Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity

Proteins: Structure, Function and Genetics

Volumn 69, Issue 2, 2007, Pages 270-284

  Auclair, Jared R ^a   Green, Karin M ^a   Shandilya, Shivender ^a   Evans, James E ^a   Somasundaran, Mohan ^a   Schiffer, Celia A ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

HIV 1 Vif; Intrinsic disorder; Mass spectrometry; Oligomerization; Topology

Indexed keywords

PEPTIDE FRAGMENT;

ARTICLE; DATA ANALYSIS; HUMAN IMMUNODEFICIENCY VIRUS 1; IMMUNOPRECIPITATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; OLIGOMERIZATION; PEPTIDE ANALYSIS; PREDICTION; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN STRUCTURE; VIRUS INFECTIVITY;

CROSS-LINKING REAGENTS; CYTIDINE DEAMINASE; GENE PRODUCTS, VIF; HIV INFECTIONS; HIV-1; HUMANS; PREDICTIVE VALUE OF TESTS; PROTEIN BINDING; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; TANDEM MASS SPECTROMETRY;

HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 34548713478     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.21471     Document Type: Article

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