Hsp70 (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "Hsp70" in Japanese language version.

refsWebsite

Global rank Japanese rank

31nih.gov

4^th place

24^th place

23doi.org

2^nd place

6^th place

4harvard.edu

18^th place

107^th place

1amolf.nl

low place

1wiley.com

222^nd place

498^th place

1dropbox.com

1,209^th place

2,948^th place

amolf.nl

request.pub.amolf.nl

“Alternative modes of client binding enable functional plasticity of Hsp70”. Nature 539 (7629): 448–451. (November 2016). Bibcode: 2016Natur.539..448M. doi:10.1038/nature20137. PMID 27783598.

doi.org

“Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein”. Nature 346 (6285): 623–8. (August 1990). Bibcode: 1990Natur.346..623F. doi:10.1038/346623a0. PMID 2143562.
“A hitchhiker's guide to the human Hsp70 family”. Cell Stress & Chaperones 1 (1): 23–8. (April 1996). doi:10.1379/1466-1268(1996)001<0023:AHSGTT>2.3.CO;2. PMC 313013. PMID 9222585.
“New tricks for an old dog: the evolving world of Hsp70”. Annals of the New York Academy of Sciences 1113 (1): 1–14. (October 2007). Bibcode: 2007NYASA1113....1M. doi:10.1196/annals.1391.018. PMID 17513460.
“Hsp70 in cancer: A double agent in the battle between survival and death”. Journal of Cellular Physiology: jcp.30132. (November 2020). doi:10.1002/jcp.30132. PMID 33169384.
“Gymnastics of molecular chaperones”. Molecular Cell 39 (3): 321–31. (August 2010). doi:10.1016/j.molcel.2010.07.012. PMID 20705236.
“Alternative modes of client binding enable functional plasticity of Hsp70”. Nature 539 (7629): 448–451. (November 2016). Bibcode: 2016Natur.539..448M. doi:10.1038/nature20137. PMID 27783598.
“Hsp70 in cancer: A double agent in the battle between survival and death”. Journal of Cellular Physiology. (November 2020). doi:10.1002/jcp.30132. PMID 33169384.
“GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones”. Sub-Cellular Biochemistry. Subcellular Biochemistry 78: 1–33. (2015). doi:10.1007/978-3-319-11731-7_1. ISBN 978-3-319-11730-0. PMID 25487014.
Hsp70 and Hsp90 – a relay team for protein folding. Reviews of Physiology, Biochemistry and Pharmacology. 151. (2004). 1–44. doi:10.1007/s10254-003-0021-1. ISBN 978-3-540-22096-1. PMID 14740253
“The level and phosphorylation of Hsp70 in the rat liver cytosol after adrenalectomy and hyperthermia”. Cell Biology International 23 (4): 313–20. (1999-04-01). doi:10.1006/cbir.1998.0247. PMID 10600240.
“The turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C”. The Journal of Biological Chemistry 277 (35): 31585–92. (August 2002). doi:10.1074/jbc.M204335200. PMID 12080070.
“CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression” (英語). Cell 151 (6): 1308–18. (December 2012). doi:10.1016/j.cell.2012.10.051. PMC 3778871. PMID 23217712.
“C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances”. Oncogene 32 (25): 3101–10. (June 2013). doi:10.1038/onc.2012.314. PMID 22824801.
“The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome”. The Journal of Biological Chemistry 275 (7): 4613–7. (February 2000). doi:10.1074/jbc.275.7.4613. PMID 10671488.
“Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome”. Nature Cell Biology 2 (8): 469–75. (August 2000). doi:10.1038/35019501. PMID 10934466.
“HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction”. PLoS Biology 8 (7): e1000410. (July 2010). doi:10.1371/journal.pbio.1000410. PMC 2897763. PMID 20625543.
“Long-term prognostic significance of HSP-70, c-myc and HLA-DR expression in patients with malignant melanoma”. European Journal of Surgical Oncology 27 (1): 88–93. (February 2001). doi:10.1053/ejso.1999.1018. PMID 11237497.
“Expression of heat shock protein 70 in renal cell carcinoma and its relation to tumor progression and prognosis”. Histology and Histopathology 22 (10): 1099–107. (October 2007). doi:10.14670/HH-22.1099. PMID 17616937.
“Heat shock proteins in cancer”. Annals of the New York Academy of Sciences 1113 (1): 192–201. (October 2007). Bibcode: 2007NYASA1113..192S. doi:10.1196/annals.1391.030. PMID 17978282.
“Systematic Proteomic Identification of the Heat Shock Proteins (Hsp) that Interact with Estrogen Receptor Alpha (ERα) and Biochemical Characterization of the ERα-Hsp70 Interaction”. PLOS One 11 (8): e0160312. (2016). doi:10.1371/journal.pone.0160312. PMID 27483141.
“Expression of heat shock proteins 70 and 47 in tissues following short-pulse laser irradiation: assessment of thermal damage and healing”. Medical Engineering & Physics 35 (10): 1406–14. (October 2013). doi:10.1016/j.medengphy.2013.03.011. PMID 23587755.
“Hsc62, Hsc56, and GrpE, the third Hsp70 chaperone system of Escherichia coli”. Biochemical and Biophysical Research Communications 293 (5): 1389–95. (May 2002). doi:10.1016/S0006-291X(02)00403-5. PMID 12054669.
“Guidelines for the nomenclature of the human heat shock proteins”. Cell Stress & Chaperones 14 (1): 105–11. (January 2009). doi:10.1007/s12192-008-0068-7. PMC 2673902. PMID 18663603.

