Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands
about
The essential role of profilin in the assembly of actin for microspike formation.Sik (BRK) phosphorylates Sam68 in the nucleus and negatively regulates its RNA binding abilityThe tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted by the viral vif proteinA proline to glycine mutation in the Lck SH3-domain affects conformational sampling and increases ligand binding affinityRegulation of FynT function by dual domain docking on PAG/CbpNovel Src homology 3 domain-binding motifs identified from proteomic screen of a Pro-rich regionAssociation of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cellsIdentification of a novel polyproline recognition site in the cytoskeletal associated protein, proline serine threonine phosphatase interacting proteinStructural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinityDeciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction siteA mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptorsPSTPIP: a tyrosine phosphorylated cleavage furrow-associated protein that is a substrate for a PEST tyrosine phosphataseDiverse recognition of non-PxxP peptide ligands by the SH3 domains from p67(phox), Grb2 and Pex13p.Crystallographic structure of the SH3 domain of the human c-Yes tyrosine kinase: loop flexibility and amyloid aggregationIntertwined dimeric structure for the SH3 domain of the c-Src tyrosine kinase induced by polyethylene glycol bindingDirected Evolution Reveals the Binding Motif Preference of the LC8/DYNLL Hub Protein and Predicts Large Numbers of Novel Binders in the Human ProteomeAtomic resolution structures of the c-Src SH3 domain in complex with two high-affinity peptides from classes I and IIThree-dimensional solution structure of the complex of alpha-bungarotoxin with a library-derived peptideArginine methylation inhibits the binding of proline-rich ligands to Src homology 3, but not WW, domainsbeta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosisInteraction of guanylyl cyclase C with SH3 domain of Src tyrosine kinase. Yet another mechanism for desensitizationUCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction blocking drugQM, a putative tumor suppressor, regulates proto-oncogene c-yesSH3 domain-dependent interactions of endophilin with amphiphysinSequence requirements for association of protein-tyrosine phosphatase PEP with the Src homology 3 domain of inhibitory tyrosine protein kinase p50(csk)Competing modes of self-association in the regulatory domains of Bruton's tyrosine kinase: intramolecular contact versus asymmetric homodimerizationQuantifying intramolecular binding in multivalent interactions: a structure-based synergistic study on Grb2-Sos1 complexEndocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's diseaseSH3 domains: modules of protein-protein interactions.Inhibition of N1-Src kinase by a specific SH3 peptide ligand reveals a role for N1-Src in neurite elongation by L1-CAM.The role of water molecules in the binding of class I and II peptides to the SH3 domain of the Fyn tyrosine kinaseDirected Evolution of a Highly Specific FN3 Monobody to the SH3 Domain of Human Lyn Tyrosine Kinase.Identification of Dual Natural Inhibitors for Chronic Myeloid Leukemia by Virtual Screening, Molecular Dynamics Simulation and ADMET Analysis.The N2-Src neuronal splice variant of C-Src has altered SH3 domain ligand specificity and a higher constitutive activity than N1-Src.Electrostatic effects in the folding of the SH3 domain of the c-Src tyrosine kinase: pH-dependence in 3D-domain swapping and amyloid formationDifferential sensitivity of Src-family kinases to activation by SH3 domain displacement.Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.Identification of polyproline II regions derived from the proline-rich nuclear receptor coactivators PNRC and PNRC2: new insights for ERα coactivator interactions.A graph kernel approach for alignment-free domain-peptide interaction prediction with an application to human SH3 domainsMetallofullerenol Gd@C₈₂(OH)₂₂ distracts the proline-rich-motif from putative binding on the SH3 domain.
