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10.1111/j.1582-4934.2007.00114.x http://scihub22266oqcxt.onion/10.1111/j.1582-4934.2007.00114.x C4401264!4401264 !17979874     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=17979874 &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 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 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\17979874 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       J+Cell+Mol+Med 2007 ; 11 (5 ): 923-34 Nephropedia Template TP {{tp|p=17979874 |t=2007. The calcium-sensing receptor and its interacting proteins |pdf=|usr=}}{{17979874 }} gab.com Text The calcium-sensing receptor and its interacting proteins JO: J Cell Mol Med http://www.kidney.de/pget.php?&tw=1&pmid=17979874 #FOAvip Seven membrane-spanning, or G protein-coupled receptors were originally thought to act through het-erotrimeric G proteins that in turn activate intracellular enzymes or ion channels, creating relatively simple, linear signalling pathways. Although this basic model remains true in that this family does act via a relatively small number of G proteins, these signalling systems are considerably more complex because the receptors interact with or are located near additional proteins that are often unique to a receptor or subset of receptors. These additional proteins give receptors their unique signalling personalities. The extracellular Ca-sensing receptor (CaR) signals via Galpha(i), Galpha(q) and Galpha(12/13), but its effects in vivo demonstrate that the signalling pathways controlled by these subunits are not sufficient to explain all its biologic effects. Additional structural or signalling proteins that interact with the CaR may explain its behaviour more fully. Although the CaR is less well studied in this respect than other receptors, several CaR-interacting proteins such as filamin, a potential scaffolding protein, receptor activity modifying proteins (RAMPs) and potassium channels may contribute to the unique characteristics of the CaR. The CaR also appears to interact with additional proteins common to other G protein-coupled receptors such as arrestins, G protein receptor kinases, protein kinase C, caveolin and proteins in the ubiquitination pathway. These proteins probably represent a few initial members of CaR-based signalling complex. These and other proteins may not all be associated with the CaR in all tissues, but they form the basis for understanding the complete nature of CaR signalling. Twit Text FOAVip The calcium-sensing receptor and its interacting proteins ????J Cell Mol Med http://www.kidney.de/pget.php?&tw=1&pmid=17979874 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=17979874 #FOAvip English Wikipedia <ref>{{Cite pmid|17979874 }}</ref> The calcium-sensing receptor and its interacting proteins #MMPMID17979874 Huang C ; Miller RT J Cell Mol Med 2007[Sep]; 11 (5 ): 923-34 PMID17979874 show ga Seven membrane-spanning, or G protein-coupled receptors were originally thought to act through het-erotrimeric G proteins that in turn activate intracellular enzymes or ion channels, creating relatively simple, linear signalling pathways. Although this basic model remains true in that this family does act via a relatively small number of G proteins, these signalling systems are considerably more complex because the receptors interact with or are located near additional proteins that are often unique to a receptor or subset of receptors. These additional proteins give receptors their unique signalling personalities. The extracellular Ca-sensing receptor (CaR) signals via Galpha(i), Galpha(q) and Galpha(12/13), but its effects in vivo demonstrate that the signalling pathways controlled by these subunits are not sufficient to explain all its biologic effects. Additional structural or signalling proteins that interact with the CaR may explain its behaviour more fully. Although the CaR is less well studied in this respect than other receptors, several CaR-interacting proteins such as filamin, a potential scaffolding protein, receptor activity modifying proteins (RAMPs) and potassium channels may contribute to the unique characteristics of the CaR. The CaR also appears to interact with additional proteins common to other G protein-coupled receptors such as arrestins, G protein receptor kinases, protein kinase C, caveolin and proteins in the ubiquitination pathway. These proteins probably represent a few initial members of CaR-based signalling complex. These and other proteins may not all be associated with the CaR in all tissues, but they form the basis for understanding the complete nature of CaR signalling. |Animals [MESH] |Contractile Proteins/metabolism [MESH] |Filamins [MESH] |Humans [MESH] |Intracellular Signaling Peptides and Proteins/metabolism [MESH] |Membrane Proteins/metabolism [MESH] |Microfilament Proteins/metabolism [MESH] |Potassium Channels/metabolism [MESH] |Protein Binding [MESH] |Receptor Activity-Modifying Proteins [MESH] |Receptors, Calcium-Sensing/*metabolism [MESH]The calcium-sensing receptor and its interacting proteins (epmc).pdf DeepDyve Pubget Overpricing