CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.

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Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam The Sam-Sam interaction between Ship2 and the EphA2 receptor: design and analysis of peptide inhibitors.

P2860

Q27701420-41897B5A-E626-450C-9DDF-0F17E06DF313 Q47133936-7D5CAC75-215E-41BB-A7DE-EAC569F351FE

P2860

CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.

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http://www.wikidata.org/entity/Q54348199

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2014 nî lūn-bûn

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2014年の論文

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2014年学术文章

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name

CD and NMR conformational stud ...... d Loop interface of Ship2-Sam.

@en

CD and NMR conformational stud ...... d Loop interface of Ship2-Sam.

@nl

type

Item

label

CD and NMR conformational stud ...... d Loop interface of Ship2-Sam.

@en

CD and NMR conformational stud ...... d Loop interface of Ship2-Sam.

@nl

prefLabel

CD and NMR conformational stud ...... d Loop interface of Ship2-Sam.

@en

CD and NMR conformational stud ...... d Loop interface of Ship2-Sam.

@nl

P1476

CD and NMR conformational stud ...... id Loop interface of Ship2-Sam

@en

P2093

Daniela Marasco

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

Maurizio Pellecchia

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

Pasqualina L Scognamiglio

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

P2860

MeDor: a metaserver for predicting protein disorder

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

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

Characterization of DLC1-SAM equilibrium unfolding at the amino acid residue level

A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import

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

Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor

Oligomeric structure of the human EphB2 receptor SAM domain

Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA

UCSF Chimera--a visualization system for exploratory research and analysis

P304

1088-1098

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

P31

scholarly article

P356

10.1002/BIP.22512

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

P433

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

P478

101

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

P50

Marilisa Leone

Concetta Di Natale

Flavia A Mercurio

P577

2014-11-01T00:00:00Z

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

P698

24889333

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

CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.

about

P2860

P2860

CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P433

P478

P50

P577

P698