SH2/SH3 signaling proteins

Current Opinion in Genetics and Development

Volumn 4, Issue 1, 1994, Pages 25-30

  Schlessinger, Joseph ^a  

^a NEW YORK UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GROWTH FACTOR RECEPTOR; PHOSPHATIDYLINOSITOL; PHOSPHOLIPASE C; PHOSPHOTYROSINE; PROLINE; PROTEIN TYROSINE KINASE; SIGNAL PEPTIDE;

HYDROLYSIS; HYDROPHOBICITY; NUCLEAR MAGNETIC RESONANCE; ONCOGENE RAS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN TARGETING; PROTEIN TERTIARY STRUCTURE; REVIEW; SIGNAL TRANSDUCTION; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMAL; BINDING SITES; HUMAN; LIGANDS; MOLECULAR SEQUENCE DATA; MOLECULAR STRUCTURE; PROTEIN SORTING SIGNALS; PROTEIN-TYROSINE KINASE; RECEPTORS, GROWTH FACTOR; SIGNAL TRANSDUCTION;

EID: 0027977799     PISSN: 0959437X     EISSN: None     Source Type: Journal    
DOI: 10.1016/0959-437X(94)90087-6     Document Type: Article

References (44)

1. Growth Factor Signaling by Receptor Tyrosine Kinases
2. SH2 and SH3 Domains
3. gag-fps
4. A Novel Viral Oncogene with Structural Similarity to Phospholipase C
5. Binding of Transforming Protein, P47gag-crk, to a Broad Range of Phosphotyrosine Containing Proteins
6. Signaling through SH2 and SH3 Domains
7. SH2 Domains Recognize Specific Phosphopeptide Sequences
8. SH2 Domains Prevent Tyrosine Dephosphorylation of the EGF-Receptor: Identification of Tyr992 as the High-Affinity Binding Site for the SH2 Domains of Phospolipase Cγ
9. Identification of a Protein that Binds to the SH3 Region of Abl and is Similar to Bcr and GAP-Rho
10. Trying on a New Pair of SH2s
11. The Tyrosine Phosphorylated Carboxyl Terminus of the EGF-Receptor is a Binding Site for GAP and PLCγ
12. Identification of Two Juxtamembrane Autophosphorylation Sites in the PDGFβ-Receptor: Involvement in the Interaction with Src Family Tyrosine Kinases
13. Phosphorylation Sites in the PDGF Receptor with Different Specificities for Binding GAP and P13 Kinase in Vivo
14. A Phosphatidylinositol 3-Kinase Binds to Platelet-Derived Growth Factor Receptors Through a Specific Receptor Sequence Containing Phosphotyrosine
15. Distinct Phosphotyrosines on a Growth Factor Receptor Bind to Specific Molecules that Mediate Different Signaling Pathways
16. Two Signaling Molecules Share a Phosphotyrosine-Containing Binding Site in the PDGF Receptor
17. The 64 kDa Protein that Associates with the PDGF Receptor Subunit via Tyrosine 1009 is the SH2 Containing Phosphotyrosine Phosphatase Syp/SH-PTP2/PTP1D/SH-PTP3
18. Tyrosines 1021 and 1009 are Phosphorylation Sites in the Carboxyl Terminus of the Platelet Derived Growth Factor Receptor β Subunit and are Required for Binding of Phospholipase Cγ and a 64-kiloDalton Protein, Respectively
19. Identification of Two C-Terminal Autophosphorylation Sites in the PDGFβ-Receptor Involvement in the Interaction with Phospholipase C-γ
20. A New Function for a Phosphotyrosine Phosphatase: Linking GRB2/Sos to a Receptor Tyrosine Kinase
21. SH2 Domains Exhibit High-Affinity Binding to Tyrosine Phosphorylated Peptides Yet Also Exhibit Rapid Dissociation and Exchange
22. Interactions Between SH2 Domains and Tyrosine Phosphorylated Platelet-Derived Growth Factor beta-Receptor Sequences: Analysis of Kinetic Parameters by a Novel Biosensor-Based Approach
23. Phosphatidylinositol 3-Kinase p85 SH2 Domain Specificity Defined by Direct Phosphopeptide/SH2 Domain Binding
24. A Tyrosine Phosphorylated Carboxy-Terminal Peptide of FGF-Receptor (flg) is a Binding Site for the SH2 Domain of Phospholipase C-γ
25. Identification of Trk Binding Sites for Shc and Phosphotidylinositol 3′-Kinase and Formation of a Multimeric Signaling Complex
26. Structure of SH2 and SH3 Domains
27. lck
28. Binding of a High Affinity Phosphotyrosyl Peptide to the src SH2 Domain: Crystal Structures of the Complexed and Peptide-Free Forms
29. Crystal Structure of a Src-Homology 3 (SH3) Domain
30. Solution Structure of the SH3 Domain of Src and Identification of its Ligand Binding Site
31. Phosphatidylinositol 3-Kinase is Activated by Association with IRS-1 During Insulin Stimulation
32. Phosphoinositide 3-Kinase is Activated by Phosphopeptides that Bind to the SH2 Domains of the 85-kDa Subunit
33. Activation of the SH2 Containing Phosphotyrosine Phosphatase SH-PTP2 by Its Binding Site Phosphotyrosine 1009 on the PDGF Receptor
34. Specific Phosphopeptide Binding Regulates a Conformational Change in the PI 3-Kinase SH2 Domain Associated with Enzyme Activation
35. C. elegans Cell Signaling Gene sem-5 Encodes a Protein with SH2 and SH3 Domains
36. The SH2 and SH3 Domain Containing Protein Grb2 Links Receptor Tyrosine Kinases to Ras Signaling
37. How Receptor Tyrosine Kinases Activate Ras
38. Association of the Shc and Grb2/Sem5 SH2-Containing Proteins is Implicated in Activation of the Ras Pathway by Tyrosine Kinases
39. Function of Protein GRB2, in Linking the Insulin Receptor to ras Signaling Pathways
40. The v-Src SH3 Domain Binds to Phosphatidylinositol 3-Kinase
41. lyn, which Interact with the Effector Molecules, Phospholipase C-γ2, Microtubule-Associated Protein Kinase, GTPase-Activating Protien, and Phosphatidylinositol 3-Kinase
42. fyn Mediates Binding to Phosphatidylinositol 3-Kinase in T Cells
43. SH3 Domains Direct Cellular Localization of Signaling Molecules