FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1985048947> ?p ?o ?g. }

• W1985048947 endingPage "279" @default.
• W1985048947 startingPage "269" @default.
• W1985048947 abstract "The human erythrocyte anion exchanger (AE1, Band 3) contains up to 14 transmembrane segments, with a single site of N-glycosylation at Asn642 in extracellular (EC) loop 4. Scanning and insertional N-glycosylation mutagenesis were used to determine the folding pattern of AE1 in the membrane. Full-length AE1, when expressed in transfected human embryonic kidney (HEK)-293 or COS-7 cells, retained a high-mannose oligosaccharide structure. Scanning N-glycosylation mutagenesis of EC loop 4 showed that N-glycosylation acceptor sites (Asn-Xaa-Ser/Thr) spaced 12 residues from the ends of adjacent transmembrane segments could be N-glycosylated. An acceptor site introduced at position 743 in intracellular (IC) loop 5 that could be N-glycosylated in a cell-free translation system was not N-glycosylated in transfected cells. Mutations designed to disrupt the folding of this loop enhanced the level of N-glycosylation at Asn743 in vitro. The results suggest that this loop might be transiently exposed to the lumen of the endoplasmic reticulum during biosynthesis but normally folds rapidly, precluding N-glycosylation. EC loop 4 insertions into positions 428, 484, 754 and 854 in EC loops 1, 2, 6 and 7 respectively were efficiently N-glycosylated, showing that these regions were extracellular. EC loop 4 insertions into positions 731 or 785 were poorly N-glycosylated, which was inconsistent with an extracellular disposition for these regions of AE1. Insertion of EC loop 4 into positions 599 and 820 in IC loops 3 and 6 respectively were not N-glycosylated in cells, which was consistent with a cytosolic disposition for these loops. Inhibitor-affinity chromatography with 4-acetamido-4'-isothiocyanostilbene-2,2'-disulphonate (SITS)-Affi-Gel was used to assess whether the AE1 mutants were in a native state. Mutants with insertions at positions 428, 484, 599, 731 and 785 showed impaired inhibitor binding, whereas insertions at positions 754, 820 and 854 retained binding. The results indicate that the folding of the C-terminal region of AE1 is more complex than originally proposed and that this region of the transporter might have a dynamic aspect." @default.
• W1985048947 created "2016-06-24" @default.
• W1985048947 creator A5012677271 @default.
• W1985048947 creator A5075981682 @default.
• W1985048947 creator A5087326906 @default.
• W1985048947 date "1999-04-08" @default.
• W1985048947 modified "2023-10-18" @default.
• W1985048947 title "Transmembrane folding of the human erythrocyte anion exchanger (AE1, Band 3) determined by scanning and insertional N-glycosylation mutagenesis" @default.
• W1985048947 cites W126395666 @default.
• W1985048947 cites W1484236229 @default.
• W1985048947 cites W1537087455 @default.
• W1985048947 cites W1538907743 @default.
• W1985048947 cites W1539001193 @default.
• W1985048947 cites W1540324344 @default.
• W1985048947 cites W1552261626 @default.
• W1985048947 cites W1561829393 @default.
• W1985048947 cites W1678488130 @default.
• W1985048947 cites W171632912 @default.
• W1985048947 cites W1822034226 @default.
• W1985048947 cites W1966255545 @default.
• W1985048947 cites W1967660315 @default.
• W1985048947 cites W1970672690 @default.
• W1985048947 cites W1971371808 @default.
• W1985048947 cites W1976922469 @default.
• W1985048947 cites W1980505982 @default.
• W1985048947 cites W1980811217 @default.
• W1985048947 cites W1980832022 @default.
• W1985048947 cites W1981511829 @default.
• W1985048947 cites W1985811899 @default.
• W1985048947 cites W1989698947 @default.
• W1985048947 cites W2000396915 @default.
• W1985048947 cites W2015759706 @default.
• W1985048947 cites W2018289835 @default.
• W1985048947 cites W2026230704 @default.
• W1985048947 cites W2027109671 @default.
• W1985048947 cites W2039237350 @default.
• W1985048947 cites W2040360036 @default.
• W1985048947 cites W2046187735 @default.
• W1985048947 cites W2047340084 @default.
• W1985048947 cites W2048034139 @default.
• W1985048947 cites W2051619299 @default.
• W1985048947 cites W2054711229 @default.
• W1985048947 cites W2060913542 @default.
• W1985048947 cites W2060914976 @default.
• W1985048947 cites W2071315089 @default.
• W1985048947 cites W2091697939 @default.
• W1985048947 cites W2093156433 @default.
• W1985048947 cites W2099602045 @default.
• W1985048947 cites W2100837269 @default.
• W1985048947 cites W2101108802 @default.
• W1985048947 cites W2112150224 @default.
• W1985048947 cites W2138270253 @default.
• W1985048947 cites W2149563853 @default.
• W1985048947 cites W2170550107 @default.
• W1985048947 cites W2181153785 @default.
• W1985048947 cites W2242135922 @default.
• W1985048947 cites W2280462289 @default.
• W1985048947 cites W2408808204 @default.
• W1985048947 cites W259081840 @default.
• W1985048947 cites W2991971711 @default.
• W1985048947 cites W92181112 @default.
• W1985048947 cites W93255434 @default.
• W1985048947 doi "https://doi.org/10.1042/bj3390269" @default.
• W1985048947 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1220155" @default.
• W1985048947 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10191257" @default.
• W1985048947 hasPublicationYear "1999" @default.
• W1985048947 type Work @default.
• W1985048947 sameAs 1985048947 @default.
• W1985048947 citedByCount "63" @default.
• W1985048947 countsByYear W19850489472012 @default.
• W1985048947 countsByYear W19850489472013 @default.
• W1985048947 countsByYear W19850489472014 @default.
• W1985048947 countsByYear W19850489472015 @default.
• W1985048947 countsByYear W19850489472016 @default.
• W1985048947 countsByYear W19850489472017 @default.
• W1985048947 countsByYear W19850489472018 @default.
• W1985048947 countsByYear W19850489472021 @default.
• W1985048947 crossrefType "journal-article" @default.
• W1985048947 hasAuthorship W1985048947A5012677271 @default.
• W1985048947 hasAuthorship W1985048947A5075981682 @default.
• W1985048947 hasAuthorship W1985048947A5087326906 @default.
• W1985048947 hasBestOaLocation W19850489472 @default.
• W1985048947 hasConcept C104317684 @default.
• W1985048947 hasConcept C108625454 @default.
• W1985048947 hasConcept C118892022 @default.
• W1985048947 hasConcept C143065580 @default.
• W1985048947 hasConcept C144647389 @default.
• W1985048947 hasConcept C153911025 @default.
• W1985048947 hasConcept C158617107 @default.
• W1985048947 hasConcept C16318435 @default.
• W1985048947 hasConcept C170493617 @default.
• W1985048947 hasConcept C185592680 @default.
• W1985048947 hasConcept C206212055 @default.
• W1985048947 hasConcept C24530287 @default.
• W1985048947 hasConcept C2776589458 @default.
• W1985048947 hasConcept C2777313579 @default.
• W1985048947 hasConcept C28406088 @default.
• W1985048947 hasConcept C30324644 @default.

• next