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.

10.1155/2017/6739236 http://scihub22266oqcxt.onion/10.1155/2017/6739236 C5480048!5480048 !28685009     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=28685009 &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\28685009 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Oxid+Med+Cell+Longev 2017 ; 2017 (ä): 6739236 Nephropedia Template TP {{tp|p=28685009 |t=2017. MNRR1, a Biorganellar Regulator of Mitochondria |pdf=|usr=}}{{28685009 }} gab.com Text MNRR1, a Biorganellar Regulator of Mitochondria JO: Oxid Med Cell Longev http://www.kidney.de/pget.php?&tw=1&pmid=28685009 #FOAvip The central role of energy metabolism in cellular activities is becoming widely recognized. However, there are many gaps in our knowledge of the mechanisms by which mitochondria evaluate their status and call upon the nucleus to make adjustments. Recently, a protein family consisting of twin CX(9)C proteins has been shown to play a role in human pathophysiology. We focus here on two family members, the isoforms CHCHD2 (renamed MNRR1) and CHCHD10. The better studied isoform, MNRR1, has the unusual property of functioning in both the mitochondria and the nucleus and of having a different function in each. In the mitochondria, it functions by binding to cytochrome c oxidase (COX), which stimulates respiration. Its binding to COX is promoted by tyrosine-99 phosphorylation, carried out by ABL2 kinase (ARG). In the nucleus, MNRR1 binds to a novel promoter element in COX4I2 and itself, increasing transcription at 4% oxygen. We discuss mutations in both MNRR1 and CHCHD10 found in a number of chronic, mostly neurodegenerative, diseases. Finally, we propose a model of a graded response to hypoxic and oxidative stresses, mediated under different oxygen tensions by CHCHD10, MNRR1, and HIF1, which operate at intermediate and very low oxygen concentrations, respectively. Twit Text FOAVip MNRR1, a Biorganellar Regulator of Mitochondria ????Oxid Med Cell Longev http://www.kidney.de/pget.php?&tw=1&pmid=28685009 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28685009 #FOAvip English Wikipedia <ref>{{Cite pmid|28685009 }}</ref> MNRR1, a Biorganellar Regulator of Mitochondria #MMPMID28685009 Grossman LI ; Purandare N ; Arshad R ; Gladyck S ; Somayajulu M ; Hüttemann M ; Aras S Oxid Med Cell Longev 2017[]; 2017 (ä): 6739236 PMID28685009 show ga The central role of energy metabolism in cellular activities is becoming widely recognized. However, there are many gaps in our knowledge of the mechanisms by which mitochondria evaluate their status and call upon the nucleus to make adjustments. Recently, a protein family consisting of twin CX(9)C proteins has been shown to play a role in human pathophysiology. We focus here on two family members, the isoforms CHCHD2 (renamed MNRR1) and CHCHD10. The better studied isoform, MNRR1, has the unusual property of functioning in both the mitochondria and the nucleus and of having a different function in each. In the mitochondria, it functions by binding to cytochrome c oxidase (COX), which stimulates respiration. Its binding to COX is promoted by tyrosine-99 phosphorylation, carried out by ABL2 kinase (ARG). In the nucleus, MNRR1 binds to a novel promoter element in COX4I2 and itself, increasing transcription at 4% oxygen. We discuss mutations in both MNRR1 and CHCHD10 found in a number of chronic, mostly neurodegenerative, diseases. Finally, we propose a model of a graded response to hypoxic and oxidative stresses, mediated under different oxygen tensions by CHCHD10, MNRR1, and HIF1, which operate at intermediate and very low oxygen concentrations, respectively. |Animals [MESH] |DNA-Binding Proteins [MESH] |Electron Transport Complex IV/metabolism [MESH] |Humans [MESH] |Mitochondria/*metabolism [MESH] |Mitochondrial Proteins/genetics/*metabolism [MESH] |Protein Binding [MESH]MNRR1, a Biorganellar Regulator of Mitochondria (epmc).pdf DeepDyve Pubget Overpricing