (December 1999). "Effects of macromolecular crowding on protein folding and aggregation". The EMBO Journal. 18 (24): 6927–33. doi:10.1093/emboj/18.24.6927. PMC 1171756. PMID 10601015.
Ellis RJ, Minton AP (May 2006). "Protein aggregation in crowded environments". Biological Chemistry. 387 (5): 485–97. doi:10.1515/BC.2006.064. PMID 16740119. S2CID 7336464.
Martin J, Hartl FU (February 1997). "The effect of macromolecular crowding on chaperonin-mediated protein folding". Proceedings of the National Academy of Sciences of the United States of America. 94 (4): 1107–12. Bibcode:1997PNAS...94.1107M. doi:10.1073/pnas.94.4.1107. PMC 19752. PMID 9037014.
Ellis RJ (2007). "Protein Misassembly". Molecular Aspects of the Stress Response: Chaperones, Membranes and Networks. Advances in Experimental Medicine and Biology. Vol. 594. New York, N.Y.: Sprinter Science+Business Media, LLC ; Austin, Tex.: Landes Bioscience/Eurekah.com. pp. 1–13. doi:10.1007/978-0-387-39975-1_1. ISBN 978-0-387-39974-4. PMID 17205670.
Pauwels K, Van Molle I, Tommassen J, Van Gelder P (May 2007). "Chaperoning Anfinsen: the steric foldases" (PDF). Molecular Microbiology. 64 (4): 917–22. doi:10.1111/j.1365-2958.2007.05718.x. PMID 17501917. S2CID 6435829. Archived from the original (PDF) on 2012-05-23.
Zhou J, Xu Z (October 2005). "The structural view of bacterial translocation-specific chaperone SecB: implications for function" (PDF). Molecular Microbiology. 58 (2): 349–57. doi:10.1111/j.1365-2958.2005.04842.x. hdl:2027.42/74325. PMID 16194224. S2CID 33227532.
Specht S, Miller SB, Mogk A, Bukau B (14 November 2011). "Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae". J. Cell Biol. 195 (4): 617–29. doi:10.1083/jcb.201106037. PMC 3257523. PMID 22065637.
Ojha J, Masilamoni G, Dunlap D, Udoff RA, Cashikar AG (August 2011). "Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism". Mol. Cell. Biol. 31 (15): 3146–57. doi:10.1128/MCB.01187-10. PMC 3147607. PMID 21670152.
Mannini B, Cascella R, Zampagni M, van Waarde-Verhagen M, Meehan S, Roodveldt C, Campioni S, Boninsegna M, Penco A, Relini A, Kampinga HH, Dobson CM, Wilson MR, Cecchi C, Chiti F (31 July 2012). "Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers". Proc. Natl. Acad. Sci. USA. 109 (31): 12479–84. Bibcode:2012PNAS..10912479M. doi:10.1073/pnas.1117799109. PMC 3411936. PMID 22802614.
Sadigh-Eteghad S, Majdi A, Talebi M, Mahmoudi J, Babri S (May 2015). "Regulation of nicotinic acetylcholine receptors in Alzheimer׳s disease: a possible role of chaperones". European Journal of Pharmacology. 755: 34–41. doi:10.1016/j.ejphar.2015.02.047. PMID 25771456. S2CID 31929001.
Salamanca HH, Antonyak MA, Cerione RA, Shi H, Lis JT (2014). "Inhibiting heat shock factor 1 in human cancer cells with a potent RNA aptamer". PLOS ONE. 9 (5): e96330. Bibcode:2014PLoSO...996330S. doi:10.1371/journal.pone.0096330. PMC 4011729. PMID 24800749.
Finka A, Goloubinoff P (September 2013). "Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis". Cell Stress & Chaperones. 18 (5): 591–605. doi:10.1007/s12192-013-0413-3. PMC 3745260. PMID 23430704.
Ruoppolo M, Orrù S, Talamo F, Ljung J, Pirneskoski A, Kivirikko KI, et al. (May 2003). "Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A". Protein Science. 12 (5): 939–52. doi:10.1110/ps.0242803. PMC 2323865. PMID 12717017.
