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10.1007/s12192-017-0776-y http://scihub22266oqcxt.onion/10.1007/s12192-017-0776-y C5352603!5352603 !28220454     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28220454 &cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28220454 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Stress+Chaperones 2017 ; 22 (2 ): 173-189 Nephropedia Template TP {{tp|p=28220454 |t=2017. The remarkable multivalency of the Hsp70 chaperones |pdf=|usr=}}{{28220454 }} gab.com Text The remarkable multivalency of the Hsp70 chaperones JO: Cell Stress Chaperones http://www.kidney.de/pget.php?&tw=1&pmid=28220454 #FOAvip Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases. Twit Text FOAVip The remarkable multivalency of the Hsp70 chaperones ????Cell Stress Chaperones http://www.kidney.de/pget.php?&tw=1&pmid=28220454 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28220454 #FOAvip English Wikipedia <ref>{{Cite pmid|28220454 }}</ref> The remarkable multivalency of the Hsp70 chaperones #MMPMID28220454 Zuiderweg ER ; Hightower LE ; Gestwicki JE Cell Stress Chaperones 2017[Mar]; 22 (2 ): 173-189 PMID28220454 show ga Hsp70 proteins are key to maintaining intracellular protein homeostasis. To carry out this task, they employ a large number of cochaperones and adapter proteins. Here, we review what is known about the interaction between the chaperones and partners, with a strong slant toward structural biology. Hsp70s in general, and Hsc70 (HSPA8) in particular, display an amazing array of interfaces with their protein cofactors. We also review the known interactions between Hsp70s with lipids and with active compounds that may become leads toward Hsp70 modulation for treatment of a variety of diseases. |Adenosine Triphosphate/chemistry/metabolism [MESH] |Escherichia coli Proteins/chemistry/*metabolism [MESH] |Escherichia coli/metabolism [MESH] |HSP70 Heat-Shock Proteins/chemistry/*metabolism [MESH] |Lipids/chemistry [MESH] |Models, Molecular [MESH] |Pharmaceutical Preparations/chemistry/metabolism [MESH] |Protein Binding [MESH]The remarkable multivalency of the Hsp70 chaperones (epmc).pdf DeepDyve Pubget Overpricing