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1 to 25 of 25  Show
  1. 1
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
    Category: Sequences.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 8 other entries.

  2. 2
    "Induction of phosphorylation of human immunodeficiency virus type 1 Nef and enhancement of CD4 down-regulation by phorbol myristate acetate."
    Luo T., Downing J.R., Garcia J.V.
    J. Virol. 71:2535-2539(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-107.
    Category: Pathology & Biotech, PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).
  3. 3
    "SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by the Nef protein of HIV-1."
    Briggs S.D., Sharkey M., Stevenson M., Smithgall T.E.
    J. Biol. Chem. 272:17899-17902(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  4. 4
    "Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4."
    Lu X., Yu H., Liu S.-H., Brodsky F.M., Peterlin B.M.
    Immunity 8:647-656(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ATP6V1H.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  5. 5
    "Induction of Fas ligand expression by HIV involves the interaction of Nef with the T cell receptor zeta chain."
    Xu X.-N., Laffert B., Screaton G.R., Kraft M., Wolf D., Kolanus W., Mongkolsapay J., McMichael A.J., Baur A.S.
    J. Exp. Med. 189:1489-1496(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HOST TCR-ZETA CHAIN/TCR-ZETA.
    Category: Function, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  6. 6
    "HIV-1 Nef plays an essential role in two independent processes in CD4 down-regulation: dissociation of the CD4-p56(lck) complex and targeting of CD4 to lysosomes."
    Kim Y.-H., Chang S.H., Kwon J.H., Rhee S.S.
    Virology 257:208-219(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).
  7. 7
    Cited for: FUNCTION, INTERACTION WITH PAK2.
    Category: Function, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 other entries.

  8. 8
    "Nef triggers a transcriptional program in T cells imitating single-signal T cell activation and inducing HIV virulence mediators."
    Simmons A., Aluvihare V., McMichael A.
    Immunity 14:763-777(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Category: Function.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  9. 9
    "HIV-1 Nef associated PAK and PI3-kinases stimulate Akt-independent Bad-phosphorylation to induce anti-apoptotic signals."
    Wolf D., Witte V., Laffert B., Blume K., Stromer E., Trapp S., d'Aloja P., Schuermann A., Baur A.S.
    Nat. Med. 7:1217-1224(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A NEF/PI3-KINASE/PAK2 COMPLEX.
    Category: Function, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).
  10. 10
    "A natural variability in the proline-rich motif of Nef modulates HIV-1 replication in primary T cells."
    Fackler O.T., Wolf D., Weber H.O., Laffert B., D'Aloja P., Schuler-Thurner B., Geffin R., Saksela K., Geyer M., Peterlin B.M., Schuler G., Baur A.S.
    Curr. Biol. 11:1294-1299(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-75.
    Category: Pathology & Biotech.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  11. 11
    "Interaction between Nef and phosphatidylinositol-3-kinase leads to activation of p21-activated kinase and increased production of HIV."
    Linnemann T., Zheng Y.-H., Mandic R., Peterlin B.M.
    Virology 294:246-255(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN PI3-KINASE.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  12. 12
    "Subunit H of the V-ATPase involved in endocytosis shows homology to beta-adaptins."
    Geyer M., Fackler O.T., Peterlin B.M.
    Mol. Biol. Cell 13:2045-2056(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ATP6V1H, MUTAGENESIS OF 168-LEU-LEU-169 AND 178-GLU-ASP-179.
    Category: Pathology & Biotech, Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).
  13. 13
    "Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery."
    Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.-H., Fackler O.T., Peterlin B.M.
    J. Biol. Chem. 277:28521-28529(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN ATP6V1H.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 2 and mapped to 6 other entries.

  14. 14
    "HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction."
    Trible R.P., Emert-Sedlak L., Smithgall T.E.
    J. Biol. Chem. 281:27029-27038(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SH3-BINDING MOTIF, FUNCTION, INTERACTION WITH HOST HCK, INTERACTION WITH HOST LYN, INTERACTION WITH HOST SRC.
    Category: Function, Interaction, Family & Domains.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  15. 15
    "Biochemical indication for myristoylation-dependent conformational changes in HIV-1 Nef."
    Breuer S., Gerlach H., Kolaric B., Urbanke C., Opitz N., Geyer M.
    Biochemistry 45:2339-2349(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
    Category: Interaction.
    Source: UniProtKB/Swiss-Prot (reviewed).
  16. 16
    "Novel (n)PKC kinases phosphorylate Nef for increased HIV transcription, replication and perinuclear targeting."
    Wolf D., Giese S.I., Witte V., Krautkraemer E., Trapp S., Sass G., Haller C., Blume K., Fackler O.T., Baur A.S.
    Virology 370:45-54(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-6.
    Category: PTM / Processing.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is mapped to 4 other entries.