dropbox.com

“Expression of heat shock proteins 70 and 47 in tissues following short-pulse laser irradiation: assessment of thermal damage and healing”. Medical Engineering & Physics 35 (10): 1406–14. (October 2013). doi:10.1016/j.medengphy.2013.03.011. PMID 23587755.

harvard.edu

ui.adsabs.harvard.edu

“Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein”. Nature 346 (6285): 623–8. (August 1990). Bibcode: 1990Natur.346..623F. doi:10.1038/346623a0. PMID 2143562.
“New tricks for an old dog: the evolving world of Hsp70”. Annals of the New York Academy of Sciences 1113 (1): 1–14. (October 2007). Bibcode: 2007NYASA1113....1M. doi:10.1196/annals.1391.018. PMID 17513460.
“Alternative modes of client binding enable functional plasticity of Hsp70”. Nature 539 (7629): 448–451. (November 2016). Bibcode: 2016Natur.539..448M. doi:10.1038/nature20137. PMID 27783598.
“Heat shock proteins in cancer”. Annals of the New York Academy of Sciences 1113 (1): 192–201. (October 2007). Bibcode: 2007NYASA1113..192S. doi:10.1196/annals.1391.030. PMID 17978282.

nih.gov

pubmed.ncbi.nlm.nih.gov

“Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein”. Nature 346 (6285): 623–8. (August 1990). Bibcode: 1990Natur.346..623F. doi:10.1038/346623a0. PMID 2143562.
“A hitchhiker's guide to the human Hsp70 family”. Cell Stress & Chaperones 1 (1): 23–8. (April 1996). doi:10.1379/1466-1268(1996)001<0023:AHSGTT>2.3.CO;2. PMC 313013. PMID 9222585.
“New tricks for an old dog: the evolving world of Hsp70”. Annals of the New York Academy of Sciences 1113 (1): 1–14. (October 2007). Bibcode: 2007NYASA1113....1M. doi:10.1196/annals.1391.018. PMID 17513460.
“Hsp70 in cancer: A double agent in the battle between survival and death”. Journal of Cellular Physiology: jcp.30132. (November 2020). doi:10.1002/jcp.30132. PMID 33169384.
“Gymnastics of molecular chaperones”. Molecular Cell 39 (3): 321–31. (August 2010). doi:10.1016/j.molcel.2010.07.012. PMID 20705236.
“Alternative modes of client binding enable functional plasticity of Hsp70”. Nature 539 (7629): 448–451. (November 2016). Bibcode: 2016Natur.539..448M. doi:10.1038/nature20137. PMID 27783598.
“Hsp70 in cancer: A double agent in the battle between survival and death”. Journal of Cellular Physiology. (November 2020). doi:10.1002/jcp.30132. PMID 33169384.
“GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones”. Sub-Cellular Biochemistry. Subcellular Biochemistry 78: 1–33. (2015). doi:10.1007/978-3-319-11731-7_1. ISBN 978-3-319-11730-0. PMID 25487014.
Hsp70 and Hsp90 – a relay team for protein folding. Reviews of Physiology, Biochemistry and Pharmacology. 151. (2004). 1–44. doi:10.1007/s10254-003-0021-1. ISBN 978-3-540-22096-1. PMID 14740253
“The level and phosphorylation of Hsp70 in the rat liver cytosol after adrenalectomy and hyperthermia”. Cell Biology International 23 (4): 313–20. (1999-04-01). doi:10.1006/cbir.1998.0247. PMID 10600240.
