Type I Interferon Signaling Is Decoupled from Specific Receptor Orientation through Lenient Requirements of the Transmembrane Domain.

about

A hot spot on interferon α/β receptor subunit 1 (IFNAR1) underpins its interaction with interferon-β and dictates signaling.The molecular basis for differential type I interferon signaling.Dynamic Modulation of Binding Affinity as a Mechanism for Regulating Interferon Signaling.

P2860

Q38712385-EC48761B-380C-4A28-9DEB-5442379F0C99 Q39176574-C87C9208-65FB-44C3-8D8E-7B3781D2E3E2 Q47565835-4D13D684-DCC9-4B61-89BB-D692B7B04559

P2860

Type I Interferon Signaling Is Decoupled from Specific Receptor Orientation through Lenient Requirements of the Transmembrane Domain.

Item

http://www.wikidata.org/entity/Q38378144

description

2015 nî lūn-bûn

@nan

2015年の論文

@ja

2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

@zh-tw

2015年论文

@wuu

2015年论文

@zh

2015年论文

@zh-cn

name

Type I Interferon Signaling Is ...... s of the Transmembrane Domain.

@en

type

Item

label

Type I Interferon Signaling Is ...... s of the Transmembrane Domain.

@en

prefLabel

Type I Interferon Signaling Is ...... s of the Transmembrane Domain.

@en

P1476

Type I Interferon Signaling Is ...... s of the Transmembrane Domain.

@en

P2093

Geeta Longjam

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

Gideon Schreiber

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

Nanaocha Sharma

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

P2860

Phosphorylated interferon-alpha receptor 1 subunit (IFNaR1) acts as a docking site for the latent form of the 113 kDa STAT2 protein

Transmembrane helix dimerization: beyond the search for sequence motifs

Receptor dimerization dynamics as a regulatory valve for plasticity of type I interferon signaling

A common model for cytokine receptor activation: combined scissor-like rotation and self-rotation of receptor dimer induced by class I cytokine

Structural Linkage between Ligand Discrimination and Receptor Activation by Type I Interferons

An antagonist peptide-EPO receptor complex suggests that receptor dimerization is not sufficient for activation

Crystallographic evidence for preformed dimers of erythropoietin receptor before ligand activation

ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids

Mechanisms of type-I- and type-II-interferon-mediated signalling

Structure and function of VEGF receptors

P304

3371-3384

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

P31

scholarly article

P356

10.1074/JBC.M115.686071

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

P407

English

P433

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

P478

291

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

P577

2015-12-17T00:00:00Z

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

P5875

287327488

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

P698

26679999

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

P921

transmembrane protein

P932

4751381

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

Type I Interferon Signaling Is Decoupled from Specific Receptor Orientation through Lenient Requirements of the Transmembrane Domain.

about

P2860

P2860

Type I Interferon Signaling Is Decoupled from Specific Receptor Orientation through Lenient Requirements of the Transmembrane Domain.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P407

P433

P478

P577

P5875

P698

P921

P932