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.

10.1038/ncb781 http://scihub22266oqcxt.onion/10.1038/ncb781 11941371!ä!11941371 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=11941371&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\11941371.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Cell+Biol 2002 ; 4 (5): 329-36 Nephropedia Template TP {{tp|p=11941371|t=2002. The TRPM7 channel is inactivated by PIP(2) hydrolysis |pdf=|usr=}}{{11941371}} gab.com Text The TRPM7 channel is inactivated by PIP(2) hydrolysis JO: Nat Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=11941371 #FOAvip TRPM7 (ChaK1, TRP-PLIK, LTRPC7) is a ubiquitous, calcium-permeant ion channel that is unique in being both an ion channel and a serine/threonine kinase. The kinase domain of TRPM7 directly associates with the C2 domain of phospholipase C (PLC). Here, we show that in native cardiac cells and heterologous expression systems, G alpha q-linked receptors or tyrosine kinase receptors that activate PLC potently inhibit channel activity. Numerous experimental approaches demonstrated that phosphatidylinositol 4,5-bisphosphate (PIP(2)), the substrate of PLC, is a key regulator of TRPM7. We conclude that receptor-mediated activation of PLC results in the hydrolysis of localized PIP(2), leading to inactivation of the TRPM7 channel. Twit Text FOAVip The TRPM7 channel is inactivated by PIP(2) hydrolysis ????Nat Cell Biol http://www.kidney.de/pget.php?&tw=1&pmid=11941371 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=11941371 #FOAvip English Wikipedia <ref>{{Cite pmid|11941371}}</ref> The TRPM7 channel is inactivated by PIP(2) hydrolysis #MMPMID11941371 Runnels LW; Yue L; Clapham DE Nat Cell Biol 2002[May]; 4 (5): 329-36 PMID11941371show ga TRPM7 (ChaK1, TRP-PLIK, LTRPC7) is a ubiquitous, calcium-permeant ion channel that is unique in being both an ion channel and a serine/threonine kinase. The kinase domain of TRPM7 directly associates with the C2 domain of phospholipase C (PLC). Here, we show that in native cardiac cells and heterologous expression systems, G alpha q-linked receptors or tyrosine kinase receptors that activate PLC potently inhibit channel activity. Numerous experimental approaches demonstrated that phosphatidylinositol 4,5-bisphosphate (PIP(2)), the substrate of PLC, is a key regulator of TRPM7. We conclude that receptor-mediated activation of PLC results in the hydrolysis of localized PIP(2), leading to inactivation of the TRPM7 channel. |*Membrane Proteins[MESH] |Animals[MESH] |Carbachol/pharmacology[MESH] |Cell Line[MESH] |Cholinergic Agonists/pharmacology[MESH] |Diglycerides/pharmacology[MESH] |Heart/drug effects[MESH] |Humans[MESH] |Hydrolysis[MESH] |Ion Channels/*metabolism[MESH] |Models, Biological[MESH] |Myocardium/cytology[MESH] |Patch-Clamp Techniques[MESH] |Phosphatidylinositol 4,5-Diphosphate/*metabolism[MESH] |Protein Kinase C/metabolism[MESH] |Protein Kinases/*metabolism[MESH] |Protein Serine-Threonine Kinases[MESH] |Protein Structure, Tertiary[MESH] |Rats[MESH] |Receptor, Muscarinic M1[MESH] |Receptors, Muscarinic/metabolism[MESH] |Recombinant Fusion Proteins/metabolism[MESH] |TRPM Cation Channels[MESH] |Two-Hybrid System Techniques[MESH] |Type C Phospholipases/*metabolism[MESH]The TRPM7 channel is inactivated by PIP(2) hydrolysis (epmc).pdf DeepDyve Pubget Overpricing