Probing the role of Arg97 in Heat shock protein 90 N-terminal domain from the parasite Leishmania braziliensis through site-directed mutagenesis on the human counterpart

2018 ◽  
Vol 1866 (11) ◽  
pp. 1190-1198 ◽  
Author(s):  
Giusy Tassone ◽  
Stefano Mangani ◽  
Maurizio Botta ◽  
Cecilia Pozzi
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Leishmania Braziliensis ◽  
Terminal Domain ◽  
Human Counterpart ◽  
Parasite Leishmania

scholarly journals Heat Shock Protein 90 as Therapeutic Target for CVDs and Heart Ageing

2022 ◽  
Vol 23 (2) ◽  
pp. 649
Author(s):  
Siarhei A. Dabravolski ◽  
Vasily N. Sukhorukov ◽  
Vladislav A. Kalmykov ◽  
Nikolay A. Orekhov ◽  
Andrey V. Grechko ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperones ◽  
Heat Shock Protein 90 ◽  
Misfolded Proteins ◽  
Heart Cells ◽  
Metabolic Demand ◽  
Heart Protection ◽  
High Metabolic Demand

Cardiovascular diseases (CVDs) are the leading cause of death globally, representing approximately 32% of all deaths worldwide. Molecular chaperones are involved in heart protection against stresses and age-mediated accumulation of toxic misfolded proteins by regulation of the protein synthesis/degradation balance and refolding of misfolded proteins, thus supporting the high metabolic demand of the heart cells. Heat shock protein 90 (HSP90) is one of the main cardioprotective chaperones, represented by cytosolic HSP90a and HSP90b, mitochondrial TRAP1 and ER-localised Grp94 isoforms. Currently, the main way to study the functional role of HSPs is the application of HSP inhibitors, which could have a different way of action. In this review, we discussed the recently investigated role of HSP90 proteins in cardioprotection, atherosclerosis, CVDs development and the involvements of HSP90 clients in the activation of different molecular pathways and signalling mechanisms, related to heart ageing.

scholarly journals The Amino-terminal Domain of Heat Shock Protein 90 (hsp90) That Binds Geldanamycin Is an ATP/ADP Switch Domain That Regulates hsp90 Conformation

1997 ◽  
Vol 272 (38) ◽  
pp. 23843-23850 ◽  
Author(s):  
James P. Grenert ◽  
William P. Sullivan ◽  
Patrick Fadden ◽  
Timothy A. J. Haystead ◽  
Jenny Clark ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Amino Terminal Domain

Role of heat shock protein 90 in bradykinin-stimulated endothelial nitric oxide release

2000 ◽  
Vol 35 (3) ◽  
pp. 165-170 ◽  
Author(s):  
M.Brennan Harris ◽  
Hong Ju ◽  
Virginia J. Venema ◽  
Michele Blackstone ◽  
Richard C. Venema
Keyword(s):  
Nitric Oxide ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90 ◽  
Nitric Oxide Release ◽  
Endothelial Nitric Oxide

scholarly journals Mechanisms of Disease: the role of heat-shock protein 90 in genitourinary malignancy

2006 ◽  
Vol 3 (11) ◽  
pp. 590-601 ◽  
Author(s):  
Jean-Baptiste Lattouf ◽  
Ramaprasad Srinivasan ◽  
Peter A Pinto ◽  
W Marston Linehan ◽  
Leonard Neckers
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 90
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