Chaperone DnaJ (English Wikipedia)

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

refsWebsite

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12nih.gov

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8doi.org

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3semanticscholar.org

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1harvard.edu

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doi.org

Qiu XB, Shao YM, Miao S, Wang L (November 2006). "The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones". Cellular and Molecular Life Sciences. 63 (22): 2560–70. doi:10.1007/s00018-006-6192-6. PMC 11136209. PMID 16952052. S2CID 21325339.
Caplan AJ, Cyr DM, Douglas MG (June 1993). "Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins". Molecular Biology of the Cell. 4 (6): 555–63. doi:10.1091/mbc.4.6.555. PMC 300962. PMID 8374166.
Douglas MG, Cyr DM, Langer T (1994). "DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70". Trends Biochem. Sci. 19 (4): 176–181. doi:10.1016/0968-0004(94)90281-x. PMID 8016869.
Hennessy F, Nicoll WS, Zimmermann R, Cheetham ME, Blatch GL (July 2005). "Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions". Protein Science. 14 (7): 1697–709. doi:10.1110/ps.051406805. PMC 2253343. PMID 15987899.
Fan CY, Lee S, Cyr DM (2003). "Mechanisms for regulation of Hsp70 function by Hsp40". Cell Stress & Chaperones. 8 (4): 309–16. doi:10.1379/1466-1268(2003)008<0309:mfrohf>2.0.co;2. PMC 514902. PMID 15115283.
Ohtsuka K, Hata M (2000). "Molecular chaperone function of mammalian Hsp70 and Hsp40--a review". International Journal of Hyperthermia. 16 (3): 231–45. doi:10.1080/026567300285259. PMID 10830586. S2CID 22622220.
Christen P, Han W (2004). "cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides". FEBS Lett. 563 (1): 146–150. Bibcode:2004FEBSL.563..146H. doi:10.1016/S0014-5793(04)00290-X. PMID 15063739. S2CID 11050399.
Martinez-Yamout, M.; Legge, G. B.; Zhang, O.; Wright, P. E.; Dyson, H. J. (2000). "Solution Structure of the Cysteine-rich Domain of the Escherichia coli Chaperone Protein DnaJ☆☆☆". Journal of Molecular Biology. 300 (4): 805–818. doi:10.1006/jmbi.2000.3923. PMID 10891270.

harvard.edu

ui.adsabs.harvard.edu

Christen P, Han W (2004). "cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides". FEBS Lett. 563 (1): 146–150. Bibcode:2004FEBSL.563..146H. doi:10.1016/S0014-5793(04)00290-X. PMID 15063739. S2CID 11050399.

nih.gov

pubmed.ncbi.nlm.nih.gov

Qiu XB, Shao YM, Miao S, Wang L (November 2006). "The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones". Cellular and Molecular Life Sciences. 63 (22): 2560–70. doi:10.1007/s00018-006-6192-6. PMC 11136209. PMID 16952052. S2CID 21325339.
Caplan AJ, Cyr DM, Douglas MG (June 1993). "Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins". Molecular Biology of the Cell. 4 (6): 555–63. doi:10.1091/mbc.4.6.555. PMC 300962. PMID 8374166.
Douglas MG, Cyr DM, Langer T (1994). "DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70". Trends Biochem. Sci. 19 (4): 176–181. doi:10.1016/0968-0004(94)90281-x. PMID 8016869.
Hennessy F, Nicoll WS, Zimmermann R, Cheetham ME, Blatch GL (July 2005). "Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions". Protein Science. 14 (7): 1697–709. doi:10.1110/ps.051406805. PMC 2253343. PMID 15987899.
Fan CY, Lee S, Cyr DM (2003). "Mechanisms for regulation of Hsp70 function by Hsp40". Cell Stress & Chaperones. 8 (4): 309–16. doi:10.1379/1466-1268(2003)008<0309:mfrohf>2.0.co;2. PMC 514902. PMID 15115283.
Ohtsuka K, Hata M (2000). "Molecular chaperone function of mammalian Hsp70 and Hsp40--a review". International Journal of Hyperthermia. 16 (3): 231–45. doi:10.1080/026567300285259. PMID 10830586. S2CID 22622220.
Christen P, Han W (2004). "cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides". FEBS Lett. 563 (1): 146–150. Bibcode:2004FEBSL.563..146H. doi:10.1016/S0014-5793(04)00290-X. PMID 15063739. S2CID 11050399.
Martinez-Yamout, M.; Legge, G. B.; Zhang, O.; Wright, P. E.; Dyson, H. J. (2000). "Solution Structure of the Cysteine-rich Domain of the Escherichia coli Chaperone Protein DnaJ☆☆☆". Journal of Molecular Biology. 300 (4): 805–818. doi:10.1006/jmbi.2000.3923. PMID 10891270.

ncbi.nlm.nih.gov

Qiu XB, Shao YM, Miao S, Wang L (November 2006). "The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones". Cellular and Molecular Life Sciences. 63 (22): 2560–70. doi:10.1007/s00018-006-6192-6. PMC 11136209. PMID 16952052. S2CID 21325339.
Caplan AJ, Cyr DM, Douglas MG (June 1993). "Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins". Molecular Biology of the Cell. 4 (6): 555–63. doi:10.1091/mbc.4.6.555. PMC 300962. PMID 8374166.
Hennessy F, Nicoll WS, Zimmermann R, Cheetham ME, Blatch GL (July 2005). "Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions". Protein Science. 14 (7): 1697–709. doi:10.1110/ps.051406805. PMC 2253343. PMID 15987899.
Fan CY, Lee S, Cyr DM (2003). "Mechanisms for regulation of Hsp70 function by Hsp40". Cell Stress & Chaperones. 8 (4): 309–16. doi:10.1379/1466-1268(2003)008<0309:mfrohf>2.0.co;2. PMC 514902. PMID 15115283.

semanticscholar.org

api.semanticscholar.org

Qiu XB, Shao YM, Miao S, Wang L (November 2006). "The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones". Cellular and Molecular Life Sciences. 63 (22): 2560–70. doi:10.1007/s00018-006-6192-6. PMC 11136209. PMID 16952052. S2CID 21325339.
Ohtsuka K, Hata M (2000). "Molecular chaperone function of mammalian Hsp70 and Hsp40--a review". International Journal of Hyperthermia. 16 (3): 231–45. doi:10.1080/026567300285259. PMID 10830586. S2CID 22622220.
Christen P, Han W (2004). "cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides". FEBS Lett. 563 (1): 146–150. Bibcode:2004FEBSL.563..146H. doi:10.1016/S0014-5793(04)00290-X. PMID 15063739. S2CID 11050399.