FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2807537095> ?p ?o ?g. }

• W2807537095 endingPage "17" @default.
• W2807537095 startingPage "17" @default.
• W2807537095 abstract "<ns4:p><ns4:bold>Background</ns4:bold>: In Duchenne muscular dystrophy, primary abnormalities in the membrane cytoskeletal protein dystrophin trigger the loss of sarcolemmal linkage between the extracellular matrix component laminin-211 and the intracellular cortical actin membrane cytoskeleton. The disintegration of the dystrophin-associated glycoprotein complex renders the plasma membrane of contractile fibres more susceptible to micro-rupturing, which is associated with abnormal calcium handling and impaired cellular signalling in dystrophinopathy.</ns4:p><ns4:p> <ns4:bold>Methods</ns4:bold>: The oligomerisation pattern of β-dystroglycan, an integral membrane protein belonging to the core dystrophin complex, was studied using immunoprecipitation and chemical crosslinking analysis. A homo-bifunctional and non-cleavable agent with water-soluble and amine-reactive properties was employed to study protein oligomerisation in normal versus dystrophin-deficient skeletal muscles. Crosslinker-induced protein oligomerisation was determined by a combination of gel-shift analysis and immunoblotting.</ns4:p><ns4:p> <ns4:bold>Results</ns4:bold>: Although proteomics was successfully applied for the identification of dystroglycan as a key component of the dystrophin-associated glycoprotein complex in the muscle membrane fraction, mass spectrometric analysis did not efficiently recognize this relatively low-abundance protein after immunoprecipitation or chemical crosslinking. As an alternative approach, comparative immunoblotting was used to evaluate the effects of chemical crosslinking. Antibody decoration of the crosslinked microsomal protein fraction from wild type versus the <ns4:italic>mdx-4cv</ns4:italic> mouse model of dystrophinopathy revealed oligomers that contain β-dystroglycan. The protein exhibited a comparable reduction in gel electrophoretic mobility in both normal and dystrophic samples. The membrane repair proteins dysferlin and myoferlin, which are essential components of fibre regeneration, as well as the caveolae-associated protein cavin-1, were also shown to exist in high-molecular mass complexes.</ns4:p><ns4:p> <ns4:bold>Conclusions</ns4:bold>: The muscular dystrophy-related reduction in the concentration of β-dystroglycan, which forms in conjunction with its extracellular binding partner α-dystroglycan a critical plasmalemmal receptor for laminin-211, does not appear to alter its oligomeric status. Thus, independent of direct interactions with dystrophin, this sarcolemmal glycoprotein appears to exist in a supramolecular assembly in muscle.</ns4:p>" @default.
• W2807537095 created "2018-06-13" @default.
• W2807537095 creator A5040363034 @default.
• W2807537095 creator A5043932435 @default.
• W2807537095 creator A5047802928 @default.
• W2807537095 creator A5060710417 @default.
• W2807537095 creator A5079726240 @default.
• W2807537095 date "2018-09-17" @default.
• W2807537095 modified "2023-10-16" @default.
• W2807537095 title "Chemical crosslinking analysis of β-dystroglycan in dystrophin-deficient skeletal muscle" @default.
• W2807537095 cites W127884157 @default.
• W2807537095 cites W1581376189 @default.
• W2807537095 cites W1643243341 @default.
• W2807537095 cites W1861332892 @default.
• W2807537095 cites W1965858834 @default.
• W2807537095 cites W1966972600 @default.
• W2807537095 cites W1968666078 @default.
• W2807537095 cites W1969067769 @default.
• W2807537095 cites W1973573851 @default.
• W2807537095 cites W2004373320 @default.
• W2807537095 cites W2008980136 @default.
• W2807537095 cites W2020800885 @default.
• W2807537095 cites W2021019297 @default.
• W2807537095 cites W2022722729 @default.
• W2807537095 cites W2025857026 @default.
• W2807537095 cites W2033305820 @default.
• W2807537095 cites W2034276422 @default.
• W2807537095 cites W2037199116 @default.
• W2807537095 cites W2038685361 @default.
• W2807537095 cites W2039306818 @default.
• W2807537095 cites W2044859197 @default.
• W2807537095 cites W2048864017 @default.
• W2807537095 cites W2059155059 @default.
• W2807537095 cites W2066180106 @default.
• W2807537095 cites W2106490838 @default.
• W2807537095 cites W2115254768 @default.
• W2807537095 cites W2123463092 @default.
• W2807537095 cites W2123966033 @default.
• W2807537095 cites W2126902662 @default.
• W2807537095 cites W2130212557 @default.
• W2807537095 cites W2148034459 @default.
• W2807537095 cites W2156427063 @default.
• W2807537095 cites W2160038542 @default.
• W2807537095 cites W2163955564 @default.
• W2807537095 cites W2180766656 @default.
• W2807537095 cites W2206766868 @default.
• W2807537095 cites W2223441991 @default.
• W2807537095 cites W2292256860 @default.
• W2807537095 cites W2339052205 @default.
• W2807537095 cites W2460612197 @default.
• W2807537095 cites W2465807227 @default.
• W2807537095 cites W2563121704 @default.
• W2807537095 cites W2580534958 @default.
• W2807537095 cites W2603459612 @default.
• W2807537095 cites W2605417878 @default.
• W2807537095 cites W2675610046 @default.
• W2807537095 cites W2744859841 @default.
• W2807537095 cites W2791744074 @default.
• W2807537095 cites W2792351470 @default.
• W2807537095 cites W2800724873 @default.
• W2807537095 cites W2801123070 @default.
• W2807537095 cites W4293247451 @default.
• W2807537095 doi "https://doi.org/10.12688/hrbopenres.12846.2" @default.
• W2807537095 hasPublicationYear "2018" @default.
• W2807537095 type Work @default.
• W2807537095 sameAs 2807537095 @default.
• W2807537095 citedByCount "1" @default.
• W2807537095 countsByYear W28075370952019 @default.
• W2807537095 crossrefType "journal-article" @default.
• W2807537095 hasAuthorship W2807537095A5040363034 @default.
• W2807537095 hasAuthorship W2807537095A5043932435 @default.
• W2807537095 hasAuthorship W2807537095A5047802928 @default.
• W2807537095 hasAuthorship W2807537095A5060710417 @default.
• W2807537095 hasAuthorship W2807537095A5079726240 @default.
• W2807537095 hasBestOaLocation W28075370951 @default.
• W2807537095 hasConcept C105702510 @default.
• W2807537095 hasConcept C142669718 @default.
• W2807537095 hasConcept C1491633281 @default.
• W2807537095 hasConcept C199096232 @default.
• W2807537095 hasConcept C2778943923 @default.
• W2807537095 hasConcept C2779959927 @default.
• W2807537095 hasConcept C2780394045 @default.
• W2807537095 hasConcept C54355233 @default.
• W2807537095 hasConcept C55493867 @default.
• W2807537095 hasConcept C86803240 @default.
• W2807537095 hasConcept C95444343 @default.
• W2807537095 hasConceptScore W2807537095C105702510 @default.
• W2807537095 hasConceptScore W2807537095C142669718 @default.
• W2807537095 hasConceptScore W2807537095C1491633281 @default.
• W2807537095 hasConceptScore W2807537095C199096232 @default.
• W2807537095 hasConceptScore W2807537095C2778943923 @default.
• W2807537095 hasConceptScore W2807537095C2779959927 @default.
• W2807537095 hasConceptScore W2807537095C2780394045 @default.
• W2807537095 hasConceptScore W2807537095C54355233 @default.
• W2807537095 hasConceptScore W2807537095C55493867 @default.
• W2807537095 hasConceptScore W2807537095C86803240 @default.
• W2807537095 hasConceptScore W2807537095C95444343 @default.
• W2807537095 hasFunder F4320312041 @default.

• next