Frickel EM, Riek R, Jelesarov I, Helenius A, Wuthrich K, Ellgaard L (February 2002). "TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain". Proceedings of the National Academy of Sciences of the United States of America. 99 (4): 1954–9. Bibcode:2002PNAS...99.1954F. doi:10.1073/pnas.042699099. PMC 122301. PMID 11842220.
Smith, Tracy (1 December 1999). "The discovery of chaperonins". Nature Structural Biology. 6 (12): 1090. doi:10.1038/70015. PMID 10581544. S2CID 6158370.
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.
Yochem, J; Uchida, H; Sunshine, M; Saito, H; Georgopoulos, CP; Feiss, M (4 August 1978). "Genetic analysis of two genes, dnaJ and dnaK, necessary for Escherichia coli and bacteriophage lambda DNA replication". Molecular & General Genetics. 164 (1): 9–14. doi:10.1007/BF00267593. PMID 360041. S2CID 28144214.
Mayer MP, Bukau B (March 2005). "Hsp70 chaperones: cellular functions and molecular mechanism". Cellular and Molecular Life Sciences. 62 (6): 670–84. doi:10.1007/s00018-004-4464-6. PMC 2773841. PMID 15770419.
Vaughan CK, Gohlke U, Sobott F, Good VM, Ali MM, Prodromou C, et al. (September 2006). "Structure of an Hsp90-Cdc37-Cdk4 complex". Molecular Cell. 23 (5): 697–707. doi:10.1016/j.molcel.2006.07.016. PMC 5704897. PMID 16949366.
Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, et al. (April 2006). "Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex". Nature. 440 (7087): 1013–7. Bibcode:2006Natur.440.1013A. doi:10.1038/nature04716. PMC 5703407. PMID 16625188.
Terasawa K, Minami M, Minami Y (April 2005). "Constantly updated knowledge of Hsp90". Journal of Biochemistry. 137 (4): 443–7. doi:10.1093/jb/mvi056. PMID 15858167.
Pearl LH, Prodromou C (2006). "Structure and mechanism of the Hsp90 molecular chaperone machinery". Annual Review of Biochemistry. 75: 271–94. doi:10.1146/annurev.biochem.75.103004.142738. PMID 16756493.
Ellis RJ (September 1996). "Discovery of molecular chaperones". Cell Stress & Chaperones. 1 (3): 155–60. PMC 248474. PMID 9222600.
Laskey RA, Honda BM, Mills AD, Finch JT (October 1978). "Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA". Nature. 275 (5679): 416–20. Bibcode:1978Natur.275..416L. doi:10.1038/275416a0. PMID 692721. S2CID 2535641.
Ellis J (1987). "Proteins as molecular chaperones". Nature. 328 (6129): 378–9. Bibcode:1987Natur.328..378E. doi:10.1038/328378a0. PMID 3112578. S2CID 4337273.
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.
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. Bibcode:1989Natur.342..884G. doi:10.1038/342884a0. PMID 10532860. S2CID 4319510.
Taylor JP (August 2015). "Multisystem proteinopathy: intersecting genetics in muscle, bone, and brain degeneration". Neurology. 85 (8): 658–60. doi:10.1212/WNL.0000000000001862. PMID 26208960. S2CID 42203997.

ncbi.nlm.nih.gov

Alekseev OM, Richardson RT, Alekseev O, O'Rand MG (May 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. doi:10.1186/1477-7827-7-45. PMC 2686705. PMID 19439102.
Bascos NA, Landry SJ (December 2019). "A History of Molecular Chaperone Structures in the Protein Data Bank". International Journal of Molecular Sciences. 20 (24): 6195. doi:10.3390/ijms20246195. PMC 6940948. PMID 31817979.
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Pauwels K, Van Molle I, Tommassen J, Van Gelder P (May 2007). "Chaperoning Anfinsen: the steric foldases" (PDF). Molecular Microbiology. 64 (4): 917–22. doi:10.1111/j.1365-2958.2007.05718.x. PMID 17501917. S2CID 6435829. Archived from the original (PDF) on 2012-05-23.