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10.1111/j.1471-4159.2007.04751.x http://scihub22266oqcxt.onion/10.1111/j.1471-4159.2007.04751.x 17608643!ä!17608643 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Neurochem 2007 ; 103 (1): 312-21 Nephropedia Template TP {{tp|p=17608643|t=2007. Ancient conserved domain protein-1 binds copper and modifies its retention in cells |pdf=|usr=}}{{17608643}} gab.com Text Ancient conserved domain protein-1 binds copper and modifies its retention in cells JO: J Neurochem http://www.kidney.de/pget.php?&tw=1&pmid=17608643 #FOAvip The ancient conserved domain protein (ACDP) family are a recently identified group of homologous mammalian proteins. Some family members have been suggested to have roles in the metabolism of metals. We investigated the capacity of ACDP-1 to bind metals. Using immobilised metal affinity chromatography and isothermal titration calorimetry we determined that ACDP-1 is a high affinity copper binding protein able to bind copper at nanomolar concentrations. In addition the promoter of ACDP-1 contains metal response elements and the cellular expression of ACDP-1 alters cellular retention of copper. However, cellular expression of ACDP-1 does not alter cellular resistance to the toxicity of copper or other metals. As our findings place the subcellular localisation of ACDP-1 in the cytoplasm it is possible that ACDP-1 represent a novel copper chaperone or storage protein. Twit Text FOAVip Ancient conserved domain protein-1 binds copper and modifies its retention in cells ????J Neurochem http://www.kidney.de/pget.php?&tw=1&pmid=17608643 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=17608643 #FOAvip English Wikipedia <ref>{{Cite pmid|17608643}}</ref> Ancient conserved domain protein-1 binds copper and modifies its retention in cells #MMPMID17608643 Alderton A; Davies P; Illman K; Brown DR J Neurochem 2007[Oct]; 103 (1): 312-21 PMID17608643show ga The ancient conserved domain protein (ACDP) family are a recently identified group of homologous mammalian proteins. Some family members have been suggested to have roles in the metabolism of metals. We investigated the capacity of ACDP-1 to bind metals. Using immobilised metal affinity chromatography and isothermal titration calorimetry we determined that ACDP-1 is a high affinity copper binding protein able to bind copper at nanomolar concentrations. In addition the promoter of ACDP-1 contains metal response elements and the cellular expression of ACDP-1 alters cellular retention of copper. However, cellular expression of ACDP-1 does not alter cellular resistance to the toxicity of copper or other metals. As our findings place the subcellular localisation of ACDP-1 in the cytoplasm it is possible that ACDP-1 represent a novel copper chaperone or storage protein. |Amino Acid Sequence[MESH] |Animals[MESH] |COS Cells[MESH] |Carrier Proteins/genetics/*metabolism[MESH] |Cation Transport Proteins[MESH] |Cell Line[MESH] |Chlorocebus aethiops[MESH] |Cloning, Molecular[MESH] |Copper/*metabolism/toxicity[MESH] |Cyclins/genetics/*metabolism[MESH] |Cytoplasm/metabolism[MESH] |Metals, Heavy/toxicity[MESH] |Mice[MESH] |Molecular Sequence Data[MESH]Ancient conserved domain protein-1 binds copper and modifies its reten(epmc).pdf DeepDyve Pubget Overpricing