FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W121680641> ?p ?o ?g. }

• W121680641 endingPage "4459" @default.
• W121680641 startingPage "4450" @default.
• W121680641 abstract "Research Article15 September 1995free access Calmodulin binding to Drosophila NinaC required for termination of phototransduction. J. A. Porter J. A. Porter Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author B. Minke B. Minke Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author C. Montell C. Montell Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author J. A. Porter J. A. Porter Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author B. Minke B. Minke Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author C. Montell C. Montell Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. Search for more papers by this author Author Information J. A. Porter1, B. Minke1 and C. Montell1 1Department of Biological Chemistry, Johns Hopkins University, School of Medicine, Baltimore, MD 21205, USA. The EMBO Journal (1995)14:4450-4459https://doi.org/10.1002/j.1460-2075.1995.tb00124.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info The ninaC locus encodes two unconventional myosins, p132 and p174, consisting of fused protein kinase and myosin head domains expressed in Drosophila photoreceptor cells. NinaC are the major calmodulin-binding proteins in the retina and the NinaC-calmodulin interaction is required for the normal subcellular localization of calmodulin as well as for normal photo-transduction. In the current report, we present evidence for two calmodulin-binding sites in NinaC, C1 and C2, which have different in vitro binding properties. C1 was found to be common to both p132 and p174 while C2 was unique to p174. To address the requirements for calmodulin binding at each site in vivo, we generated transgenic flies expressing ninaC genes deleted for either C1 or C2. We found that the spatial localization of calmodulin depended on binding to both C1 and C2. Furthermore, mutation of either site resulted in a defective photoresponse. A prolonged depolarization afterpotential (PDA) was elicited at lower light intensities than necessary to produce a PDA in wild-type flies. These results suggest that calmodulin binding to both C1 and C2 is required in vivo for termination of phototransduction. Previous ArticleNext Article Volume 14Issue 181 September 1995In this issue RelatedDetailsLoading ..." @default.
• W121680641 created "2016-06-24" @default.
• W121680641 creator A5047197225 @default.
• W121680641 creator A5059045594 @default.
• W121680641 creator A5085906302 @default.
• W121680641 date "1995-09-01" @default.
• W121680641 modified "2023-09-23" @default.
• W121680641 title "Calmodulin binding to Drosophila NinaC required for termination of phototransduction." @default.
• W121680641 cites W1496223818 @default.
• W121680641 cites W1498962226 @default.
• W121680641 cites W1576751611 @default.
• W121680641 cites W1595738876 @default.
• W121680641 cites W1964200801 @default.
• W121680641 cites W1972858438 @default.
• W121680641 cites W1979161220 @default.
• W121680641 cites W1981990755 @default.
• W121680641 cites W1987500506 @default.
• W121680641 cites W1994528729 @default.
• W121680641 cites W1994728394 @default.
• W121680641 cites W2001574178 @default.
• W121680641 cites W2014610293 @default.
• W121680641 cites W2014893784 @default.
• W121680641 cites W2015231758 @default.
• W121680641 cites W2017854700 @default.
• W121680641 cites W2018857111 @default.
• W121680641 cites W2022864334 @default.
• W121680641 cites W2024782877 @default.
• W121680641 cites W2029880376 @default.
• W121680641 cites W2056963317 @default.
• W121680641 cites W2078470195 @default.
• W121680641 cites W2097371819 @default.
• W121680641 cites W2101379527 @default.
• W121680641 cites W2103080800 @default.
• W121680641 cites W2104018418 @default.
• W121680641 cites W2109825947 @default.
• W121680641 cites W2111629985 @default.
• W121680641 cites W2152203056 @default.
• W121680641 cites W2159497398 @default.
• W121680641 cites W2160337925 @default.
• W121680641 cites W2162741288 @default.
• W121680641 cites W2166845172 @default.
• W121680641 cites W2415134306 @default.
• W121680641 cites W4229913877 @default.
• W121680641 cites W4245386636 @default.
• W121680641 doi "https://doi.org/10.1002/j.1460-2075.1995.tb00124.x" @default.
• W121680641 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/394537" @default.
• W121680641 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7556088" @default.
• W121680641 hasPublicationYear "1995" @default.
• W121680641 type Work @default.
• W121680641 sameAs 121680641 @default.
• W121680641 citedByCount "81" @default.
• W121680641 countsByYear W1216806412012 @default.
• W121680641 countsByYear W1216806412013 @default.
• W121680641 countsByYear W1216806412014 @default.
• W121680641 countsByYear W1216806412015 @default.
• W121680641 countsByYear W1216806412019 @default.
• W121680641 countsByYear W1216806412020 @default.
• W121680641 countsByYear W1216806412021 @default.
• W121680641 crossrefType "journal-article" @default.
• W121680641 hasAuthorship W121680641A5047197225 @default.
• W121680641 hasAuthorship W121680641A5059045594 @default.
• W121680641 hasAuthorship W121680641A5085906302 @default.
• W121680641 hasBestOaLocation W1216806411 @default.
• W121680641 hasConcept C131667965 @default.
• W121680641 hasConcept C161191863 @default.
• W121680641 hasConcept C169760540 @default.
• W121680641 hasConcept C181199279 @default.
• W121680641 hasConcept C2777093970 @default.
• W121680641 hasConcept C29688787 @default.
• W121680641 hasConcept C41008148 @default.
• W121680641 hasConcept C55493867 @default.
• W121680641 hasConcept C86803240 @default.
• W121680641 hasConceptScore W121680641C131667965 @default.
• W121680641 hasConceptScore W121680641C161191863 @default.
• W121680641 hasConceptScore W121680641C169760540 @default.
• W121680641 hasConceptScore W121680641C181199279 @default.
• W121680641 hasConceptScore W121680641C2777093970 @default.
• W121680641 hasConceptScore W121680641C29688787 @default.
• W121680641 hasConceptScore W121680641C41008148 @default.
• W121680641 hasConceptScore W121680641C55493867 @default.
• W121680641 hasConceptScore W121680641C86803240 @default.
• W121680641 hasIssue "18" @default.
• W121680641 hasLocation W1216806411 @default.
• W121680641 hasLocation W1216806412 @default.
• W121680641 hasLocation W1216806413 @default.
• W121680641 hasOpenAccess W121680641 @default.
• W121680641 hasPrimaryLocation W1216806411 @default.
• W121680641 hasRelatedWork W1973875627 @default.
• W121680641 hasRelatedWork W1995810743 @default.
• W121680641 hasRelatedWork W2018595727 @default.
• W121680641 hasRelatedWork W2028283916 @default.
• W121680641 hasRelatedWork W2052996930 @default.
• W121680641 hasRelatedWork W2056963317 @default.
• W121680641 hasRelatedWork W2127697107 @default.
• W121680641 hasRelatedWork W2159459905 @default.
• W121680641 hasRelatedWork W287586545 @default.
• W121680641 hasRelatedWork W4309269384 @default.
• W121680641 hasVolume "14" @default.

• next