NMR Studies of a Heterotypic Sam−Sam Domain Association: The Interaction between the Lipid Phosphatase Ship2 and the EphA2 Receptor † , ‡
about
Activation of protein phosphatase 2A tumor suppressor as potential treatment of pancreatic cancer.The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-SamStructural basis of p63α SAM domain mutants involved in AEC syndromeSolution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 ReceptorCharacterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-SamA new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein.Binding and function of phosphotyrosines of the Ephrin A2 (EphA2) receptor using synthetic sterile α motif (SAM) domains.A human sterile alpha motif domain polymerizome.Eph/ephrin signaling in epidermal differentiation and diseaseNMR structure of a heterodimeric SAM:SAM complex: characterization and manipulation of EphA2 binding reveal new cellular functions of SHIP2.Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insightsMolecular simulations of a dynamic protein complex: role of salt-bridges and polar interactions in configurational transitions.SHIP2 and its involvement in various diseases.Eph-dependent cell-cell adhesion and segregation in development and cancer.EphA3 biology and cancer.SHIP2: Structure, Function and Inhibition.How does SHIP1/2 balance PtdIns(3,4)P2 and does it signal independently of its phosphatase activity?Site-to-site interdomain communication may mediate different loss-of-function mechanisms in a cancer-associated NQO1 polymorphism.Structural insights into SAM domain-mediated tankyrase oligomerization.Specificity of HCPTP variants toward EphA2 tyrosines by quantitative selected reaction monitoring.The Sam-Sam interaction between Ship2 and the EphA2 receptor: design and analysis of peptide inhibitors.Targeting EphA2-Sam and Its Interactome: Design and Evaluation of Helical Peptides Enriched in Charged Residues.The SAM domain inhibits EphA2 interactions in the plasma membrane.CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.
P2860
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P2860
NMR Studies of a Heterotypic Sam−Sam Domain Association: The Interaction between the Lipid Phosphatase Ship2 and the EphA2 Receptor † , ‡
description
2008 nî lūn-bûn
@nan
2008 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@ast
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@en
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@nl
type
label
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@ast
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@en
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@nl
prefLabel
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@ast
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@en
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@nl
P2860
P3181
P356
P1433
P1476
NMR Studies of a Heterotypic S ...... 2 and the EphA2 Receptor † , ‡
@en
P2093
Jason Cellitti
P2860
P304
P3181
P356
10.1021/BI801713F
P407
P577
2008-12-02T00:00:00Z