FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2011723492> ?p ?o ?g. }

• W2011723492 endingPage "44" @default.
• W2011723492 startingPage "31" @default.
• W2011723492 abstract "Six amino-terminal deletion mutants of the NH2-terminally anchored (type II orientation) hemagglutinin-neuraminidase (HN) protein of parainfluenza virus type 3 were expressed in tissue culture by recombinant SV-40 viruses. The mutations consisted of progressive deletions of the cytoplasmic domain and, in some cases, of the hydrophobic signal/anchor. Three activities were dissociated for the signal/anchor: membrane insertion, translocation, and anchoring/transport. HN protein lacking the entire cytoplasmic tail was inserted efficiently into the membrane of the endoplasmic reticulum but was translocated inefficiently into the lumen. However, the small amounts that were successfully translocated appeared to be processed subsequently in a manner indistinguishable from that of parental HN. Thus, the cytoplasmic domain was not required for maturation of this type II glycoprotein. Progressive deletions into the membrane anchor restored efficient translocation, indicating that the NH2-terminal 44 amino acids were fully dispensable for membrane insertion and translocation and that a 10-amino acid hydrophobic signal sequence was sufficient for both activities. These latter HN molecules appeared to be folded authentically as assayed by hemagglutination activity, reactivity with a conformation-specific antiserum, correct formation of intramolecular disulfide bonds, and homooligomerization. However, most (85-90%) of these molecules accumulated in the ER. This showed that folding and oligomerization into a biologically active form, which presumably represents a virion spike, occurs essentially to completion within that compartment but is not sufficient for efficient transport through the exocytotic pathway. Protein transport also appeared to depend on the structure of the membrane anchor. These latter mutants were not stably integrated in the membrane, and the small proportion (10-15%) that was processed through the exocytotic pathway was secreted. The maturation steps and some of the effects of mutations described here for a type II glycoprotein resemble previous observations for prototypic type I glycoproteins and are indicative of close similarities in these processes for proteins of both membrane orientations." @default.
• W2011723492 created "2016-06-24" @default.
• W2011723492 creator A5027582911 @default.
• W2011723492 creator A5073973143 @default.
• W2011723492 date "1990-07-01" @default.
• W2011723492 modified "2023-09-26" @default.
• W2011723492 title "Intracellular processing and transport of NH2-terminally truncated forms of a hemagglutinin-neuraminidase type II glycoprotein." @default.
• W2011723492 cites W138271398 @default.
• W2011723492 cites W1527457670 @default.
• W2011723492 cites W1535265831 @default.
• W2011723492 cites W1537777030 @default.
• W2011723492 cites W1578161318 @default.
• W2011723492 cites W1927789601 @default.
• W2011723492 cites W1928492408 @default.
• W2011723492 cites W1935533918 @default.
• W2011723492 cites W1949134279 @default.
• W2011723492 cites W1963505541 @default.
• W2011723492 cites W1964449641 @default.
• W2011723492 cites W1973993781 @default.
• W2011723492 cites W1981862236 @default.
• W2011723492 cites W1989526931 @default.
• W2011723492 cites W1997662437 @default.
• W2011723492 cites W2002662104 @default.
• W2011723492 cites W2022000888 @default.
• W2011723492 cites W2024258680 @default.
• W2011723492 cites W2026929149 @default.
• W2011723492 cites W2027407556 @default.
• W2011723492 cites W2030812496 @default.
• W2011723492 cites W2035826838 @default.
• W2011723492 cites W2040453003 @default.
• W2011723492 cites W2042027043 @default.
• W2011723492 cites W2046389334 @default.
• W2011723492 cites W2048157776 @default.
• W2011723492 cites W2059838316 @default.
• W2011723492 cites W2070102173 @default.
• W2011723492 cites W2072664180 @default.
• W2011723492 cites W2081823976 @default.
• W2011723492 cites W2085676855 @default.
• W2011723492 cites W2097343334 @default.
• W2011723492 cites W2105534447 @default.
• W2011723492 cites W2110846125 @default.
• W2011723492 cites W2124756168 @default.
• W2011723492 cites W2127325978 @default.
• W2011723492 cites W2128207929 @default.
• W2011723492 cites W2139761159 @default.
• W2011723492 cites W2140223829 @default.
• W2011723492 cites W2152708819 @default.
• W2011723492 cites W2160107586 @default.
• W2011723492 cites W2164179462 @default.
• W2011723492 cites W2171903383 @default.
• W2011723492 doi "https://doi.org/10.1083/jcb.111.1.31" @default.
• W2011723492 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2116159" @default.
• W2011723492 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/2164031" @default.
• W2011723492 hasPublicationYear "1990" @default.
• W2011723492 type Work @default.
• W2011723492 sameAs 2011723492 @default.
• W2011723492 citedByCount "9" @default.
• W2011723492 countsByYear W20117234922016 @default.
• W2011723492 crossrefType "journal-article" @default.
• W2011723492 hasAuthorship W2011723492A5027582911 @default.
• W2011723492 hasAuthorship W2011723492A5073973143 @default.
• W2011723492 hasBestOaLocation W20117234921 @default.
• W2011723492 hasConcept C104317684 @default.
• W2011723492 hasConcept C10858879 @default.
• W2011723492 hasConcept C108625454 @default.
• W2011723492 hasConcept C134164806 @default.
• W2011723492 hasConcept C143065580 @default.
• W2011723492 hasConcept C158617107 @default.
• W2011723492 hasConcept C167625842 @default.
• W2011723492 hasConcept C181199279 @default.
• W2011723492 hasConcept C190062978 @default.
• W2011723492 hasConcept C2778692840 @default.
• W2011723492 hasConcept C515207424 @default.
• W2011723492 hasConcept C55493867 @default.
• W2011723492 hasConcept C86803240 @default.
• W2011723492 hasConcept C95444343 @default.
• W2011723492 hasConceptScore W2011723492C104317684 @default.
• W2011723492 hasConceptScore W2011723492C10858879 @default.
• W2011723492 hasConceptScore W2011723492C108625454 @default.
• W2011723492 hasConceptScore W2011723492C134164806 @default.
• W2011723492 hasConceptScore W2011723492C143065580 @default.
• W2011723492 hasConceptScore W2011723492C158617107 @default.
• W2011723492 hasConceptScore W2011723492C167625842 @default.
• W2011723492 hasConceptScore W2011723492C181199279 @default.
• W2011723492 hasConceptScore W2011723492C190062978 @default.
• W2011723492 hasConceptScore W2011723492C2778692840 @default.
• W2011723492 hasConceptScore W2011723492C515207424 @default.
• W2011723492 hasConceptScore W2011723492C55493867 @default.
• W2011723492 hasConceptScore W2011723492C86803240 @default.
• W2011723492 hasConceptScore W2011723492C95444343 @default.
• W2011723492 hasIssue "1" @default.
• W2011723492 hasLocation W20117234921 @default.
• W2011723492 hasLocation W20117234922 @default.
• W2011723492 hasLocation W20117234923 @default.
• W2011723492 hasLocation W20117234924 @default.
• W2011723492 hasOpenAccess W2011723492 @default.
• W2011723492 hasPrimaryLocation W20117234921 @default.
• W2011723492 hasRelatedWork W1917535562 @default.

• next