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10.2174/092986609789055368 http://scihub22266oqcxt.onion/10.2174/092986609789055368 19508229!ä!19508229 Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=19508229&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 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 217.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Protein+Pept+Lett 2009 ; 16 (9): 1081-7 Nephropedia Template TP {{tp|p=19508229|t=2009. Functional roles of EF-hands in human potassium channel-interacting protein 2 2 |pdf=|usr=}}{{19508229}} gab.com Text Functional roles of EF-hands in human potassium channel-interacting protein 2 2 JO: Protein Pept Lett http://www.kidney.de/pget.php?&tw=1&pmid=19508229 #FOAvip Single site-directed mutations at each of the four EF-hand loops of potassium channel-interacting protein 2.2 (KChIP2.2) were carried out to explore the functional roles of EF-hands in KChIP2.2. In contrast to those on EF-hands 1 and 2, mutations on EF-hands 3 or 4 distorted the high affinity Ca(2+)-binding site of KChIP2.2. However, the Mg(2+)-binding ability of KChIP2.2 was marginally affected by the mutations. The gross conformation of mutated KChIP2.2 was indistinguishable from wild-type KChIP2.2 as revealed by CD spectra. The results of size exclusion chromatography showed that, with exception of EF-hand 4 mutant, mutations on EF-hands 1, 2 or 3 caused KChIP2.2 to form oligomer. Pull-down assay revealed that, unlike wild-type KChIP2.2, the interaction between mutated KChIP2.2 and Kv4.2 was not notably enhanced by Ca(2+) and Mg(2+). Coexpression of Kv4.2 and KChIP2.2 in HeLa cells revealed that mutations on EF-hands did not alter the intracellular co-localization of KChIP2.2 and Kv4.2. Together with previous findings that EF-hand mutants of KChIP proteins are unable to regulate the kinetics of Kv4.2, our data show that the intact EF-hands should be crucial for the formation of active conformation of KChIP2.2 when the protein is loaded with Ca(2+) and Mg(2+). Twit Text FOAVip Functional roles of EF-hands in human potassium channel-interacting protein 2 2 ????Protein Pept Lett http://www.kidney.de/pget.php?&tw=1&pmid=19508229 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=19508229 #FOAvip English Wikipedia <ref>{{Cite pmid|19508229}}</ref> Functional roles of EF-hands in human potassium channel-interacting protein 2 2 #MMPMID19508229 Lee L; Chen KC; Chang LS Protein Pept Lett 2009[]; 16 (9): 1081-7 PMID19508229show ga Single site-directed mutations at each of the four EF-hand loops of potassium channel-interacting protein 2.2 (KChIP2.2) were carried out to explore the functional roles of EF-hands in KChIP2.2. In contrast to those on EF-hands 1 and 2, mutations on EF-hands 3 or 4 distorted the high affinity Ca(2+)-binding site of KChIP2.2. However, the Mg(2+)-binding ability of KChIP2.2 was marginally affected by the mutations. The gross conformation of mutated KChIP2.2 was indistinguishable from wild-type KChIP2.2 as revealed by CD spectra. The results of size exclusion chromatography showed that, with exception of EF-hand 4 mutant, mutations on EF-hands 1, 2 or 3 caused KChIP2.2 to form oligomer. Pull-down assay revealed that, unlike wild-type KChIP2.2, the interaction between mutated KChIP2.2 and Kv4.2 was not notably enhanced by Ca(2+) and Mg(2+). Coexpression of Kv4.2 and KChIP2.2 in HeLa cells revealed that mutations on EF-hands did not alter the intracellular co-localization of KChIP2.2 and Kv4.2. Together with previous findings that EF-hand mutants of KChIP proteins are unable to regulate the kinetics of Kv4.2, our data show that the intact EF-hands should be crucial for the formation of active conformation of KChIP2.2 when the protein is loaded with Ca(2+) and Mg(2+). |Calcium/metabolism[MESH] |Circular Dichroism[MESH] |EF Hand Motifs/*genetics[MESH] |HeLa Cells[MESH] |Humans[MESH] |Kv Channel-Interacting Proteins/genetics/*physiology[MESH] |Magnesium/metabolism[MESH] |Shal Potassium Channels/genetics[MESH]Functional roles of EF-hands in human potassium channel-interacting pr(epmc).pdf DeepDyve Pubget Overpricing