“The turn motif is a phosphorylation switch that regulates the binding of Hsp70 to protein kinase C”. The Journal of Biological Chemistry 277 (35): 31585–92. (August 2002). doi:10.1074/jbc.M204335200. PMID 12080070.
“CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression” (英語). Cell 151 (6): 1308–18. (December 2012). doi:10.1016/j.cell.2012.10.051. PMC 3778871. PMID 23217712.
“C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances”. Oncogene 32 (25): 3101–10. (June 2013). doi:10.1038/onc.2012.314. PMID 22824801.
“The ubiquitin-related BAG-1 provides a link between the molecular chaperones Hsc70/Hsp70 and the proteasome”. The Journal of Biological Chemistry 275 (7): 4613–7. (February 2000). doi:10.1074/jbc.275.7.4613. PMID 10671488.
“Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome”. Nature Cell Biology 2 (8): 469–75. (August 2000). doi:10.1038/35019501. PMID 10934466.
“HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction”. PLoS Biology 8 (7): e1000410. (July 2010). doi:10.1371/journal.pbio.1000410. PMC 2897763. PMID 20625543.
“Long-term prognostic significance of HSP-70, c-myc and HLA-DR expression in patients with malignant melanoma”. European Journal of Surgical Oncology 27 (1): 88–93. (February 2001). doi:10.1053/ejso.1999.1018. PMID 11237497.
“Expression of heat shock protein 70 in renal cell carcinoma and its relation to tumor progression and prognosis”. Histology and Histopathology 22 (10): 1099–107. (October 2007). doi:10.14670/HH-22.1099. PMID 17616937.
“Heat shock proteins in cancer”. Annals of the New York Academy of Sciences 1113 (1): 192–201. (October 2007). Bibcode: 2007NYASA1113..192S. doi:10.1196/annals.1391.030. PMID 17978282.
“Systematic Proteomic Identification of the Heat Shock Proteins (Hsp) that Interact with Estrogen Receptor Alpha (ERα) and Biochemical Characterization of the ERα-Hsp70 Interaction”. PLOS One 11 (8): e0160312. (2016). doi:10.1371/journal.pone.0160312. PMID 27483141.
“Expression of heat shock proteins 70 and 47 in tissues following short-pulse laser irradiation: assessment of thermal damage and healing”. Medical Engineering & Physics 35 (10): 1406–14. (October 2013). doi:10.1016/j.medengphy.2013.03.011. PMID 23587755.
“Hsc62, Hsc56, and GrpE, the third Hsp70 chaperone system of Escherichia coli”. Biochemical and Biophysical Research Communications 293 (5): 1389–95. (May 2002). doi:10.1016/S0006-291X(02)00403-5. PMID 12054669.
“Guidelines for the nomenclature of the human heat shock proteins”. Cell Stress & Chaperones 14 (1): 105–11. (January 2009). doi:10.1007/s12192-008-0068-7. PMC 2673902. PMID 18663603.

ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

wiley.com

onlinelibrary.wiley.com

“Hsp70 in cancer: A double agent in the battle between survival and death”. Journal of Cellular Physiology. (November 2020). doi:10.1002/jcp.30132. PMID 33169384.