FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2008061760> ?p ?o ?g. }

• W2008061760 endingPage "482" @default.
• W2008061760 startingPage "473" @default.
• W2008061760 abstract "Structural requirements for signal processing by human placental insulin receptors have been examined. Insulin binding has been found to change the physico-chemical properties of (alpha beta)2 receptors solubilized with Triton X-100, indicating a marked alteration of the form, i.e. size and shape, of the molecular complex. (a) The Stokes radius decreases from about 9.5 nm to 7.9 nm, as determined by PAGE with Triton X-100 in the buffer (Triton X-100/PAGE), and from 9.1 nm to 8.7 nm, as assessed by gel filtration. (b) The sedimentation coefficient s20,w rises from 10.1 S to 11.4 S. Upon dissociation of the receptor-hormone complex, the alterations are reversed. After autophosphorylation of hormone-bound (alpha beta)2-insulin receptors, phosphate incorporation was found for 7.9-nm receptor forms when receptor-insulin complexes were crosslinked with disuccinimide suberate prior to Triton X-100/PAGE. However, phosphate incorporation was demonstrated for the 9.5-nm receptor forms when receptor-insulin complexes were not prevented from dissociation. This strongly indicates that the (alpha beta)2 receptor is autophosphorylated after assuming its 7.9-nm form upon insulin binding. Moreover, the insulin-dependent structural alterations are not affected by autophosphorylation. In contrast to (alpha beta)2 receptors, the diffusion and the sedimentation behaviour of alpha beta receptors, which carry a dormant tyrosine kinase even in the hormone-laden state, has been found to be insensitive to insulin binding. Different molecular properties of alpha beta and (alpha beta)2 receptors have also been detected by hormone binding studies. Insulin binding to (alpha beta)2 and alpha beta receptors differs markedly with respect to pH, ionic strength, and temperature. This might indicate that the structure of the hormone binding domain of alpha beta receptor changes on association into the (alpha beta)2 species. Alternatively, distinct hormone-induced conformational alterations at the molecular level of alpha beta and (alpha beta)2 receptor species may lead to the different binding properties. Our data demonstrate that the (alpha beta)2-insulin receptor undergoes extended conformational alterations upon insulin binding. This capacity for structural changes coincides with the hormone-inducable enhancement of tyrosine autophosphorylation of the 7.9-nm insulin-bound receptor form. In contrast, alpha beta receptors appear to be locked in an inactive nonconvertable state. Thus, interaction between two alpha beta receptor units is required to allow extended conformational alterations, which are assumed to be the triggering event for augmented auto-phosphorylation." @default.
• W2008061760 created "2016-06-24" @default.
• W2008061760 creator A5003590118 @default.
• W2008061760 creator A5068023913 @default.
• W2008061760 creator A5077783532 @default.
• W2008061760 date "1990-07-01" @default.
• W2008061760 modified "2023-10-18" @default.
• W2008061760 title "Structural requirements for signal transduction of the insulin receptor" @default.
• W2008061760 cites W1479900350 @default.
• W2008061760 cites W1502900852 @default.
• W2008061760 cites W1507928574 @default.
• W2008061760 cites W1507982628 @default.
• W2008061760 cites W1513216428 @default.
• W2008061760 cites W1527803305 @default.
• W2008061760 cites W1533778697 @default.
• W2008061760 cites W1534556626 @default.
• W2008061760 cites W1534571178 @default.
• W2008061760 cites W1546867328 @default.
• W2008061760 cites W1563354863 @default.
• W2008061760 cites W1564258903 @default.
• W2008061760 cites W1568118221 @default.
• W2008061760 cites W1573534810 @default.
• W2008061760 cites W1577543390 @default.
• W2008061760 cites W1577657954 @default.
• W2008061760 cites W1604679503 @default.
• W2008061760 cites W1605981237 @default.
• W2008061760 cites W1651166309 @default.
• W2008061760 cites W1654759002 @default.
• W2008061760 cites W1729199928 @default.
• W2008061760 cites W1770317606 @default.
• W2008061760 cites W1865509903 @default.
• W2008061760 cites W1971703378 @default.
• W2008061760 cites W1978120642 @default.
• W2008061760 cites W1979787131 @default.
• W2008061760 cites W1980999662 @default.
• W2008061760 cites W1984159784 @default.
• W2008061760 cites W1991710558 @default.
• W2008061760 cites W1992173986 @default.
• W2008061760 cites W1996544551 @default.
• W2008061760 cites W2011249780 @default.
• W2008061760 cites W2012330599 @default.
• W2008061760 cites W2015000698 @default.
• W2008061760 cites W2018751358 @default.
• W2008061760 cites W2030156849 @default.
• W2008061760 cites W2039734922 @default.
• W2008061760 cites W2046431546 @default.
• W2008061760 cites W2057323896 @default.
• W2008061760 cites W2072929425 @default.
• W2008061760 cites W2074010959 @default.
• W2008061760 cites W2075096741 @default.
• W2008061760 cites W2078607174 @default.
• W2008061760 cites W2086269149 @default.
• W2008061760 cites W2095381863 @default.
• W2008061760 cites W2100837269 @default.
• W2008061760 cites W2119460480 @default.
• W2008061760 cites W2122567567 @default.
• W2008061760 cites W2235973623 @default.
• W2008061760 cites W2409195510 @default.
• W2008061760 cites W628204631 @default.
• W2008061760 cites W745670538 @default.
• W2008061760 doi "https://doi.org/10.1111/j.1432-1033.1990.tb19146.x" @default.
• W2008061760 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2200676" @default.
• W2008061760 hasPublicationYear "1990" @default.
• W2008061760 type Work @default.
• W2008061760 sameAs 2008061760 @default.
• W2008061760 citedByCount "22" @default.
• W2008061760 countsByYear W20080617602013 @default.
• W2008061760 countsByYear W20080617602014 @default.
• W2008061760 countsByYear W20080617602015 @default.
• W2008061760 crossrefType "journal-article" @default.
• W2008061760 hasAuthorship W2008061760A5003590118 @default.
• W2008061760 hasAuthorship W2008061760A5068023913 @default.
• W2008061760 hasAuthorship W2008061760A5077783532 @default.
• W2008061760 hasBestOaLocation W20080617601 @default.
• W2008061760 hasConcept C112446052 @default.
• W2008061760 hasConcept C11960822 @default.
• W2008061760 hasConcept C12554922 @default.
• W2008061760 hasConcept C134018914 @default.
• W2008061760 hasConcept C136543978 @default.
• W2008061760 hasConcept C150109051 @default.
• W2008061760 hasConcept C170493617 @default.
• W2008061760 hasConcept C181199279 @default.
• W2008061760 hasConcept C185592680 @default.
• W2008061760 hasConcept C185967709 @default.
• W2008061760 hasConcept C193363816 @default.
• W2008061760 hasConcept C2777391703 @default.
• W2008061760 hasConcept C2779306644 @default.
• W2008061760 hasConcept C55493867 @default.
• W2008061760 hasConcept C71240020 @default.
• W2008061760 hasConcept C86803240 @default.
• W2008061760 hasConcept C97029542 @default.
• W2008061760 hasConceptScore W2008061760C112446052 @default.
• W2008061760 hasConceptScore W2008061760C11960822 @default.
• W2008061760 hasConceptScore W2008061760C12554922 @default.
• W2008061760 hasConceptScore W2008061760C134018914 @default.
• W2008061760 hasConceptScore W2008061760C136543978 @default.
• W2008061760 hasConceptScore W2008061760C150109051 @default.
• W2008061760 hasConceptScore W2008061760C170493617 @default.

• next