Structural recognition mechanisms between human Src homology domain 3 (SH3) and ALG‐2‐interacting protein X (Alix)

FynR96I physically interacts with NEF by two hybrid ( View interaction )

[1]  B. Blot,et al.  Alix, a Protein Regulating Endosomal Trafficking, Is Involved in Neuronal Death* , 2004, Journal of Biological Chemistry.

[2]  I. Dikic,et al.  Src Phosphorylation of Alix/AIP1 Modulates Its Interaction with Binding Partners and Antagonizes Its Activities* , 2005, Journal of Biological Chemistry.

[3]  G. Odorizzi The multiple personalities of Alix , 2006, Journal of Cell Science.

[4]  B. Chait,et al.  Crystal Structure of the Conserved Core of HIV-1 Nef Complexed with a Src Family SH3 Domain , 1996, Cell.

[5]  D. Cowburn,et al.  A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV‐1 Nef protein. , 1995, The EMBO journal.

[6]  R. D. Fisher,et al.  Structural and Biochemical Studies of ALIX/AIP1 and Its Role in Retrovirus Budding , 2007, Cell.

[7]  M. Maki,et al.  The ALG-2-interacting Protein Alix Associates with CHMP4b, a Human Homologue of Yeast Snf7 That Is Involved in Multivesicular Body Sorting* , 2003, Journal of Biological Chemistry.

[8]  S. Arold,et al.  The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling. , 1997, Structure.

[9]  J. Corbeil,et al.  Identification and biophysical assessment of the molecular recognition mechanisms between the human haemopoietic cell kinase Src homology domain 3 and ALG-2-interacting protein X. , 2010, The Biochemical journal.

[10]  R. Poincloux,et al.  Hematopoietic cell kinase (Hck) isoforms and phagocyte duties - from signaling and actin reorganization to migration and phagocytosis. , 2008, European journal of cell biology.

[11]  Stefan Matile,et al.  Role of LBPA and Alix in Multivesicular Liposome Formation and Endosome Organization , 2004, Science.

[12]  M. Vidal,et al.  High-throughput yeast two-hybrid assays for large-scale protein interaction mapping. , 2001, Methods.

[13]  S. Li Specificity and versatility of SH3 and other proline-recognition domains: structural basis and implications for cellular signal transduction. , 2005, The Biochemical journal.

[14]  S. Arold,et al.  RT loop flexibility enhances the specificity of Src family SH3 domains for HIV-1 Nef. , 1998, Biochemistry.

[15]  Ora Schueler-Furman,et al.  Rosetta FlexPepDock web server—high resolution modeling of peptide–protein interactions , 2011, Nucleic Acids Res..

[16]  A. Calistri,et al.  AIP1/ALIX Is a Binding Partner for HIV-1 p6 and EIAV p9 Functioning in Virus Budding , 2003, Cell.

[17]  S. Arold,et al.  Energetics of Src homology domain interactions in receptor tyrosine kinase-mediated signaling. , 2011, Methods in enzymology.

[18]  Xiaoping Zhou,et al.  Involvement of the Conserved Adaptor Protein Alix in Actin Cytoskeleton Assembly* , 2006, Journal of Biological Chemistry.

[19]  W. Cavenee,et al.  Alix/AIP1 Antagonizes Epidermal Growth Factor Receptor Downregulation by the Cbl-SETA/CIN85 Complex , 2004, Molecular and Cellular Biology.

[20]  K. Nagashima,et al.  Structural basis for viral late-domain binding to Alix , 2007, Nature Structural &Molecular Biology.

[21]  B. Blot,et al.  Alix (ALG-2-interacting Protein X), a Protein Involved in Apoptosis, Binds to Endophilins and Induces Cytoplasmic Vacuolization* , 2002, The Journal of Biological Chemistry.

[22]  S. Grzesiek,et al.  The solution structure of HIV-1 Nef reveals an unexpected fold and permits delineation of the binding surface for the SH3 domain of Hck tyrosine protein kinase , 1996, Nature Structural Biology.