Use my Search Websuite to scan PubMed, PMCentral, Journal Hosts and Journal Archives, FullText. Kick-your-searchterm to multiple Engines kick-your-query now !>

A dictionary by aggregated review articles of nephrology, medicine and the life sciences Your one-stop-run pathway from word to the immediate pdf of peer-reviewed on-topic knowledge.

10.1073/pnas.1414073111 http://scihub22266oqcxt.onion/10.1073/pnas.1414073111 C4273377!4273377 !25468961     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25468961 &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 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 229.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\25468961 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Proc+Natl+Acad+Sci+U+S+A 2014 ; 111 (50 ): 17881-6 Nephropedia Template TP {{tp|p=25468961 |t=2014. The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function |pdf=|usr=}}{{25468961 }} gab.com Text The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25468961 #FOAvip The heat shock protein 90 (Hsp90) is a dimeric molecular chaperone essential in numerous cellular processes. Its three domains (N, M, and C) are connected via linkers that allow the rearrangement of domains during Hsp90's chaperone cycle. A unique linker, called charged linker (CL), connects the N- and M-domain of Hsp90. We used an integrated approach, combining single-molecule techniques and biochemical and in vivo methods, to study the unresolved structure and function of this region. Here we show that the CL facilitates intramolecular rearrangements on the milliseconds timescale between a state in which the N-domain is docked to the M-domain and a state in which the N-domain is more flexible. The docked conformation is stabilized by 1.1 kBT (2.7 kJ/mol) through binding of the CL to the N-domain of Hsp90. Docking and undocking of the CL affects the much slower intermolecular domain movement and Hsp90's chaperone cycle governing client activation, cell viability, and stress tolerance. Twit Text FOAVip The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=25468961 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25468961 #FOAvip English Wikipedia <ref>{{Cite pmid|25468961 }}</ref> The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function #MMPMID25468961 Jahn M ; Rehn A ; Pelz B ; Hellenkamp B ; Richter K ; Rief M ; Buchner J ; Hugel T Proc Natl Acad Sci U S A 2014[Dec]; 111 (50 ): 17881-6 PMID25468961 show ga The heat shock protein 90 (Hsp90) is a dimeric molecular chaperone essential in numerous cellular processes. Its three domains (N, M, and C) are connected via linkers that allow the rearrangement of domains during Hsp90's chaperone cycle. A unique linker, called charged linker (CL), connects the N- and M-domain of Hsp90. We used an integrated approach, combining single-molecule techniques and biochemical and in vivo methods, to study the unresolved structure and function of this region. Here we show that the CL facilitates intramolecular rearrangements on the milliseconds timescale between a state in which the N-domain is docked to the M-domain and a state in which the N-domain is more flexible. The docked conformation is stabilized by 1.1 kBT (2.7 kJ/mol) through binding of the CL to the N-domain of Hsp90. Docking and undocking of the CL affects the much slower intermolecular domain movement and Hsp90's chaperone cycle governing client activation, cell viability, and stress tolerance. |*Models, Molecular [MESH] |Blotting, Western [MESH] |Cross-Linking Reagents/*chemistry [MESH] |Electrophoresis, Polyacrylamide Gel [MESH] |Fluorescence [MESH] |Fluorescence Resonance Energy Transfer [MESH] |HSP90 Heat-Shock Proteins/*chemistry/*metabolism [MESH] |Immunoblotting [MESH] |Optical Tweezers [MESH] |Protein Structure, Tertiary [MESH] |Saccharomyces cerevisiae Proteins/*chemistry/*metabolism [MESH]The charged linker of the molecular chaperone Hsp90 modulates domain c(epmc).pdf DeepDyve Pubget Overpricing