P2860
Q22008023-75B5D264-CCA7-4FCB-8FF9-41D375EEB064Q22254678-5481B548-A2E0-4F49-B007-C6A91A8E504BQ24291013-DBAB7926-0701-4413-A493-42A6C6270240Q24300837-06D31E15-E2B2-48F2-A1AA-C107085426E2Q24302122-0579A08A-F6B0-4125-8133-516E524B6A51Q24304310-DD56D7E1-A5EE-451E-BAA1-E4AF48D8B579Q24315982-4173716F-3DDF-4C77-A1A3-E528856B457EQ24318588-ED12EED2-C3B6-495D-A3C1-698CE909AC77Q24322616-38AD3059-C055-4F74-BF4B-1A91F623D524Q24337409-EB3602A1-D739-40A7-80CC-710807E5EBFAQ24544391-6FF4FC34-3FD7-45D6-A9CC-29A312B11191Q24679587-1DD87431-54E5-41FB-91FD-C3EFB4DF6409Q27639477-6A8D9CAB-F06D-4388-A947-A0EEB68EDFA7Q27644377-57B2AC98-CA4D-4B26-9D5E-17640B8587AAQ27653621-AFAFA894-3B99-4A84-B189-EB44895636B5Q27667635-71322EE3-A3BF-4FF8-ABEB-609BB481F2F3Q27684520-C97CA642-F95F-48AA-8FE1-83EEF805C021Q27738777-68AE5E13-9973-42E4-B319-601C6CC1622AQ28140712-6D40040D-F1B4-4915-B2B5-B3D70B75C437Q28141212-63FC1BC5-0ADA-4C41-B51A-269645881C3CQ28185390-338D330C-7BF8-44F7-9054-8D0E29B89E4CQ28215101-5F91599C-55F8-4BFC-8E24-1FBAD13B2F01Q28215778-3ED609C9-0524-4BD6-952E-758BFEEC9465Q28250171-D9C9D25A-DA1F-46E5-9663-4639D5CE0BE4Q28270491-FC6B3B2B-3862-4BBD-8A0A-8B1A4AE2F32CQ28366182-AD31F83C-CC4E-48C1-A060-2C4B9C25123EQ28477483-5F69090A-29A5-4260-9E9F-1B4F906D6DC5Q29048183-3C6F62AA-CC6A-428D-932D-644ED54F054FQ30008731-D5C71589-4485-40A6-9773-7A56631A61D9Q30008772-F0C0B861-9FE0-4991-837C-DDA8216BBF50Q30008867-EC300397-1789-4E40-94C5-DFC336990F9CQ30009044-748F09DA-824C-4910-841D-A099B25C8DC8Q30009113-CB56336A-0CFF-4A4D-85F6-327B16B3D9DEQ30009160-3C6F2572-00EB-4CB6-BB15-8A1C40091767Q30009257-7EB9751A-02C6-4990-8A71-63D42334E426Q30009328-68FC1B10-5CB0-4E2B-B625-D557CF24458BQ30009332-64E43121-DE38-42B8-ADEE-2D3358B88A22Q30009591-11776DAC-6E0D-4F73-9C7C-790226AC839DQ30009822-F2F7478B-B562-44D8-AC1A-72B5CA2DB2C3Q30009919-37126C32-CB06-4C0C-AB5E-E085E3797795
P2860
Specific interactions outside the proline-rich core of two classes of Src homology 3 ligands
description
1995 nî lūn-bûn
@nan
1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Specific interactions outside ...... sses of Src homology 3 ligands
@ast
Specific interactions outside ...... sses of Src homology 3 ligands
@en
Specific interactions outside ...... sses of Src homology 3 ligands
@nl
type
label
Specific interactions outside ...... sses of Src homology 3 ligands
@ast
Specific interactions outside ...... sses of Src homology 3 ligands
@en
Specific interactions outside ...... sses of Src homology 3 ligands
@nl
prefLabel
Specific interactions outside ...... sses of Src homology 3 ligands
@ast
Specific interactions outside ...... sses of Src homology 3 ligands
@en
Specific interactions outside ...... sses of Src homology 3 ligands
@nl
P2093
P2860
P356
P1476
Specific interactions outside ...... sses of Src homology 3 ligands
@en
P2093
C Kasahara
R J Rickles
S L Schreiber
P2860
P304
P356
10.1073/PNAS.92.26.12408
P407
P577
1995-12-19T00:00:00Z