Hsp90 (Italian Wikipedia)

Analysis of information sources in references of the Wikipedia article "Hsp90" in Italian language version.

refsWebsite

Global rank Italian rank

13oadoi.org

799^th place

22^nd place

13doi.org

2^nd place

7^th place

13nih.gov

4^th place

9^th place

1linkgroup.hu

low place

1biologists.org

3,870^th place

4,543^rd place

biologists.org (Global: 3,870^th place; Italian: 4,543^rd place)

jcs.biologists.org

G. Crevel, H. Bates, H. Huikeshoven, S. Cotterill, The Drosophila Dpit47 protein is a nuclear Hsp90 co-chaperone that interacts with DNA polymerase alpha^{[collegamento interrotto]}, in J. Cell. Sci., vol. 114, n. 11, giugno 2001, pp. 2015–25.

doi.org (Global: 2^nd place; Italian: 7^th place)

dx.doi.org

P. Csermely, T. Schnaider, C. Soti, Z. Prohászka, G. Nardai, The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review, in Pharmacol. Ther., vol. 79, n. 2, agosto 1998, pp. 129–68, DOI:10.1016/S0163-7258(98)00013-8, PMID 9749880.
M.P. Goetz, D.O. Toft, M.M. Ames, C. Erlichman, The Hsp90 chaperone complex as a novel target for cancer therapy, in Ann. Oncol., vol. 14, n. 8, agosto 2003, pp. 1169–76, DOI:10.1093/annonc/mdg316, PMID 12881371.
L.H. Pearl, C. Prodromou, Structure and in vivo function of Hsp90, in Curr. Opin. Struct. Biol., vol. 10, n. 1, febbraio 2000, pp. 46–51, DOI:10.1016/S0959-440X(99)00047-0, PMID 10679459.
C. Prodromou, L.H. Pearl, Structure and functional relationships of Hsp90, in Curr Cancer Drug Targets, vol. 3, n. 5, ottobre 2003, pp. 301–23, DOI:10.2174/1568009033481877, PMID 14529383.
L.H. Pearl, C. Prodromou, Structure, function, and mechanism of the Hsp90 molecular chaperone, in Adv. Protein Chem., Advances in Protein Chemistry, vol. 59, 2001, pp. 157–86, DOI:10.1016/S0065-3233(01)59005-1, ISBN 978-0-12-034259-4, PMID 11868271.
C.E. Stebbins, A.A. Russo, C. Schneider, N. Rosen, F.U. Hartl, N.P. Pavletich, Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent, in Cell, vol. 89, n. 2, aprile 1997, pp. 239–50, DOI:10.1016/S0092-8674(00)80203-2, PMID 9108479.
C. Prodromou, S.M. Roe, R. O'Brien, J.E. Ladbury, P.W. Piper, L.H. Pearl, Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone, in Cell, vol. 90, n. 1, luglio 1997, pp. 65–75, DOI:10.1016/S0092-8674(00)80314-1, PMID 9230303.
C. Prodromou, S.M. Roe, P.W. Piper, L.H. Pearl, A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone, in Nat. Struct. Biol., vol. 4, n. 6, giugno 1997, pp. 477–82, DOI:10.1038/nsb0697-477, PMID 9187656.
P. Meyer, C. Prodromou, B. Hu, C. Vaughan, S.M. Roe, B. Panaretou, P.W. Piper, L.H. Pearl, Structural andunctional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions, in Mol. Cell, vol. 11, n. 3, marzo 2003, pp. 647–58, DOI:10.1016/S1097-2765(03)00065-0, PMID 12667448.
P. Meyer, C. Prodromou, B. Hu, C. Vaughan, S.M. Roe, B. Panaretou, P.W. Piper, L.H. Pearl, Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions, in Mol. Cell, vol. 11, n. 3, marzo 2003, pp. 647–58, DOI:10.1016/S1097-2765(03)00065-0, PMID 12667448.
A. Sawai, S. Chandarlapaty, H. Greulich, M. Gonen, Q. Ye, C.L. Arteaga, W. Sellers, N. Rosen, D.B. Solit, Inhibition of Hsp90 down-regulates mutant epidermal growth factor receptor (EGFR) expression and sensitizes EGFR mutant tumors to paclitaxel, in Cancer Res., vol. 68, n. 2, gennaio 2008, pp. 589–96, DOI:10.1158/0008-5472.CAN-07-1570, PMID 18199556.
S.K. Mohsin, H.L. Weiss, M.C. Gutierrez, G.C. Chamness, R. Schiff, M.P. Digiovanna, C.X. Wang, S.G. Hilsenbeck, C.K. Osborne, D.C. Allred, R. Elledge, J.C. Chang, Neoadjuvant trastuzumab induces apoptosis in primary breast cancers, in J. Clin. Oncol., vol. 23, n. 11, aprile 2005, pp. 2460–8, DOI:10.1200/JCO.2005.00.661, PMID 15710948.
S.K. Calderwood, M.A. Khaleque, D.B. Sawyer, D.R. Ciocca, Heat shock proteins in cancer: chaperones of tumorigenesis, in Trends in Biochemical Sciences, vol. 31, n. 3, marzo 2006, pp. 164–72, DOI:10.1016/j.tibs.2006.01.006, PMID 16483782.