  17. 17
    "Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by intermolecular domain assembly."
    Horenkamp F.A., Breuer S., Schulte A., Lulf S., Weyand M., Saksela K., Geyer M.
    Traffic 12:867-877(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 45-210, DILEUCINE MOTIF.
    Category: Structure, Family & Domains.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is cited by 1 other entry.

  18. 18
    "Interaction with the Src homology (SH3-SH2) region of the Src-family kinase Hck structures the HIV-1 Nef dimer for kinase activation and effector recruitment."
    Alvarado J.J., Tarafdar S., Yeh J.I., Smithgall T.E.
    J. Biol. Chem. 289:28539-28553(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 62-209, INTERACTION WITH HOST HCK.
    Category: Interaction, Structure.
    Source: UniProtKB/Swiss-Prot (reviewed).

    This publication is mapped to 4 other entries.

  19. 19
    "Conserved residues in the HIV-1 Nef hydrophobic pocket are essential for recruitment and activation of the Hck tyrosine kinase."
    Choi H.J., Smithgall T.E.
    J. Mol. Biol. 343:1255-1268(2004) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P03407.

    This publication is mapped to 4 other entries.

  20. 20
    "Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef."
    Breuer S., Schievink S.I., Schulte A., Blankenfeldt W., Fackler O.T., Geyer M.
    PLoS ONE 6:E20033-E20033(2011) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:3REA, PDB:3REB.
  21. 21
    "Structural recognition mechanisms between human Src homology domain 3 (SH3) and ALG-2-interacting protein X (Alix)."
    Shi X., Betzi S., Lugari A., Opi S., Restouin A., Parrot I., Martinez J., Zimmermann P., Lecine P., Huang M., Arold S.T., Collette Y., Morelli X.
    FEBS Lett. 586:1759-1764(2012) [PubMed] [Europe PMC] [Abstract]
    Category: Interaction.
    Source: IntAct:P03407.

    This publication is mapped to 7 other entries.

  22. 22
    "Structural basis for the inhibition of HIV-1 Nef by a high-affinity binding single-domain antibody."
    Lulf S., Matz J., Rouyez M.C., Jarviluoma A., Saksela K., Benichou S., Geyer M.
    Retrovirology 11:24-24(2014) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:4ORZ.

    This publication is mapped to 1 other entry.

  23. 23
    "A molecular switch in immunodominant HIV-1-specific CD8 T-cell epitopes shapes differential HLA-restricted escape."
    Kloverpris H.N., Cole D.K., Fuller A., Carlson J., Beck K., Schauenburg A.J., Rizkallah P.J., Buus S., Sewell A.K., Goulder P.
    Retrovirology 12:20-20(2015) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:4U1M, PDB:4U1K, PDB:4U1L, PDB:4U1N.

    This publication is mapped to 6 other entries.

  24. 24
    "Conserved Vdelta1 Binding Geometry in a Setting of Locus-Disparate pHLA Recognition by delta/alphabeta T Cell Receptors (TCRs): Insight into Recognition of HIV Peptides by TCRs."
    Shi Y., Kawana-Tachikawa A., Gao F., Qi J., Liu C., Gao J., Cheng H., Ueno T., Iwamoto A., Gao G.F.
    J. Virol. 91:0-0(2017) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:5XOV.

    This publication is mapped to 4 other entries.

  25. 25
    "A single beta-octyl glucoside molecule induces HIV-1 Nef dimer formation in the absence of partner protein binding."
    Wu M., Alvarado J.J., Augelli-Szafran C.E., Ptak R.G., Smithgall T.E.
    PLoS ONE 13:e0192512-e0192512(2018) [PubMed] [Europe PMC] [Abstract]
    Category: Structure.
    Source: PDB:6B72.
1 to 25 of 25  Show
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