Matches in SemOpenAlex for { <https://semopenalex.org/work/W1967786141> ?p ?o ?g. }
Showing items 1 to 86 of
86
with 100 items per page.
- W1967786141 endingPage "3706" @default.
- W1967786141 startingPage "3702" @default.
- W1967786141 abstract "In illuminated rod outer segment membranes, GTP and guanosine 5'-[beta, gamma-imido]triphosphate (p[NH]ppG) have reciprocal effects on cGMP phosphodiesterase (PDEase; 3':5'-cyclic-nucleotide 5'-nucleotidohydrolase, EC 3.1.4.17) activity and cGMP binding to noncatalytic sites on that enzyme. Two micromolar p[NH]ppG increased PDEase activity more than 2-fold while inhibiting cGMP binding more than 40%. Reduction of noncatalytic cGMP binding, which followed addition of p[NH]ppG, was not a result of PDEase activation. Both effects of p[NH]ppG were completely dependent on the presence of bleached rhodopsin. A heat-stable factor has been found to inhibit PDEase activity and also to stimulate cGMP binding to noncatalytic cGMP binding sites. Addition of p[NH]ppG reversed the effects of this factor on both PDEase activity and cGMP binding. During purification of this material, the activity peaks for both PDEase inhibition and activation of noncatalytic cGMP binding comigrated on both Blue Sepharose CL-6B column chromatography and sucrose density gradients centrifugation, suggesting that the same factor could be responsible for both inhibition of PDEase activity and enhancement of noncatalytic cGMP binding. Limited tryptic proteolysis of PDEase, which markedly reduced cGMP binding to the noncatalytic sites, and experiments using highly purified cAMP (free of cGMP) as substrate for PDEase showed that the binding of cGMP to noncatalytic sites was not required for the heat-stable inhibitory factor to inhibit PDEase activity. We discuss possible relationships between the regulation of PDEase and the binding of cGMP to noncatalytic sites." @default.
- W1967786141 created "2016-06-24" @default.
- W1967786141 creator A5000309095 @default.
- W1967786141 creator A5030095220 @default.
- W1967786141 creator A5030924082 @default.
- W1967786141 creator A5032729264 @default.
- W1967786141 date "1982-06-01" @default.
- W1967786141 modified "2023-09-26" @default.
- W1967786141 title "Reciprocal effects of an inhibitory factor on catalytic activity and noncatalytic cGMP binding sites of rod phosphodiesterase." @default.
- W1967786141 cites W102592356 @default.
- W1967786141 cites W111988334 @default.
- W1967786141 cites W1485225530 @default.
- W1967786141 cites W1503740541 @default.
- W1967786141 cites W1964548100 @default.
- W1967786141 cites W1974617220 @default.
- W1967786141 cites W1994317901 @default.
- W1967786141 cites W2002308682 @default.
- W1967786141 cites W2016542329 @default.
- W1967786141 cites W2029479735 @default.
- W1967786141 cites W2035567650 @default.
- W1967786141 cites W2040057938 @default.
- W1967786141 cites W2113506485 @default.
- W1967786141 cites W2127944926 @default.
- W1967786141 cites W2128635872 @default.
- W1967786141 cites W2408825623 @default.
- W1967786141 cites W2413000770 @default.
- W1967786141 doi "https://doi.org/10.1073/pnas.79.12.3702" @default.
- W1967786141 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/346494" @default.
- W1967786141 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6285360" @default.
- W1967786141 hasPublicationYear "1982" @default.
- W1967786141 type Work @default.
- W1967786141 sameAs 1967786141 @default.
- W1967786141 citedByCount "96" @default.
- W1967786141 countsByYear W19677861412012 @default.
- W1967786141 countsByYear W19677861412013 @default.
- W1967786141 countsByYear W19677861412014 @default.
- W1967786141 countsByYear W19677861412018 @default.
- W1967786141 countsByYear W19677861412019 @default.
- W1967786141 countsByYear W19677861412020 @default.
- W1967786141 countsByYear W19677861412021 @default.
- W1967786141 crossrefType "journal-article" @default.
- W1967786141 hasAuthorship W1967786141A5000309095 @default.
- W1967786141 hasAuthorship W1967786141A5030095220 @default.
- W1967786141 hasAuthorship W1967786141A5030924082 @default.
- W1967786141 hasAuthorship W1967786141A5032729264 @default.
- W1967786141 hasBestOaLocation W19677861411 @default.
- W1967786141 hasConcept C107824862 @default.
- W1967786141 hasConcept C118716 @default.
- W1967786141 hasConcept C181199279 @default.
- W1967786141 hasConcept C185592680 @default.
- W1967786141 hasConcept C2777995097 @default.
- W1967786141 hasConcept C55493867 @default.
- W1967786141 hasConcept C62826618 @default.
- W1967786141 hasConcept C79418042 @default.
- W1967786141 hasConceptScore W1967786141C107824862 @default.
- W1967786141 hasConceptScore W1967786141C118716 @default.
- W1967786141 hasConceptScore W1967786141C181199279 @default.
- W1967786141 hasConceptScore W1967786141C185592680 @default.
- W1967786141 hasConceptScore W1967786141C2777995097 @default.
- W1967786141 hasConceptScore W1967786141C55493867 @default.
- W1967786141 hasConceptScore W1967786141C62826618 @default.
- W1967786141 hasConceptScore W1967786141C79418042 @default.
- W1967786141 hasIssue "12" @default.
- W1967786141 hasLocation W19677861411 @default.
- W1967786141 hasLocation W19677861412 @default.
- W1967786141 hasLocation W19677861413 @default.
- W1967786141 hasLocation W19677861414 @default.
- W1967786141 hasOpenAccess W1967786141 @default.
- W1967786141 hasPrimaryLocation W19677861411 @default.
- W1967786141 hasRelatedWork W1527029741 @default.
- W1967786141 hasRelatedWork W1967443949 @default.
- W1967786141 hasRelatedWork W1988823914 @default.
- W1967786141 hasRelatedWork W2007514289 @default.
- W1967786141 hasRelatedWork W2046624033 @default.
- W1967786141 hasRelatedWork W2052537837 @default.
- W1967786141 hasRelatedWork W2237660709 @default.
- W1967786141 hasRelatedWork W2248158391 @default.
- W1967786141 hasRelatedWork W2411341413 @default.
- W1967786141 hasRelatedWork W975436475 @default.
- W1967786141 hasVolume "79" @default.
- W1967786141 isParatext "false" @default.
- W1967786141 isRetracted "false" @default.
- W1967786141 magId "1967786141" @default.
- W1967786141 workType "article" @default.