FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2014283693> ?p ?o ?g. }

• W2014283693 endingPage "557" @default.
• W2014283693 startingPage "546" @default.
• W2014283693 abstract "Abstract Vpu is an 81‐residue accessory protein of HIV‐1. Because it is a membrane protein, it presents substantial technical challenges for the characterization of its structure and function, which are of considerable interest because the protein enhances the release of new virus particles from cells infected with HIV‐1 and induces the intracellular degradation of the CD4 receptor protein. The Vpu‐mediated enhancement of the virus release rate from HIV‐1‐infected cells is correlated with the expression of an ion channel activity associated with the transmembrane hydrophobic helical domain. Vpu‐induced CD4 degradation and, to a lesser extent, enhancement of particle release are both dependent on the phosphorylation of two highly conserved serine residues in the cytoplasmic domain of Vpu. To define the minimal folding units of Vpu and to identify their activities, we prepared three truncated forms of Vpu and compared their structural and functional properties to those of full‐length Vpu (residues 2–81). Vpu 2–37 encompasses the N‐terminal transmembrane α‐helix; Vpu 2–51 spans the N‐terminal transmembrane helix and the first cytoplasmic α‐helix; Vpu 28–81 includes the entire cytoplasmic domain containing the two C‐terminal amphipathic α‐helices without the transmembrane helix. Uniformly isotopically labeled samples of the polypeptides derived from Vpu were prepared by expression of fusion proteins in E. coli and were studied in the model membrane environments of lipid micelles by solution NMR spectroscopy and oriented lipid bilayers by solid‐state NMR spectroscopy. The assignment of backbone resonances enabled the secondary structure of the constructs corresponding to the transmembrane and the cytoplasmic domains of Vpu to be defined in micelle samples by solution NMR spectroscopy. Solid‐state NMR spectra of the polypeptides in oriented lipid bilayers demonstrated that the topology of the domains is retained in the truncated polypeptides. The biological activities of the constructs of Vpu were evaluated. The ion channel activity is confined to the transmembrane α‐helix. The C‐terminal α‐helices modulate or promote the oligomerization of Vpu in the membrane and stabilize the conductive state of the channel, in addition to their involvement in CD4 degradation." @default.
• W2014283693 created "2016-06-24" @default.
• W2014283693 creator A5020312337 @default.
• W2014283693 creator A5035427242 @default.
• W2014283693 creator A5038390972 @default.
• W2014283693 creator A5046677875 @default.
• W2014283693 creator A5047434116 @default.
• W2014283693 creator A5059649140 @default.
• W2014283693 creator A5063595434 @default.
• W2014283693 creator A5070830317 @default.
• W2014283693 creator A5075012306 @default.
• W2014283693 creator A5085601838 @default.
• W2014283693 date "2002-03-01" @default.
• W2014283693 modified "2023-10-14" @default.
• W2014283693 title "Expression, purification, and activities of full‐length and truncated versions of the integral membrane protein Vpu from HIV‐1" @default.
• W2014283693 cites W1497943846 @default.
• W2014283693 cites W1498574963 @default.
• W2014283693 cites W1504625876 @default.
• W2014283693 cites W1511584652 @default.
• W2014283693 cites W1534033542 @default.
• W2014283693 cites W1555930389 @default.
• W2014283693 cites W1571744798 @default.
• W2014283693 cites W1658514113 @default.
• W2014283693 cites W1659719610 @default.
• W2014283693 cites W1857017278 @default.
• W2014283693 cites W1891596881 @default.
• W2014283693 cites W1964832767 @default.
• W2014283693 cites W1965489457 @default.
• W2014283693 cites W1974314313 @default.
• W2014283693 cites W1975304761 @default.
• W2014283693 cites W1975993749 @default.
• W2014283693 cites W1976172896 @default.
• W2014283693 cites W1984125372 @default.
• W2014283693 cites W1986322598 @default.
• W2014283693 cites W1986384364 @default.
• W2014283693 cites W1992144784 @default.
• W2014283693 cites W1994057597 @default.
• W2014283693 cites W1994277766 @default.
• W2014283693 cites W1999272522 @default.
• W2014283693 cites W2005039237 @default.
• W2014283693 cites W2015041653 @default.
• W2014283693 cites W2018643676 @default.
• W2014283693 cites W2019770663 @default.
• W2014283693 cites W2022496873 @default.
• W2014283693 cites W2027929929 @default.
• W2014283693 cites W2030017358 @default.
• W2014283693 cites W2036270340 @default.
• W2014283693 cites W2045684019 @default.
• W2014283693 cites W2049236358 @default.
• W2014283693 cites W2062973238 @default.
• W2014283693 cites W2097213667 @default.
• W2014283693 cites W2098608499 @default.
• W2014283693 cites W2106886123 @default.
• W2014283693 cites W2112328158 @default.
• W2014283693 cites W2115840790 @default.
• W2014283693 cites W2143984668 @default.
• W2014283693 cites W2334665661 @default.
• W2014283693 cites W2949250147 @default.
• W2014283693 cites W4242009576 @default.
• W2014283693 doi "https://doi.org/10.1110/ps.37302" @default.
• W2014283693 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2373459" @default.
• W2014283693 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11847278" @default.
• W2014283693 hasPublicationYear "2002" @default.
• W2014283693 type Work @default.
• W2014283693 sameAs 2014283693 @default.
• W2014283693 citedByCount "112" @default.
• W2014283693 countsByYear W20142836932012 @default.
• W2014283693 countsByYear W20142836932013 @default.
• W2014283693 countsByYear W20142836932014 @default.
• W2014283693 countsByYear W20142836932015 @default.
• W2014283693 countsByYear W20142836932016 @default.
• W2014283693 countsByYear W20142836932017 @default.
• W2014283693 countsByYear W20142836932020 @default.
• W2014283693 countsByYear W20142836932021 @default.
• W2014283693 countsByYear W20142836932023 @default.
• W2014283693 crossrefType "journal-article" @default.
• W2014283693 hasAuthorship W2014283693A5020312337 @default.
• W2014283693 hasAuthorship W2014283693A5035427242 @default.
• W2014283693 hasAuthorship W2014283693A5038390972 @default.
• W2014283693 hasAuthorship W2014283693A5046677875 @default.
• W2014283693 hasAuthorship W2014283693A5047434116 @default.
• W2014283693 hasAuthorship W2014283693A5059649140 @default.
• W2014283693 hasAuthorship W2014283693A5063595434 @default.
• W2014283693 hasAuthorship W2014283693A5070830317 @default.
• W2014283693 hasAuthorship W2014283693A5075012306 @default.
• W2014283693 hasAuthorship W2014283693A5085601838 @default.
• W2014283693 hasBestOaLocation W20142836932 @default.
• W2014283693 hasConcept C118892022 @default.
• W2014283693 hasConcept C12554922 @default.
• W2014283693 hasConcept C144647389 @default.
• W2014283693 hasConcept C161200384 @default.
• W2014283693 hasConcept C170493617 @default.
• W2014283693 hasConcept C185592680 @default.
• W2014283693 hasConcept C18903297 @default.
• W2014283693 hasConcept C190062978 @default.
• W2014283693 hasConcept C24530287 @default.
• W2014283693 hasConcept C2778530040 @default.
• W2014283693 hasConcept C2779965526 @default.

• next