Structure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers. - Test2 - elhamkhani - TriplyDB

Structure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers.

Structure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers.

http://www.wikidata.org/entity/Q37571141

about

Structure of Full-Length Human PDGFRβ Bound to Its Activating Ligand PDGF-B as Determined by Negative-Stain Electron Microscopy.MET-activating Residues in the B-repeat of the Listeria monocytogenes Invasion Protein InlB.Viral miniproteins The strength and cooperativity of KIT ectodomain contacts determine normal ligand-dependent stimulation or oncogenic activation in cancer.Recombinant expression in E. coli of human FGFR2 with its transmembrane and extracellular domains.A selective NMR probe to monitor the conformational transition from inactive to active kinase.Two variants in the KIT gene as candidate causative mutations for a dominant white and a white spotting phenotype in the donkey.

P2860

Q30380246-8634BE0C-26A6-425D-9913-044E8081EC19 Q30394618-633F1592-38B2-418E-81A8-9F15EF49C1CE Q35151120-FA6CCD51-5BA1-4A8E-912F-A43A6A5BF9CD Q38600953-A69525BF-B0CA-4FAD-9B4D-FF8DE9D9F4E4 Q40983650-10E92D84-8AF7-4C0C-ADD1-4C410CF322D7 Q43113518-648D286A-8814-4710-B7F7-369BF64A99ED Q54281262-7E74B427-0D55-4352-BF9B-FD3B0C909362

P2860

Structure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers.

http://www.wikidata.org/entity/Q37571141

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 21 January 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Structure, domain organization ...... tor-induced intact KIT dimers.

@en

Structure, domain organization ...... tor-induced intact KIT dimers.

@nl

type

label

Structure, domain organization ...... tor-induced intact KIT dimers.

@en

Structure, domain organization ...... tor-induced intact KIT dimers.

@nl

prefLabel

Structure, domain organization ...... tor-induced intact KIT dimers.

@en

Structure, domain organization ...... tor-induced intact KIT dimers.

@nl

P1433

Q37571141-72E56DE8-2B4A-4838-A633-35A9B699BF24

P1476

Q37571141-56AEC88D-7C43-462D-9838-3183F49996A4

P2093

Q37571141-118C21B9-CA8E-4744-8E97-0AF0C254650E

Q37571141-42D65A44-1E3F-4CDC-AE5F-83EA47EC7F13

Q37571141-D5E933AD-0125-417F-A483-63CFB660323C

Q37571141-DE1DA036-C285-42A1-A167-06C97E5CD3BC

Q37571141-FAD50E06-B016-4B42-9C2C-DB524BDDAE08

P2860

Q37571141-02C7F5D8-183A-4536-ACAF-FCC62556676B

Q37571141-0E04E1A6-3CD0-4513-9EBA-89B3E41D1240

Q37571141-136C5B61-B651-4332-8041-9F7B87635271

Q37571141-1BE7848D-6EE7-4AAA-A694-AB4D1B2E1A70

Q37571141-1D2BBBE5-6C2C-4A86-BB07-EAE6C01CE573

Q37571141-22AA1C27-9E8C-4839-B1CB-713032E95537

Q37571141-25DCEA14-2D5B-4D44-A3B6-EE07C158A4EA

Q37571141-33151FCC-E9D4-42DC-A994-C553BB137E27

Q37571141-4B57F60A-02F7-41E7-B8A2-AA076369DBB3

Q37571141-53FB1B4A-64DB-48C8-92AB-06E5722ACEAA

P304

Q37571141-75075DAD-D247-4AF9-A6DA-02CA70A6B017

P31

Q37571141-E4935452-A771-4B9C-BA25-DCCBB9E8476B

P356

Q37571141-B0CAB939-0E08-441A-B608-4DF4BBAC88F1

P407

Q37571141-127E289B-097C-4D75-8EC1-7E4056C14489

P433

Q37571141-02E5FC3A-7297-4999-AC8A-B6FC49AC4863

P478

Q37571141-3E1A43F5-72FD-4125-B43C-1B529CF173BB

P50

Q37571141-BED07E4A-1543-4168-93C8-EBA3EC17D43A

P577

Q37571141-0564A2DB-48B1-428E-A81B-9FE2C0A5D59B

P5875

Q37571141-6F522B64-1ABF-4F9D-9A23-99F777B84366

P698

Q37571141-BDC76D9F-F4A0-4F6A-ACFF-2E881283F6C1

P932

Q37571141-E66A2443-BB78-49C6-A204-73205CD6182D

P356

PNAS.1323254111

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Structure, domain organization ...... tor-induced intact KIT dimers.

@en

P2093

Francisco Tomé

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

Franziska Bleichert

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

Irit Lax

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

Vinzenz M Unger

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

Yarden Opatowsky

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

P2860

An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor

Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells

Structural basis for activation of the receptor tyrosine kinase KIT by stem cell factor

Structure of the active core of human stem cell factor and analysis of binding to its receptor Kit

Crystal structure of human stem cell factor: implication for stem cell factor receptor dimerization and activation

Structure of a c-kit product complex reveals the basis for kinase transactivation

Structural basis for stem cell factor–KIT signaling and activation of class III receptor tyrosine kinases

Direct contacts between extracellular membrane-proximal domains are required for VEGF receptor activation and cell signaling

Cell signaling by receptor tyrosine kinases

A new generation of the IMAGIC image processing system

P304

1772-1777

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

P31

scholarly article

P356

10.1073/PNAS.1323254111

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

P407

P433

5

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

P478

111

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

P50

Joseph Schlessinger

P577

2014-01-21T00:00:00Z

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

P5875

259848083

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

P698

24449920

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

P932

3918759

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