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10.1186/s11658-016-0020-2 http://scihub22266oqcxt.onion/10.1186/s11658-016-0020-2 C5415834!5415834 !28536620     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\28536620 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Cell+Mol+Biol+Lett 2016 ; 21 (ä): 18 Nephropedia Template TP {{tp|p=28536620 |t=2016. BAG2 structure, function and involvement in disease |pdf=|usr=}}{{28536620 }} gab.com Text BAG2 structure, function and involvement in disease JO: Cell Mol Biol Lett http://www.kidney.de/pget.php?&tw=1&pmid=28536620 #FOAvip Bcl2-associated athanogene 2 (BAG2) shares a similar molecular structure and function with other BAG family members. Functioning as a co-chaperone, it interacts with the ATPase domain of the heat shock protein 70 (dHsp70) through its BAG domain. It also interacts with many other molecules and regulates various cellular functions. An increasing number of studies have indicated that BAG2 is involved in the pathogenesis of various diseases, including cancers and neurodegenerative diseases. This paper is a comprehensive review of the structure, functions, and protein interactions of BAG2. We also discuss its roles in diseases, including cancer, Alzheimer's disease, Parkinson's disease and spinocerebellar ataxia type-3. Further research on BAG2 could lead to an understanding of the pathogenesis of these disorders or even to novel therapeutic approaches. Twit Text FOAVip BAG2 structure, function and involvement in disease ????Cell Mol Biol Lett http://www.kidney.de/pget.php?&tw=1&pmid=28536620 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28536620 #FOAvip English Wikipedia <ref>{{Cite pmid|28536620 }}</ref> BAG2 structure, function and involvement in disease #MMPMID28536620 Qin L ; Guo J ; Zheng Q ; Zhang H Cell Mol Biol Lett 2016[]; 21 (ä): 18 PMID28536620 show ga Bcl2-associated athanogene 2 (BAG2) shares a similar molecular structure and function with other BAG family members. Functioning as a co-chaperone, it interacts with the ATPase domain of the heat shock protein 70 (dHsp70) through its BAG domain. It also interacts with many other molecules and regulates various cellular functions. An increasing number of studies have indicated that BAG2 is involved in the pathogenesis of various diseases, including cancers and neurodegenerative diseases. This paper is a comprehensive review of the structure, functions, and protein interactions of BAG2. We also discuss its roles in diseases, including cancer, Alzheimer's disease, Parkinson's disease and spinocerebellar ataxia type-3. Further research on BAG2 could lead to an understanding of the pathogenesis of these disorders or even to novel therapeutic approaches. |Animals [MESH] |Humans [MESH] |Molecular Chaperones/*metabolism/physiology [MESH] |Neoplasms/metabolism/pathology [MESH] |Neurodegenerative Diseases/metabolism/pathology [MESH]BAG2 structure, function and involvement in disease (epmc).pdf DeepDyve Pubget Overpricing