linkgroup.hu (Global: low place; Italian: low place)

Amere Subbarao Sreedhara, EŁ va Kalmára, Peéter Csermelya, Yu-Fei Shenb, Hsp90 isoforms: functions, expression and clinical importance (PDF), in FEBS Letters, vol. 562, n. 1, 08 03 2004, p. 11.

nih.gov (Global: 4^th place; Italian: 9^th place)

ncbi.nlm.nih.gov

P. Csermely, T. Schnaider, C. Soti, Z. Prohászka, G. Nardai, The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review, in Pharmacol. Ther., vol. 79, n. 2, agosto 1998, pp. 129–68, DOI:10.1016/S0163-7258(98)00013-8, PMID 9749880.
M.P. Goetz, D.O. Toft, M.M. Ames, C. Erlichman, The Hsp90 chaperone complex as a novel target for cancer therapy, in Ann. Oncol., vol. 14, n. 8, agosto 2003, pp. 1169–76, DOI:10.1093/annonc/mdg316, PMID 12881371.
L.H. Pearl, C. Prodromou, Structure and in vivo function of Hsp90, in Curr. Opin. Struct. Biol., vol. 10, n. 1, febbraio 2000, pp. 46–51, DOI:10.1016/S0959-440X(99)00047-0, PMID 10679459.
C. Prodromou, L.H. Pearl, Structure and functional relationships of Hsp90, in Curr Cancer Drug Targets, vol. 3, n. 5, ottobre 2003, pp. 301–23, DOI:10.2174/1568009033481877, PMID 14529383.
L.H. Pearl, C. Prodromou, Structure, function, and mechanism of the Hsp90 molecular chaperone, in Adv. Protein Chem., Advances in Protein Chemistry, vol. 59, 2001, pp. 157–86, DOI:10.1016/S0065-3233(01)59005-1, ISBN 978-0-12-034259-4, PMID 11868271.
C.E. Stebbins, A.A. Russo, C. Schneider, N. Rosen, F.U. Hartl, N.P. Pavletich, Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent, in Cell, vol. 89, n. 2, aprile 1997, pp. 239–50, DOI:10.1016/S0092-8674(00)80203-2, PMID 9108479.
C. Prodromou, S.M. Roe, R. O'Brien, J.E. Ladbury, P.W. Piper, L.H. Pearl, Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone, in Cell, vol. 90, n. 1, luglio 1997, pp. 65–75, DOI:10.1016/S0092-8674(00)80314-1, PMID 9230303.
C. Prodromou, S.M. Roe, P.W. Piper, L.H. Pearl, A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone, in Nat. Struct. Biol., vol. 4, n. 6, giugno 1997, pp. 477–82, DOI:10.1038/nsb0697-477, PMID 9187656.
P. Meyer, C. Prodromou, B. Hu, C. Vaughan, S.M. Roe, B. Panaretou, P.W. Piper, L.H. Pearl, Structural andunctional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions, in Mol. Cell, vol. 11, n. 3, marzo 2003, pp. 647–58, DOI:10.1016/S1097-2765(03)00065-0, PMID 12667448.
P. Meyer, C. Prodromou, B. Hu, C. Vaughan, S.M. Roe, B. Panaretou, P.W. Piper, L.H. Pearl, Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions, in Mol. Cell, vol. 11, n. 3, marzo 2003, pp. 647–58, DOI:10.1016/S1097-2765(03)00065-0, PMID 12667448.
A. Sawai, S. Chandarlapaty, H. Greulich, M. Gonen, Q. Ye, C.L. Arteaga, W. Sellers, N. Rosen, D.B. Solit, Inhibition of Hsp90 down-regulates mutant epidermal growth factor receptor (EGFR) expression and sensitizes EGFR mutant tumors to paclitaxel, in Cancer Res., vol. 68, n. 2, gennaio 2008, pp. 589–96, DOI:10.1158/0008-5472.CAN-07-1570, PMID 18199556.
S.K. Mohsin, H.L. Weiss, M.C. Gutierrez, G.C. Chamness, R. Schiff, M.P. Digiovanna, C.X. Wang, S.G. Hilsenbeck, C.K. Osborne, D.C. Allred, R. Elledge, J.C. Chang, Neoadjuvant trastuzumab induces apoptosis in primary breast cancers, in J. Clin. Oncol., vol. 23, n. 11, aprile 2005, pp. 2460–8, DOI:10.1200/JCO.2005.00.661, PMID 15710948.
S.K. Calderwood, M.A. Khaleque, D.B. Sawyer, D.R. Ciocca, Heat shock proteins in cancer: chaperones of tumorigenesis, in Trends in Biochemical Sciences, vol. 31, n. 3, marzo 2006, pp. 164–72, DOI:10.1016/j.tibs.2006.01.006, PMID 16483782.

