FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2098282337> ?p ?o ?g. }

• W2098282337 endingPage "284" @default.
• W2098282337 startingPage "270" @default.
• W2098282337 abstract "Abstract HIV‐1 Vif, an accessory protein in the viral genome, performs an important role in viral pathogenesis by facilitating the degradation of APOBEC3G, an endogenous cellular inhibitor of HIV‐1 replication. In this study, intrinsically disordered regions are predicted in HIV‐1 Vif using sequence‐based algorithms. Intrinsic disorder may explain why traditional structure determination of HIV‐1 Vif has been elusive, making structure‐based drug design impossible. To characterize HIV‐1 Vif's structural topology and to map the domains involved in oligomerization we used chemical cross‐linking, proteolysis, and mass spectrometry. Cross‐linking showed evidence of monomer, dimer, and trimer species via denaturing gel analysis and an additional tetramer via western blot analysis. We identified 47 unique linear peptides and 24 (13 intramolecular; 11 intermolecular) noncontiguous, cross‐linked peptides, among the noncross‐linked monomer, cross‐linked monomer, cross‐linked dimer, and cross‐linked trimer samples. Almost complete peptide coverage of the N‐terminus is observed in all samples analyzed, however reduced peptide coverage in the C‐terminal region is observed in the dimer and trimer samples. These differences in peptide coverage or “protections” between dimer and trimer indicate specific differences in packing between the two oligomeric forms. Intramolecular cross‐links within the monomer suggest that the N‐terminus is likely folded into a compact domain, while the C‐terminus remains intrinsically disordered. Upon oligomerization, as evidenced by the intermolecular cross‐links, the C‐terminus of one Vif protein becomes ordered by wrapping back on the N‐terminal domain of another. In addition, the majority of the intramolecular cross‐links map to regions that have been previously reported to be necessary for viral infectivity. Thus, this data suggests HIV‐1 Vif is in a dynamic equilibrium between the various oligomers potentially allowing it to interact with other binding partners. Proteins 2007. © 2007 Wiley‐Liss, Inc." @default.
• W2098282337 created "2016-06-24" @default.
• W2098282337 creator A5001131028 @default.
• W2098282337 creator A5009290437 @default.
• W2098282337 creator A5027145969 @default.
• W2098282337 creator A5051758668 @default.
• W2098282337 creator A5061873399 @default.
• W2098282337 creator A5071261828 @default.
• W2098282337 date "2007-06-27" @default.
• W2098282337 modified "2023-10-18" @default.
• W2098282337 title "Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity" @default.
• W2098282337 cites W1546971287 @default.
• W2098282337 cites W1585397042 @default.
• W2098282337 cites W1614881750 @default.
• W2098282337 cites W1796915314 @default.
• W2098282337 cites W1963594716 @default.
• W2098282337 cites W1964493335 @default.
• W2098282337 cites W1970120490 @default.
• W2098282337 cites W1971557089 @default.
• W2098282337 cites W1974719543 @default.
• W2098282337 cites W1975121208 @default.
• W2098282337 cites W1980996639 @default.
• W2098282337 cites W1982145590 @default.
• W2098282337 cites W1988594928 @default.
• W2098282337 cites W1991069890 @default.
• W2098282337 cites W1992984336 @default.
• W2098282337 cites W1993897877 @default.
• W2098282337 cites W1997874752 @default.
• W2098282337 cites W2001375348 @default.
• W2098282337 cites W2005044802 @default.
• W2098282337 cites W2006192061 @default.
• W2098282337 cites W2006419756 @default.
• W2098282337 cites W2009808421 @default.
• W2098282337 cites W2012816540 @default.
• W2098282337 cites W2015567856 @default.
• W2098282337 cites W2031513106 @default.
• W2098282337 cites W2035301032 @default.
• W2098282337 cites W2035939622 @default.
• W2098282337 cites W2037607325 @default.
• W2098282337 cites W2041874026 @default.
• W2098282337 cites W2042486230 @default.
• W2098282337 cites W2042882433 @default.
• W2098282337 cites W2044228723 @default.
• W2098282337 cites W2049476357 @default.
• W2098282337 cites W2049948812 @default.
• W2098282337 cites W2050310724 @default.
• W2098282337 cites W2063244983 @default.
• W2098282337 cites W2071068229 @default.
• W2098282337 cites W2072003663 @default.
• W2098282337 cites W2081093969 @default.
• W2098282337 cites W2082027989 @default.
• W2098282337 cites W2086250067 @default.
• W2098282337 cites W2092153867 @default.
• W2098282337 cites W2092233154 @default.
• W2098282337 cites W2096197897 @default.
• W2098282337 cites W2100032808 @default.
• W2098282337 cites W2105111621 @default.
• W2098282337 cites W2106340902 @default.
• W2098282337 cites W2119986079 @default.
• W2098282337 cites W2120881407 @default.
• W2098282337 cites W2131397695 @default.
• W2098282337 cites W2140460338 @default.
• W2098282337 cites W2143824409 @default.
• W2098282337 cites W2149643442 @default.
• W2098282337 cites W2152282874 @default.
• W2098282337 cites W2152630682 @default.
• W2098282337 cites W2157356733 @default.
• W2098282337 cites W2166597417 @default.
• W2098282337 cites W2171221859 @default.
• W2098282337 cites W2409902764 @default.
• W2098282337 doi "https://doi.org/10.1002/prot.21471" @default.
• W2098282337 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3366188" @default.
• W2098282337 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17598142" @default.
• W2098282337 hasPublicationYear "2007" @default.
• W2098282337 type Work @default.
• W2098282337 sameAs 2098282337 @default.
• W2098282337 citedByCount "46" @default.
• W2098282337 countsByYear W20982823372012 @default.
• W2098282337 countsByYear W20982823372013 @default.
• W2098282337 countsByYear W20982823372014 @default.
• W2098282337 countsByYear W20982823372015 @default.
• W2098282337 countsByYear W20982823372016 @default.
• W2098282337 countsByYear W20982823372020 @default.
• W2098282337 crossrefType "journal-article" @default.
• W2098282337 hasAuthorship W2098282337A5001131028 @default.
• W2098282337 hasAuthorship W2098282337A5009290437 @default.
• W2098282337 hasAuthorship W2098282337A5027145969 @default.
• W2098282337 hasAuthorship W2098282337A5051758668 @default.
• W2098282337 hasAuthorship W2098282337A5061873399 @default.
• W2098282337 hasAuthorship W2098282337A5071261828 @default.
• W2098282337 hasBestOaLocation W20982823372 @default.
• W2098282337 hasConcept C104317684 @default.
• W2098282337 hasConcept C12554922 @default.
• W2098282337 hasConcept C14053116 @default.
• W2098282337 hasConcept C166940927 @default.
• W2098282337 hasConcept C167625842 @default.
• W2098282337 hasConcept C178790620 @default.
• W2098282337 hasConcept C181199279 @default.

• next