Structural Basis for Homodimerization of the Src-associated during Mitosis, 68-kDa Protein (Sam68) Qua1 Domain
about
Comprehensive analysis of interactions between the Src-associated protein in mitosis of 68 kDa and the human Src-homology 3 proteomeSAM68: Signal Transduction and RNA Metabolism in Human CancerStructural Analysis of the Quaking Homodimerization InterfaceGet5 Carboxyl-terminal Domain Is a Novel Dimerization Motif That Tethers an Extended Get4/Get5 ComplexThe N-terminus of FILIA Forms an Atypical KH Domain with a Unique Extension Involved in Interaction with RNASolution Structure of the QUA1 Dimerization Domain of pXqua, the Xenopus Ortholog of QuakingStructure-function studies of STAR family Quaking proteins bound to their in vivo RNA target sitesStructural and functional implications of the QUA2 domain on RNA recognition by GLD-1The RNA-binding protein Sam68 regulates expression and transcription function of the androgen receptor splice variant AR-V7Parameterization of solvent-protein interaction and its use on NMR protein structure determinationMechanisms of HGF/Met signaling to Brk and Sam68 in breast cancer progression.Phosphorylation of the Drosophila melanogaster RNA-binding protein HOW by MAPK/ERK enhances its dimerization and activityEvolutionary Dynamics of GLD-1-mRNA complexes in Caenorhabditis nematodes.Analysis of the interaction between host factor Sam68 and viral elements during foot-and-mouth disease virus infectionsRole of Sam68 in post-transcriptional gene regulation.Neuronal cell type-specific alternative splicing is regulated by the KH domain protein SLM1.Studying the structure and dynamics of biomolecules by using soluble paramagnetic probesAlternative splicing programs in prostate cancer.Structural investigations of the RNA-binding properties of STAR proteins.Screening protein--single stranded RNA complexes by NMR spectroscopy for structure determination.Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68.Intrinsically disordered proteins in the nucleus of human cells.Post-Translational Modifications and RNA-Binding Proteins.
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P2860
Structural Basis for Homodimerization of the Src-associated during Mitosis, 68-kDa Protein (Sam68) Qua1 Domain
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
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2010年论文
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name
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@ast
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@en
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@nl
type
label
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@ast
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@en
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@nl
prefLabel
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@ast
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@en
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@nl
P2093
P2860
P50
P356
P1476
Structural Basis for Homodimer ...... Da Protein (Sam68) Qua1 Domain
@en
P2093
Fatiha Kateb
Michelle Vincendeau
N Helge Meyer
Ruth Brack-Werner
P2860
P304
P356
10.1074/JBC.M110.126185
P407
P577
2010-09-10T00:00:00Z