| pubmed-article:17135270 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C1149880 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:17135270 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:17135270 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:17135270 | pubmed:dateCreated | 2007-1-29 | lld:pubmed |
| pubmed-article:17135270 | pubmed:abstractText | Protein tyrosine phosphatase 1B (PTP-1B) has been implicated in the regulation of the insulin receptor. Dephosphorylation of the insulin receptor results in decreased insulin signaling and thus decreased glucose uptake. PTP-1B-/- mice have increased insulin sensitivity and are resistant to weight gain when fed a high fat diet, validating PTP-1B as a potential target for the treatment of type 2 diabetes. Many groups throughout the world have been searching for selective inhibitors for PTP-1B, and most of them target inhibitors to PTP-1B-(1-298), the N-terminal catalytic domain of the enzyme. However, the C-terminal domain is quite large and could influence the activity of the enzyme. Using two constructs of PTP-1B and a phosphopeptide as substrate, steady state assays showed that the presence of the C-terminal domain decreased both the Km and the k(cat) 2-fold. Pre-steady state kinetic experiments showed that the presence of the C-terminal domain improved the affinity of the enzyme for a phosphopeptide 2-fold, primarily because the off-rate was slower. This suggests that the C-terminal domain of PTP-1B may contact the phosphopeptide in some manner, allowing it to remain at the active site longer. This could be useful when screening libraries of compounds for inhibitors of PTP-1B. A compound that is able to make contacts with the C-terminal domain of PTP-1B would not only have a modest improvement in affinity but may also provide for specificity over other phosphatases. | lld:pubmed |
| pubmed-article:17135270 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17135270 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17135270 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17135270 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17135270 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17135270 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17135270 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17135270 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17135270 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17135270 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17135270 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17135270 | pubmed:author | pubmed-author:PatelSmita... | lld:pubmed |
| pubmed-article:17135270 | pubmed:author | pubmed-author:KoehnJamesJ | lld:pubmed |
| pubmed-article:17135270 | pubmed:author | pubmed-author:WennogleLawre... | lld:pubmed |
| pubmed-article:17135270 | pubmed:author | pubmed-author:PichaKristen... | lld:pubmed |
| pubmed-article:17135270 | pubmed:author | pubmed-author:MandiyanSreek... | lld:pubmed |
| pubmed-article:17135270 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17135270 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:17135270 | pubmed:volume | 282 | lld:pubmed |
| pubmed-article:17135270 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17135270 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17135270 | pubmed:pagination | 2911-7 | lld:pubmed |
| pubmed-article:17135270 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:meshHeading | pubmed-meshheading:17135270... | lld:pubmed |
| pubmed-article:17135270 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17135270 | pubmed:articleTitle | The role of the C-terminal domain of protein tyrosine phosphatase-1B in phosphatase activity and substrate binding. | lld:pubmed |
| pubmed-article:17135270 | pubmed:affiliation | Metabolic and Cardiovascular Diseases Research, Novartis Institutes for Biomedical Research, Cambridge, Massachusetts 02139, USA. | lld:pubmed |
| pubmed-article:17135270 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:5770 | entrezgene:pubmed | pubmed-article:17135270 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:17135270 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17135270 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17135270 | lld:pubmed |
