The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam - Wikidata - wikimedia - TriplyDB

The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam

The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam

http://www.wikidata.org/entity/Q27657472

about

Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3 Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam ARAP3 functions in hematopoietic stem cells Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights Survey of the year 2009: applications of isothermal titration calorimetry.Biochemistry and structure of phosphoinositide phosphatases.SHIP2: Structure, Function and Inhibition.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.Influence of the R823W mutation on the interaction of the ANKS6-ANKS3: insights from molecular dynamics simulation and free energy analysis.CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.Specific Eph receptor-cytoplasmic effector signaling mediated by SAM-SAM domain interactions.

P2860

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P2860

The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam

http://www.wikidata.org/entity/Q27657472

description

2009 nî lūn-bûn

@nan

2009 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@ast

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@en

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@nl

type

label

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@ast

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@en

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@nl

prefLabel

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@ast

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@en

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@nl

P1433

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P1433

BMC Structural Biology

P1476

The Sam domain of the lipid ph ...... t with Arap3-Sam and EphA2-Sam

@en

P2093

Jason Cellitti

http://www.w3.org/2001/XMLSchema#string

P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices

ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner

Gapped BLAST and PSI-BLAST: a new generation of protein database search programs

Solution structure of the receptor tyrosine kinase EphB2 SAM domain and identification of two distinct homotypic interaction sites

Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression

The SAM domain of polyhomeotic forms a helical polymer

CNK and HYP form a discrete dimer by their SAM domains to mediate RAF kinase signaling

Regulation of enzyme localization by polymerization: polymer formation by the SAM domain of diacylglycerol kinase delta1

NMR Studies of a Heterotypic Sam−Sam Domain Association: The Interaction between the Lipid Phosphatase Ship2 and the EphA2 Receptor † , ‡

P2888

P304

59

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P31

scholarly article

P356

10.1186/1472-6807-9-59

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P433

1

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P478

9

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P50

Maurizio Pellecchia

P577

2009-09-18T00:00:00Z

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P5875

26822780

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P6179

1051861959

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19765305

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P921

structural biology

P932

2755476

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