Matches in SemOpenAlex for { <https://semopenalex.org/work/W2054165364> ?p ?o ?g. }
Showing items 1 to 95 of
95
with 100 items per page.
- W2054165364 endingPage "664" @default.
- W2054165364 startingPage "657" @default.
- W2054165364 abstract "This investigation ascertains whether, in (smooth muscle) myosin, certain residues engage in functional interactions with their actin conjugates in an actomyosin complex. Such interactions have been postulated from putting together crystallographic models of the two proteins [Rayment, I., Rypniewski, W. R., Schmidt-Bäse, K., Smith, R., Tomchick, D. R., Benning, M. M., Winkelmann, D. A., Wesenberg, G., and Holden, H. M. (1993) Science 261, 50-58]. Here, in several instances, we ask whether mutation of a particular residue significantly impairs a function, and find that the answers are largely rationalized by the original postulation. Additionally, a novel element emerges from our investigation. To assess function, we test the wild type and mutant systems as they perform in the steady state of ATP degradation. In doing so, we assume, as usual, that degradation proceeds from an early stage in which the complex forms (and is described by parameter K(app)) to a later stage during which the product leaves the complex (and is described by parameter V(max)). Interestingly, certain defects induced by the mutations are associated with changes in K(app), and other defects are associated with changes in V(max), suggesting that our procedure at least roughly distinguishes between events according to the time in the degradation at which they occur. In this framework, we suggest that (1) in the actin-myosin association phase, cationic residues Lys-576 and Lys-578 interact with anionic residues of the so-called second actin, and (2) in the product leaving phase, hydrophobic residues Trp-546, Phe-547, and Pro-548, as well as the Thr-532/Asn-533/Pro-534/Pro-535 sequence, sever connections with the so-called first actin. The role of Glu-473 is also examined." @default.
- W2054165364 created "2016-06-24" @default.
- W2054165364 creator A5015054549 @default.
- W2054165364 creator A5025946910 @default.
- W2054165364 creator A5040964959 @default.
- W2054165364 creator A5060048812 @default.
- W2054165364 creator A5061765991 @default.
- W2054165364 creator A5082853086 @default.
- W2054165364 creator A5089073990 @default.
- W2054165364 date "2000-12-22" @default.
- W2054165364 modified "2023-10-03" @default.
- W2054165364 title "Functional Roles of Ionic and Hydrophobic Surface Loops in Smooth Muscle Myosin: Their Interactions with Actin" @default.
- W2054165364 cites W1538692246 @default.
- W2054165364 cites W1569283491 @default.
- W2054165364 cites W1661233179 @default.
- W2054165364 cites W1965299116 @default.
- W2054165364 cites W1969074918 @default.
- W2054165364 cites W2022703044 @default.
- W2054165364 cites W2026064166 @default.
- W2054165364 cites W2044629144 @default.
- W2054165364 cites W2140040046 @default.
- W2054165364 cites W2440125231 @default.
- W2054165364 doi "https://doi.org/10.1021/bi0011328" @default.
- W2054165364 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11170382" @default.
- W2054165364 hasPublicationYear "2000" @default.
- W2054165364 type Work @default.
- W2054165364 sameAs 2054165364 @default.
- W2054165364 citedByCount "16" @default.
- W2054165364 countsByYear W20541653642012 @default.
- W2054165364 countsByYear W20541653642013 @default.
- W2054165364 countsByYear W20541653642014 @default.
- W2054165364 countsByYear W20541653642015 @default.
- W2054165364 countsByYear W20541653642016 @default.
- W2054165364 countsByYear W20541653642017 @default.
- W2054165364 countsByYear W20541653642022 @default.
- W2054165364 crossrefType "journal-article" @default.
- W2054165364 hasAuthorship W2054165364A5015054549 @default.
- W2054165364 hasAuthorship W2054165364A5025946910 @default.
- W2054165364 hasAuthorship W2054165364A5040964959 @default.
- W2054165364 hasAuthorship W2054165364A5060048812 @default.
- W2054165364 hasAuthorship W2054165364A5061765991 @default.
- W2054165364 hasAuthorship W2054165364A5082853086 @default.
- W2054165364 hasAuthorship W2054165364A5089073990 @default.
- W2054165364 hasConcept C104317684 @default.
- W2054165364 hasConcept C12554922 @default.
- W2054165364 hasConcept C125705527 @default.
- W2054165364 hasConcept C14036430 @default.
- W2054165364 hasConcept C143065580 @default.
- W2054165364 hasConcept C178790620 @default.
- W2054165364 hasConcept C183882617 @default.
- W2054165364 hasConcept C185592680 @default.
- W2054165364 hasConcept C2781338088 @default.
- W2054165364 hasConcept C55493867 @default.
- W2054165364 hasConcept C6997183 @default.
- W2054165364 hasConcept C71240020 @default.
- W2054165364 hasConcept C8010536 @default.
- W2054165364 hasConcept C86803240 @default.
- W2054165364 hasConcept C95444343 @default.
- W2054165364 hasConceptScore W2054165364C104317684 @default.
- W2054165364 hasConceptScore W2054165364C12554922 @default.
- W2054165364 hasConceptScore W2054165364C125705527 @default.
- W2054165364 hasConceptScore W2054165364C14036430 @default.
- W2054165364 hasConceptScore W2054165364C143065580 @default.
- W2054165364 hasConceptScore W2054165364C178790620 @default.
- W2054165364 hasConceptScore W2054165364C183882617 @default.
- W2054165364 hasConceptScore W2054165364C185592680 @default.
- W2054165364 hasConceptScore W2054165364C2781338088 @default.
- W2054165364 hasConceptScore W2054165364C55493867 @default.
- W2054165364 hasConceptScore W2054165364C6997183 @default.
- W2054165364 hasConceptScore W2054165364C71240020 @default.
- W2054165364 hasConceptScore W2054165364C8010536 @default.
- W2054165364 hasConceptScore W2054165364C86803240 @default.
- W2054165364 hasConceptScore W2054165364C95444343 @default.
- W2054165364 hasIssue "3" @default.
- W2054165364 hasLocation W20541653641 @default.
- W2054165364 hasLocation W20541653642 @default.
- W2054165364 hasOpenAccess W2054165364 @default.
- W2054165364 hasPrimaryLocation W20541653641 @default.
- W2054165364 hasRelatedWork W110208742 @default.
- W2054165364 hasRelatedWork W2028529336 @default.
- W2054165364 hasRelatedWork W2052841776 @default.
- W2054165364 hasRelatedWork W2108709757 @default.
- W2054165364 hasRelatedWork W2113186347 @default.
- W2054165364 hasRelatedWork W2584251531 @default.
- W2054165364 hasRelatedWork W2613165074 @default.
- W2054165364 hasRelatedWork W4213456994 @default.
- W2054165364 hasRelatedWork W4308247217 @default.
- W2054165364 hasRelatedWork W4315754344 @default.
- W2054165364 hasVolume "40" @default.
- W2054165364 isParatext "false" @default.
- W2054165364 isRetracted "false" @default.
- W2054165364 magId "2054165364" @default.
- W2054165364 workType "article" @default.