pubmed-article:17510962 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:17510962 | lifeskim:mentions | umls-concept:C0205474 | lld:lifeskim |
pubmed-article:17510962 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
pubmed-article:17510962 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
pubmed-article:17510962 | pubmed:issue | 3 | lld:pubmed |
pubmed-article:17510962 | pubmed:dateCreated | 2007-7-26 | lld:pubmed |
pubmed-article:17510962 | pubmed:abstractText | Inhibitor-1alpha is one of the isoforms of human protein phosphatase inhibitor-1. It is a product of alternative splicing of inhibitor-1 gene and lacks 51 internal amino acids from residue 84 to 134 of inhibitor-1. Here we have characterized the structural and biochemical properties of inhibitor-1alpha. Structural analysis of recombinant inhibitor-1alpha by NMR spectroscopy revealed that inhibitor-1alpha adopts a predominantly random coil conformation. Excluding the region from residue 84 to 134 of inhibitor-1, the structural features of inhibitor-1 and inhibitor-1alpha are almost the same as each other. The IC(50) value of inhibitor-1alpha in inhibition of Protein phosphatase-1 (PP1) is comparable to that of inhibitor-1, indicating that inhibitor-1alpha is a potent inhibitor of PP1 when Thr-35 is phosphorylated by PKA. For phosphorylation by PKA and dephosphorylation by protein phosphatase-1, -2A, and -2B, the measured kinetic parameters of inhibitor-1alpha are very close to those of inhibitor-1. Taken together, these results suggest that inhibitor-1alpha preserves the structure of inhibitor-1, the PP1 inhibitory activity and the functional specificities toward phosphorylation by PKA and dephosphorylation by protein phosphatase-1, -2A, and -2B. | lld:pubmed |
pubmed-article:17510962 | pubmed:language | eng | lld:pubmed |
pubmed-article:17510962 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17510962 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:17510962 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17510962 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17510962 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17510962 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17510962 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17510962 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17510962 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:17510962 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:17510962 | pubmed:month | Aug | lld:pubmed |
pubmed-article:17510962 | pubmed:issn | 1097-0134 | lld:pubmed |
pubmed-article:17510962 | pubmed:author | pubmed-author:HuangHsien-Bi... | lld:pubmed |
pubmed-article:17510962 | pubmed:author | pubmed-author:TsayHuey-JenH... | lld:pubmed |
pubmed-article:17510962 | pubmed:author | pubmed-author:LinTa-HsienTH | lld:pubmed |
pubmed-article:17510962 | pubmed:author | pubmed-author:ChenYi-ChenYC | lld:pubmed |
pubmed-article:17510962 | pubmed:author | pubmed-author:LeeTing-TingT... | lld:pubmed |
pubmed-article:17510962 | pubmed:author | pubmed-author:HuangYi-Choan... | lld:pubmed |
pubmed-article:17510962 | pubmed:author | pubmed-author:LiuHsin-TzuHT | lld:pubmed |
pubmed-article:17510962 | pubmed:author | pubmed-author:LiuChen-Kuang... | lld:pubmed |
pubmed-article:17510962 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:17510962 | pubmed:day | 15 | lld:pubmed |
pubmed-article:17510962 | pubmed:volume | 68 | lld:pubmed |
pubmed-article:17510962 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:17510962 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:17510962 | pubmed:pagination | 779-88 | lld:pubmed |
pubmed-article:17510962 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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pubmed-article:17510962 | pubmed:year | 2007 | lld:pubmed |
pubmed-article:17510962 | pubmed:articleTitle | Structural and biochemical characterization of inhibitor-1alpha. | lld:pubmed |
pubmed-article:17510962 | pubmed:affiliation | Institute of Molecular Biology, National Chung Cheng University, Chia-Yi 621, Taiwan, Republic of China. | lld:pubmed |
pubmed-article:17510962 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:17510962 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |