FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1975592859> ?p ?o ?g. }

• W1975592859 endingPage "1914" @default.
• W1975592859 startingPage "1904" @default.
• W1975592859 abstract "A calcium-activated potassium channel in posterior pituitary nerve terminals was modulated by phosphorylation and dephosphorylation. Nearly every patch of membrane containing this channel also contained both membrane bound protein phosphatase and membrane-bound protein kinase. By examining the statistical and kinetic nature of phosphorylation and dephosphorylation in excised patches, it was possible to evaluate two contrasting models for these enzymatic reactions. One of these models treated catalysis as an intermolecular process in which the enzyme and substrate are separate molecular species that diffuse and encounter one another during collisions. The second model treated catalysis as an intramolecular process in which the enzyme and substrate reside within a stable macromolecular complex. The study began with a Poisson analysis of the distribution of channel number in patches, and of the number of protein phosphatase-free and protein kinase-free patches. Subsequent kinetic analysis of dephosphorylation yielded an estimate of the mean number of protein phosphatase molecules per patch that was similar to the value obtained from Poisson analysis. Because these two estimates were independent predictions based on the intermolecular model, their agreement supported this model. Analysis of channel number in protein phosphatase-free patches and of the rarity of patches showing partial but incomplete rundown provided additional support for the intermolecular model over the intramolecular model. Furthermore, dephosphorylation exhibited monotonic kinetics with a rate well below the diffusion limit. Thus, several different lines of analysis support the intermolecular model for dephosphorylation, in which the protein phosphatase must encounter its substrate to effect catalysis. In contrast to the monotonic kinetics of dephosphorylation, the phosphorylation reaction exhibited sigmoidal kinetics, with a rate that depended on membrane potential. Voltage dependence is an unlikely property for a kinetic step involving encounters resulting from diffusion. Furthermore, the velocity of the phosphorylation reaction exceeded the diffusion limit, and this observation is inconsistent with the intermolecular model. Thus, both intermolecular and intramolecular enzymatic mechanisms operate in the modulation of the calcium-activated potassium channel of the posterior pituitary. These studies provide a functional characterization of the interactions between enzyme and substrate in intact patches of cell membrane." @default.
• W1975592859 created "2016-06-24" @default.
• W1975592859 creator A5027305249 @default.
• W1975592859 creator A5046833465 @default.
• W1975592859 date "1994-06-01" @default.
• W1975592859 modified "2023-10-14" @default.
• W1975592859 title "Intramolecular and intermolecular enzymatic modulation of ion channels in excised membrane patches" @default.
• W1975592859 cites W1436525548 @default.
• W1975592859 cites W1883087802 @default.
• W1975592859 cites W1953658339 @default.
• W1975592859 cites W1974997331 @default.
• W1975592859 cites W1976243291 @default.
• W1975592859 cites W1983918349 @default.
• W1975592859 cites W1984308273 @default.
• W1975592859 cites W1984434545 @default.
• W1975592859 cites W1986909301 @default.
• W1975592859 cites W1997511216 @default.
• W1975592859 cites W2002957477 @default.
• W1975592859 cites W2009667219 @default.
• W1975592859 cites W2009758634 @default.
• W1975592859 cites W2015426350 @default.
• W1975592859 cites W2016311464 @default.
• W1975592859 cites W2019433768 @default.
• W1975592859 cites W2019945905 @default.
• W1975592859 cites W2024184910 @default.
• W1975592859 cites W2035395088 @default.
• W1975592859 cites W2036991975 @default.
• W1975592859 cites W2039599894 @default.
• W1975592859 cites W2046322215 @default.
• W1975592859 cites W2049914201 @default.
• W1975592859 cites W2050567695 @default.
• W1975592859 cites W2073068631 @default.
• W1975592859 cites W2075625699 @default.
• W1975592859 cites W2092020962 @default.
• W1975592859 cites W2092552227 @default.
• W1975592859 cites W2101811790 @default.
• W1975592859 cites W2129160359 @default.
• W1975592859 cites W2169198206 @default.
• W1975592859 cites W2172481658 @default.
• W1975592859 cites W2222790656 @default.
• W1975592859 cites W2467448488 @default.
• W1975592859 doi "https://doi.org/10.1016/s0006-3495(94)80984-1" @default.
• W1975592859 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1275916" @default.
• W1975592859 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7521226" @default.
• W1975592859 hasPublicationYear "1994" @default.
• W1975592859 type Work @default.
• W1975592859 sameAs 1975592859 @default.
• W1975592859 citedByCount "24" @default.
• W1975592859 countsByYear W19755928592014 @default.
• W1975592859 countsByYear W19755928592015 @default.
• W1975592859 crossrefType "journal-article" @default.
• W1975592859 hasAuthorship W1975592859A5027305249 @default.
• W1975592859 hasAuthorship W1975592859A5046833465 @default.
• W1975592859 hasBestOaLocation W19755928591 @default.
• W1975592859 hasConcept C11960822 @default.
• W1975592859 hasConcept C12554922 @default.
• W1975592859 hasConcept C166950319 @default.
• W1975592859 hasConcept C178666793 @default.
• W1975592859 hasConcept C178790620 @default.
• W1975592859 hasConcept C181912034 @default.
• W1975592859 hasConcept C185592680 @default.
• W1975592859 hasConcept C18903297 @default.
• W1975592859 hasConcept C2777289219 @default.
• W1975592859 hasConcept C32909587 @default.
• W1975592859 hasConcept C55493867 @default.
• W1975592859 hasConcept C71240020 @default.
• W1975592859 hasConcept C75079739 @default.
• W1975592859 hasConcept C86803240 @default.
• W1975592859 hasConceptScore W1975592859C11960822 @default.
• W1975592859 hasConceptScore W1975592859C12554922 @default.
• W1975592859 hasConceptScore W1975592859C166950319 @default.
• W1975592859 hasConceptScore W1975592859C178666793 @default.
• W1975592859 hasConceptScore W1975592859C178790620 @default.
• W1975592859 hasConceptScore W1975592859C181912034 @default.
• W1975592859 hasConceptScore W1975592859C185592680 @default.
• W1975592859 hasConceptScore W1975592859C18903297 @default.
• W1975592859 hasConceptScore W1975592859C2777289219 @default.
• W1975592859 hasConceptScore W1975592859C32909587 @default.
• W1975592859 hasConceptScore W1975592859C55493867 @default.
• W1975592859 hasConceptScore W1975592859C71240020 @default.
• W1975592859 hasConceptScore W1975592859C75079739 @default.
• W1975592859 hasConceptScore W1975592859C86803240 @default.
• W1975592859 hasIssue "6" @default.
• W1975592859 hasLocation W19755928591 @default.
• W1975592859 hasLocation W19755928592 @default.
• W1975592859 hasLocation W19755928593 @default.
• W1975592859 hasLocation W19755928594 @default.
• W1975592859 hasOpenAccess W1975592859 @default.
• W1975592859 hasPrimaryLocation W19755928591 @default.
• W1975592859 hasRelatedWork W1972691843 @default.
• W1975592859 hasRelatedWork W1975616086 @default.
• W1975592859 hasRelatedWork W2014552723 @default.
• W1975592859 hasRelatedWork W2015862623 @default.
• W1975592859 hasRelatedWork W2033875669 @default.
• W1975592859 hasRelatedWork W2044365168 @default.
• W1975592859 hasRelatedWork W2068751031 @default.
• W1975592859 hasRelatedWork W2345376172 @default.
• W1975592859 hasRelatedWork W2810494566 @default.

• next