Hsp40 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "Hsp40" in Japanese language version.

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14nih.gov

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doi.org

“The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones”. Cellular and Molecular Life Sciences 63 (22): 2560–70. (November 2006). doi:10.1007/s00018-006-6192-6. PMID 16952052.
“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. (June 1993). doi:10.1091/mbc.4.6.555. PMC 300962. PMID 8374166.
“DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70”. Trends Biochem. Sci. 19 (4): 176–181. (1994). doi:10.1016/0968-0004(94)90281-x. PMID 8016869.
“Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions”. Protein Science 14 (7): 1697–709. (July 2005). doi:10.1110/ps.051406805. PMC 2253343. PMID 15987899.
“Molecular chaperone function of mammalian Hsp70 and Hsp40--a review”. International Journal of Hyperthermia 16 (3): 231–45. (2000). doi:10.1080/026567300285259. PMID 10830586.
“cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides”. FEBS Lett. 563 (1): 146–150. (2004). doi:10.1016/S0014-5793(04)00290-X. PMID 15063739.
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.

nih.gov

pubmed.ncbi.nlm.nih.gov

“The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones”. Cellular and Molecular Life Sciences 63 (22): 2560–70. (November 2006). doi:10.1007/s00018-006-6192-6. PMID 16952052.
“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. (June 1993). doi:10.1091/mbc.4.6.555. PMC 300962. PMID 8374166.
“DnaJ-like proteins: molecular chaperones and specific regulators of Hsp70”. Trends Biochem. Sci. 19 (4): 176–181. (1994). doi:10.1016/0968-0004(94)90281-x. PMID 8016869.
“Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions”. Protein Science 14 (7): 1697–709. (July 2005). doi:10.1110/ps.051406805. PMC 2253343. PMID 15987899.
“Mechanisms for regulation of Hsp70 function by Hsp40”. Cell Stress & Chaperones 8 (4): 309–16. (2003). PMC 514902. PMID 15115283.
“Molecular chaperone function of mammalian Hsp70 and Hsp40--a review”. International Journal of Hyperthermia 16 (3): 231–45. (2000). doi:10.1080/026567300285259. PMID 10830586.
“cis-Effect of DnaJ on DnaK in ternary complexes with chimeric DnaK/DnaJ-binding peptides”. FEBS Lett. 563 (1): 146–150. (2004). doi:10.1016/S0014-5793(04)00290-X. PMID 15063739.
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.

Hsp40 (Japanese Wikipedia)

doi.org

nih.gov

pubmed.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov