FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1520385835> ?p ?o ?g. }

• W1520385835 endingPage "5236" @default.
• W1520385835 startingPage "5231" @default.
• W1520385835 abstract "The synaptic basal membrane protein agrin initiates the aggregation of acetylcholine receptors at the postsynaptic membrane of the developing neuromuscular junction. Recently, α-dystroglycan was found to be a major agrin-binding protein on the muscle cell surface and was therefore considered a candidate agrin receptor. Employing different truncation fragments of agrin, we determined regions of the protein involved in binding to α-dystroglycan and to heparin, an inhibitor of α-dystroglycan binding. Deletion of a 15-kDa fragment from the C terminus of agrin had no effect on its binding to α-dystroglycan from rabbit muscle membranes, even though this deletion completely abolishes its acetylcholine receptor aggregating activity. Conversely, deletion of a central region does not affect agrin's clustering activity, but reduced its affinity for α-dystroglycan. Combination of these two deletions resulted in a fragment of ~35 kDa that weakly bound to α-dystroglycan, but displayed no clustering activity. All of these fragments bound to heparin with high affinity. Thus, α-dystroglycan does not show the binding specificity expected for an agrin receptor. Our data suggest the existence of an additional component on the muscle cell surface that generates the observed ligand specificity. The synaptic basal membrane protein agrin initiates the aggregation of acetylcholine receptors at the postsynaptic membrane of the developing neuromuscular junction. Recently, α-dystroglycan was found to be a major agrin-binding protein on the muscle cell surface and was therefore considered a candidate agrin receptor. Employing different truncation fragments of agrin, we determined regions of the protein involved in binding to α-dystroglycan and to heparin, an inhibitor of α-dystroglycan binding. Deletion of a 15-kDa fragment from the C terminus of agrin had no effect on its binding to α-dystroglycan from rabbit muscle membranes, even though this deletion completely abolishes its acetylcholine receptor aggregating activity. Conversely, deletion of a central region does not affect agrin's clustering activity, but reduced its affinity for α-dystroglycan. Combination of these two deletions resulted in a fragment of ~35 kDa that weakly bound to α-dystroglycan, but displayed no clustering activity. All of these fragments bound to heparin with high affinity. Thus, α-dystroglycan does not show the binding specificity expected for an agrin receptor. Our data suggest the existence of an additional component on the muscle cell surface that generates the observed ligand specificity." @default.
• W1520385835 created "2016-06-24" @default.
• W1520385835 creator A5015538026 @default.
• W1520385835 creator A5062905648 @default.
• W1520385835 date "1996-03-01" @default.
• W1520385835 modified "2023-10-11" @default.
• W1520385835 title "Agrin Binding to α-Dystroglycan" @default.
• W1520385835 cites W1516158645 @default.
• W1520385835 cites W1528710182 @default.
• W1520385835 cites W1531251890 @default.
• W1520385835 cites W1538052598 @default.
• W1520385835 cites W1564301159 @default.
• W1520385835 cites W1968666078 @default.
• W1520385835 cites W1968957805 @default.
• W1520385835 cites W1969570221 @default.
• W1520385835 cites W1981850472 @default.
• W1520385835 cites W1987098829 @default.
• W1520385835 cites W1989272637 @default.
• W1520385835 cites W1994560336 @default.
• W1520385835 cites W1999880438 @default.
• W1520385835 cites W2003381971 @default.
• W1520385835 cites W2003481405 @default.
• W1520385835 cites W2008115339 @default.
• W1520385835 cites W2008169950 @default.
• W1520385835 cites W2008256279 @default.
• W1520385835 cites W2015114304 @default.
• W1520385835 cites W2042450135 @default.
• W1520385835 cites W2045644095 @default.
• W1520385835 cites W2046678465 @default.
• W1520385835 cites W2047428077 @default.
• W1520385835 cites W2056743924 @default.
• W1520385835 cites W2056884826 @default.
• W1520385835 cites W2058698951 @default.
• W1520385835 cites W2058966822 @default.
• W1520385835 cites W2068836997 @default.
• W1520385835 cites W2073377967 @default.
• W1520385835 cites W2083350777 @default.
• W1520385835 cites W2087362044 @default.
• W1520385835 cites W2089011655 @default.
• W1520385835 cites W2090390636 @default.
• W1520385835 cites W2090473949 @default.
• W1520385835 cites W2094689830 @default.
• W1520385835 cites W2108009593 @default.
• W1520385835 cites W2113222492 @default.
• W1520385835 cites W2120362450 @default.
• W1520385835 cites W2146367762 @default.
• W1520385835 cites W2146435874 @default.
• W1520385835 cites W2155080404 @default.
• W1520385835 cites W2167173372 @default.
• W1520385835 cites W70216565 @default.
• W1520385835 doi "https://doi.org/10.1074/jbc.271.9.5231" @default.
• W1520385835 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/8617807" @default.
• W1520385835 hasPublicationYear "1996" @default.
• W1520385835 type Work @default.
• W1520385835 sameAs 1520385835 @default.
• W1520385835 citedByCount "72" @default.
• W1520385835 countsByYear W15203858352012 @default.
• W1520385835 countsByYear W15203858352018 @default.
• W1520385835 countsByYear W15203858352019 @default.
• W1520385835 crossrefType "journal-article" @default.
• W1520385835 hasAuthorship W1520385835A5015538026 @default.
• W1520385835 hasAuthorship W1520385835A5062905648 @default.
• W1520385835 hasBestOaLocation W15203858351 @default.
• W1520385835 hasConcept C169760540 @default.
• W1520385835 hasConcept C170493617 @default.
• W1520385835 hasConcept C185592680 @default.
• W1520385835 hasConcept C189165786 @default.
• W1520385835 hasConcept C197341189 @default.
• W1520385835 hasConcept C2777240379 @default.
• W1520385835 hasConcept C2778384963 @default.
• W1520385835 hasConcept C2779024559 @default.
• W1520385835 hasConcept C2779814568 @default.
• W1520385835 hasConcept C55493867 @default.
• W1520385835 hasConcept C80161118 @default.
• W1520385835 hasConcept C86803240 @default.
• W1520385835 hasConcept C95444343 @default.
• W1520385835 hasConceptScore W1520385835C169760540 @default.
• W1520385835 hasConceptScore W1520385835C170493617 @default.
• W1520385835 hasConceptScore W1520385835C185592680 @default.
• W1520385835 hasConceptScore W1520385835C189165786 @default.
• W1520385835 hasConceptScore W1520385835C197341189 @default.
• W1520385835 hasConceptScore W1520385835C2777240379 @default.
• W1520385835 hasConceptScore W1520385835C2778384963 @default.
• W1520385835 hasConceptScore W1520385835C2779024559 @default.
• W1520385835 hasConceptScore W1520385835C2779814568 @default.
• W1520385835 hasConceptScore W1520385835C55493867 @default.
• W1520385835 hasConceptScore W1520385835C80161118 @default.
• W1520385835 hasConceptScore W1520385835C86803240 @default.
• W1520385835 hasConceptScore W1520385835C95444343 @default.
• W1520385835 hasIssue "9" @default.
• W1520385835 hasLocation W15203858351 @default.
• W1520385835 hasOpenAccess W1520385835 @default.
• W1520385835 hasPrimaryLocation W15203858351 @default.
• W1520385835 hasRelatedWork W1168805970 @default.
• W1520385835 hasRelatedWork W1963748908 @default.
• W1520385835 hasRelatedWork W1968278323 @default.
• W1520385835 hasRelatedWork W1992710299 @default.
• W1520385835 hasRelatedWork W2061672899 @default.

• next