oadoi.org (Global: 799^th place; Italian: 22^nd place)

P. Csermely, T. Schnaider, C. Soti, Z. Prohászka, G. Nardai, The 90-kDa molecular chaperone family: structure, function, and clinical applications. A comprehensive review, in Pharmacol. Ther., vol. 79, n. 2, agosto 1998, pp. 129–68, DOI:10.1016/S0163-7258(98)00013-8, PMID 9749880.
M.P. Goetz, D.O. Toft, M.M. Ames, C. Erlichman, The Hsp90 chaperone complex as a novel target for cancer therapy, in Ann. Oncol., vol. 14, n. 8, agosto 2003, pp. 1169–76, DOI:10.1093/annonc/mdg316, PMID 12881371.
L.H. Pearl, C. Prodromou, Structure and in vivo function of Hsp90, in Curr. Opin. Struct. Biol., vol. 10, n. 1, febbraio 2000, pp. 46–51, DOI:10.1016/S0959-440X(99)00047-0, PMID 10679459.
C. Prodromou, L.H. Pearl, Structure and functional relationships of Hsp90, in Curr Cancer Drug Targets, vol. 3, n. 5, ottobre 2003, pp. 301–23, DOI:10.2174/1568009033481877, PMID 14529383.
L.H. Pearl, C. Prodromou, Structure, function, and mechanism of the Hsp90 molecular chaperone, in Adv. Protein Chem., Advances in Protein Chemistry, vol. 59, 2001, pp. 157–86, DOI:10.1016/S0065-3233(01)59005-1, ISBN 978-0-12-034259-4, PMID 11868271.
C.E. Stebbins, A.A. Russo, C. Schneider, N. Rosen, F.U. Hartl, N.P. Pavletich, Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent, in Cell, vol. 89, n. 2, aprile 1997, pp. 239–50, DOI:10.1016/S0092-8674(00)80203-2, PMID 9108479.
C. Prodromou, S.M. Roe, R. O'Brien, J.E. Ladbury, P.W. Piper, L.H. Pearl, Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone, in Cell, vol. 90, n. 1, luglio 1997, pp. 65–75, DOI:10.1016/S0092-8674(00)80314-1, PMID 9230303.
C. Prodromou, S.M. Roe, P.W. Piper, L.H. Pearl, A molecular clamp in the crystal structure of the N-terminal domain of the yeast Hsp90 chaperone, in Nat. Struct. Biol., vol. 4, n. 6, giugno 1997, pp. 477–82, DOI:10.1038/nsb0697-477, PMID 9187656.
P. Meyer, C. Prodromou, B. Hu, C. Vaughan, S.M. Roe, B. Panaretou, P.W. Piper, L.H. Pearl, Structural andunctional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions, in Mol. Cell, vol. 11, n. 3, marzo 2003, pp. 647–58, DOI:10.1016/S1097-2765(03)00065-0, PMID 12667448.
P. Meyer, C. Prodromou, B. Hu, C. Vaughan, S.M. Roe, B. Panaretou, P.W. Piper, L.H. Pearl, Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions, in Mol. Cell, vol. 11, n. 3, marzo 2003, pp. 647–58, DOI:10.1016/S1097-2765(03)00065-0, PMID 12667448.
A. Sawai, S. Chandarlapaty, H. Greulich, M. Gonen, Q. Ye, C.L. Arteaga, W. Sellers, N. Rosen, D.B. Solit, Inhibition of Hsp90 down-regulates mutant epidermal growth factor receptor (EGFR) expression and sensitizes EGFR mutant tumors to paclitaxel, in Cancer Res., vol. 68, n. 2, gennaio 2008, pp. 589–96, DOI:10.1158/0008-5472.CAN-07-1570, PMID 18199556.
S.K. Mohsin, H.L. Weiss, M.C. Gutierrez, G.C. Chamness, R. Schiff, M.P. Digiovanna, C.X. Wang, S.G. Hilsenbeck, C.K. Osborne, D.C. Allred, R. Elledge, J.C. Chang, Neoadjuvant trastuzumab induces apoptosis in primary breast cancers, in J. Clin. Oncol., vol. 23, n. 11, aprile 2005, pp. 2460–8, DOI:10.1200/JCO.2005.00.661, PMID 15710948.
S.K. Calderwood, M.A. Khaleque, D.B. Sawyer, D.R. Ciocca, Heat shock proteins in cancer: chaperones of tumorigenesis, in Trends in Biochemical Sciences, vol. 31, n. 3, marzo 2006, pp. 164–72, DOI:10.1016/j.tibs.2006.01.006, PMID 16483782.

Hsp90 (Italian Wikipedia)

biologists.org (Global: 3,870th place; Italian: 4,543rd place)