Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
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JAK kinase targeting in hematologic malignancies: a sinuous pathway from identification of genetic alterations towards clinical indicationsInhibition of STAT5: a therapeutic option in BCR-ABL1-driven leukemiaStructure of the STRA6 receptor for retinol uptakeMolecular basis for pseudokinase-dependent autoinhibition of JAK2 tyrosine kinase.The Thrombopoietin Receptor: Structural Basis of Traffic and Activation by Ligand, Mutations, Agonists, and Mutated Calreticulin.A Conserved Residue, Tyrosine (Y) 84, in H5N1 Influenza A Virus NS1 Regulates IFN Signaling Responses to Enhance Viral Infection.The molecular regulation of Janus kinase (JAK) activationCrystal Structure of the FERM-SH2 Module of Human Jak2.Local sequence assembly reveals a high-resolution profile of somatic structural variations in 97 cancer genomes.Uncoupling JAK2 V617F activation from cytokine-induced signalling by modulation of JH2 αC helix.The Structural Basis for Class II Cytokine Receptor Recognition by JAK1Regulation of Connexin43 Function and Expression by Tyrosine Kinase 2.Type I Interferon Signaling Is Decoupled from Specific Receptor Orientation through Lenient Requirements of the Transmembrane Domain.JAK-STAT Signaling as a Target for Inflammatory and Autoimmune Diseases: Current and Future Prospects.Defining the functional binding sites of interleukin 12 receptor β1 and interleukin 23 receptor to Janus kinases.Evolution of Cytokine Receptor Signaling.Structural basis of the specificity of USP18 toward ISG15.The Janus Kinase (JAK) FERM and SH2 Domains: Bringing Specificity to JAK-Receptor Interactions.A combined computational and structural model of the full-length human prolactin receptor.Coexistence of gain-of-function JAK2 germ line mutations with JAK2V617F in polycythemia vera.Mechanistic Insights into Regulation of JAK2 Tyrosine Kinase.Expression and Purification of JAK1 and SOCS1 for Structural and Biochemical Studies.Expression and Production of SH2 Domain Proteins.Phosphorylation of Janus kinase 1 (JAK1) by AMP-activated protein kinase (AMPK) links energy sensing to anti-inflammatory signaling.The Growth Hormone Receptor: Mechanism of Receptor Activation, Cell Signaling, and Physiological Aspects.Compound heterozygous TYK2 mutations underlie primary immunodeficiency with T-cell lymphopenia.The molecular basis of JAK/STAT inhibition by SOCS1.JAK-cytokine receptor recognition, unboxed.Are Janus Kinase Inhibitors Superior over Classic Biologic Agents in RA Patients?The psoriasis-protective TYK2 I684S variant impairs IL-12 stimulated pSTAT4 response in skin-homing CD4+ and CD8+ memory T-cells.Receptor-mediated dimerization of JAK2 FERM domains is required for JAK2 activationCytokine Receptors
P2860
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P2860
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
description
2014 nî lūn-bûn
@nan
2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@ast
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@en
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@nl
type
label
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@ast
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@en
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@nl
prefLabel
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@ast
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@en
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@nl
P2093
P2860
P356
P1476
Structural basis of recognition of interferon-α receptor by tyrosine kinase 2
@en
P2093
Christine Tam
Heidi J A Wallweber
Melissa A Starovasnik
Patrick J Lupardus
Yvonne Franke
P2860
P2888
P304
P356
10.1038/NSMB.2807
P577
2014-04-06T00:00:00Z