Matches in SemOpenAlex for { <https://semopenalex.org/work/W4242749203> ?p ?o ?g. }
Showing items 1 to 62 of
62
with 100 items per page.
- W4242749203 endingPage "444" @default.
- W4242749203 startingPage "441" @default.
- W4242749203 abstract "Cys10 is located in subdomain 1 of actin, which has an important role in the interaction of actin with myosin- and actin-binding proteins. Cys10 was modified with fluorescence probes N-(iodoacetyl)N′-(5-sulfo-1-naphthyl)ethylene diamine (IAEDANS), 7-diethylamino-3-(4′-maleimidylphenyl)-4-methylcoumarin (CPM), or monobromo bimane (MBB) by the method of Drewes and Faulstich (1991, J. Biol. Chem. 266:5508–5513). The specificity of Cys10 modification was verified by showing that the 33-kDa subtilisin fragment of actin (residues 48–375), which contains all of the actin thiols but Cys10, is not fluorescent. Cys10 modification exposed a new site on actin to subtilisin cleavage. Edman degradation revealed this site to be between Ala19 and Gly20. The modification slightly increased the rate of ϵATP-ATP exchange and decreased the rates of G-actin ATPase and polymerization. The activation of S1 ATPase by Cys10-modified F-actin showed small probe-dependent changes in the values of Vmax and KM. The sliding speed of actin filaments in the in vitro motility assay remained unchanged upon modification of Cys10. These results indicate that although the labeling of Cys10 perturbs the structure of subdomain 1, the modified actin remains fully functional. The binding of S1 to actin filaments decreases the accessibility of Cys10 probes to acrylamide and nitromethane quenchers. Because Cys10 does not participate directly in either actin polymerization or S1 binding, our results indicate that actin-actin and actin-myosin interactions induce dynamic, allosteric changes in actin structure." @default.
- W4242749203 created "2022-05-12" @default.
- W4242749203 date "1990-03-01" @default.
- W4242749203 modified "2023-09-26" @default.
- W4242749203 title "Author index" @default.
- W4242749203 doi "https://doi.org/10.1016/0167-4838(90)90049-l" @default.
- W4242749203 hasPublicationYear "1990" @default.
- W4242749203 type Work @default.
- W4242749203 citedByCount "0" @default.
- W4242749203 crossrefType "journal-article" @default.
- W4242749203 hasConcept C12554922 @default.
- W4242749203 hasConcept C125705527 @default.
- W4242749203 hasConcept C130861313 @default.
- W4242749203 hasConcept C142669718 @default.
- W4242749203 hasConcept C1491633281 @default.
- W4242749203 hasConcept C166342909 @default.
- W4242749203 hasConcept C181199279 @default.
- W4242749203 hasConcept C185592680 @default.
- W4242749203 hasConcept C189040839 @default.
- W4242749203 hasConcept C2779811187 @default.
- W4242749203 hasConcept C2993400109 @default.
- W4242749203 hasConcept C3620293 @default.
- W4242749203 hasConcept C55493867 @default.
- W4242749203 hasConcept C59999672 @default.
- W4242749203 hasConcept C6997183 @default.
- W4242749203 hasConcept C86803240 @default.
- W4242749203 hasConceptScore W4242749203C12554922 @default.
- W4242749203 hasConceptScore W4242749203C125705527 @default.
- W4242749203 hasConceptScore W4242749203C130861313 @default.
- W4242749203 hasConceptScore W4242749203C142669718 @default.
- W4242749203 hasConceptScore W4242749203C1491633281 @default.
- W4242749203 hasConceptScore W4242749203C166342909 @default.
- W4242749203 hasConceptScore W4242749203C181199279 @default.
- W4242749203 hasConceptScore W4242749203C185592680 @default.
- W4242749203 hasConceptScore W4242749203C189040839 @default.
- W4242749203 hasConceptScore W4242749203C2779811187 @default.
- W4242749203 hasConceptScore W4242749203C2993400109 @default.
- W4242749203 hasConceptScore W4242749203C3620293 @default.
- W4242749203 hasConceptScore W4242749203C55493867 @default.
- W4242749203 hasConceptScore W4242749203C59999672 @default.
- W4242749203 hasConceptScore W4242749203C6997183 @default.
- W4242749203 hasConceptScore W4242749203C86803240 @default.
- W4242749203 hasIssue "3" @default.
- W4242749203 hasLocation W42427492031 @default.
- W4242749203 hasOpenAccess W4242749203 @default.
- W4242749203 hasPrimaryLocation W42427492031 @default.
- W4242749203 hasRelatedWork W2020577203 @default.
- W4242749203 hasRelatedWork W2030370318 @default.
- W4242749203 hasRelatedWork W2081602955 @default.
- W4242749203 hasRelatedWork W2147062922 @default.
- W4242749203 hasRelatedWork W2401809724 @default.
- W4242749203 hasRelatedWork W2886383051 @default.
- W4242749203 hasRelatedWork W3105510862 @default.
- W4242749203 hasRelatedWork W3216060643 @default.
- W4242749203 hasRelatedWork W631415394 @default.
- W4242749203 hasRelatedWork W7655210 @default.
- W4242749203 hasVolume "1037" @default.
- W4242749203 isParatext "false" @default.
- W4242749203 isRetracted "false" @default.
- W4242749203 workType "article" @default.