The nef-like effect of murine leukemia virus glycosylated gag on HIV-1 infectivity is mediated by its cytoplasmic domain and depends on the AP-2 adaptor complex

Journal of Virology

Volumn 88, Issue 6, 2014, Pages 3443-3454

  Usami, Yoshiko ^a   Popov, Sergei ^a   Göttlinger, Heinrich G ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; GAG PROTEIN; NEF PROTEIN; PROTEIN AP 2; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CONTROLLED STUDY; CYTOPLASM; HUMAN IMMUNODEFICIENCY VIRUS 1 INFECTION; MUTAGENIC ACTIVITY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN MOTIF; PROTEIN PROTEIN INTERACTION; STRUCTURE ACTIVITY RELATION; VIRUS INFECTIVITY;

ADAPTOR PROTEIN COMPLEX 2; ADAPTOR PROTEIN COMPLEX MU SUBUNITS; ANIMALS; GENE PRODUCTS, GAG; GENE PRODUCTS, NEF; GLYCOSYLATION; HIV INFECTIONS; HIV-1; HUMANS; MICE; MOLONEY MURINE LEUKEMIA VIRUS; NEF GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS; PROTEIN STRUCTURE, TERTIARY;

EID: 84894595646     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01933-13     Document Type: Article

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