APOBEC3G is degraded by the proteasomal pathway in a vif-dependent manner without being polyubiquitylated

Journal of Biological Chemistry

Volumn 283, Issue 19, 2008, Pages 13124-13131

  Dang, Ying ^a   Lai, Mun Siew ^a   Zheng, Yong Hui ^a,b  

^a Michigan State University ^*  (United States)

^b MICHIGAN STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; PROTEINS; VIRUSES;

BINDING PARTNERS; COVALENT ATTACHMENTS; CYTIDINE DEAMINASE; HUMAN IMMUNODEFICIENCY VIRUSES; ISOPEPTIDE LIGASE; LYSINE RESIDUES; POLYUBIQUITIN; POLYUBIQUITYLATION; PROTEASOMAL DEGRADATIONS; PROTEASOMAL PATHWAYS; PROTEASOMES; REVERSE TRANSCRIPTIONS; UBIQUITIN; UBIQUITYLATION; VIRAL INFECTIVITY FACTORS;

DEGRADATION;

APOLIPOPROTEIN B MRNA EDITING CATALYTIC POLYPEPTIDE 3; COMPLEMENTARY DNA; CULLIN; CYTIDINE DEAMINASE; GLUTATHIONE TRANSFERASE; LUCIFERASE; LYSINE; PLASMID DNA; POLYPEPTIDE; POLYUBIQUITIN; PROTEASOME; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VIF PROTEIN; VIRUS PROTEIN; APOBEC3G PROTEIN, HUMAN; CUL5 PROTEIN, HUMAN; VIF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

AMINO ACID SEQUENCE; ARTICLE; CHROMOSOME 22; CONTROLLED STUDY; ENZYME ASSAY; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; HUMAN CELL; HUMAN IMMUNODEFICIENCY VIRUS 1; HUMAN IMMUNODEFICIENCY VIRUS 1 INFECTION; NONHUMAN; PLASMID; POLYACRYLAMIDE GEL ELECTROPHORESIS; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; REPORTER GENE; VIRUS CELL INTERACTION; VIRUS INHIBITION; VIRUS REPLICATION; CELL LINE; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; UBIQUITINATION;

HUMAN IMMUNODEFICIENCY VIRUS 1;

AMINO ACID SEQUENCE; CELL LINE; CULLIN PROTEINS; CYTIDINE DEAMINASE; HIV-1; HUMANS; MOLECULAR SEQUENCE DATA; MUTATION; PROTEASOME ENDOPEPTIDASE COMPLEX; SUBSTRATE SPECIFICITY; UBIQUITINATION; VIF GENE PRODUCTS, HUMAN IMMUNODEFICIENCY VIRUS;

EID: 45149106103     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M708728200     Document Type: Article

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