IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly - Wikidata - wikimedia - TriplyDB

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

http://www.wikidata.org/entity/Q28247501

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Recent Progress in the Molecular Recognition and Therapeutic Importance of Interleukin-1 Receptor-Associated Kinase 4 Identifying three-dimensional structures of autophosphorylation complexes in crystals of protein kinases SMOCs: supramolecular organizing centres that control innate immunity.Structural biology of innate immunity.Pellino-1 Positively Regulates Toll-like Receptor (TLR) 2 and TLR4 Signaling and Is Suppressed upon Induction of Endotoxin Tolerance.Pellino-3 promotes endotoxin tolerance and acts as a negative regulator of TLR2 and TLR4 signaling.Structures of the inactive and active states of RIP2 kinase inform on the mechanism of activation.Selective interleukin-1 receptor-associated kinase 4 inhibitors for the treatment of autoimmune disorders and lymphoid malignancy.The Structure and Dynamics of Higher-Order Assemblies: Amyloids, Signalosomes, and Granules.The N-terminal loop of IRAK-4 death domain regulates ordered assembly of the Myddosome signalling scaffold.E3 ubiquitin ligases Pellinos as regulators of pattern recognition receptor signaling and immune responses.The mechanism of activation of IRAK1 and IRAK4 by interleukin-1 and Toll-like receptor agonists.Toll-like receptors targeting technology for the treatment of lymphoma.Structural basis of TIR-domain-assembly formation in MAL- and MyD88-dependent TLR4 signaling.IRAKM-Mincle axis links cell death to inflammation: Pathophysiological implications for chronic alcoholic liver disease.The family of the interleukin-1 receptors.Cellular FLIP long isoform (cFLIPL)-IKKα interactions inhibit IRF7 activation, representing a new cellular strategy to inhibit IFNα expression.Crystal structure of human IRAK1.Generation of Innate Immune Reporter Cells Using Retroviral Transduction.Biochemical Isolation of the Myddosome from Murine Macrophages.Activation of the Innate Immune Receptors: Guardians of the Micro Galaxy : Activation and Functions of the Innate Immune Receptors.Autophosphorylation Affects Substrate-Binding Affinity of Tobacco Ca2+-Dependent Protein Kinase1.TLR4 Signaling Pathway Modulators as Potential Therapeutics in Inflammation and Sepsis.IRAK4 activity controls immune responses to intracellular bacteria Listeria monocytogenes and Mycobacterium smegmatis.Mechanism of dysfunction of human variants of the IRAK4 kinase and a role for its kinase activity in interleukin-1 receptor signaling Interleukin-1 receptor-associated kinase 4 (IRAK4) plays a dual role in myddosome formation and Toll-like receptor signaling

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P2860

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

http://www.wikidata.org/entity/Q28247501

description

2014 nî lūn-bûn

@nan

2014 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի սեպտեմբերին 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

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

@ast

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

@en

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

@nl

type

label

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

@ast

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

@en

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

@nl

prefLabel

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

@ast

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

@en

IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

@nl

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J.MOLCEL.2014.08.006

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IRAK4 dimerization and trans-autophosphorylation are induced by Myddosome assembly

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David E Shaw

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

Hao Wu

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

Hao Zhou

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

Qiubai Li

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

Ryan Ferrao

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

Xiaoxia Li

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

Yibing Shan

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

P2860

A dimeric kinase assembly underlying autophosphorylation in the p21 activated kinases

IRAK-4: a novel member of the IRAK family with the properties of an IRAK-kinase

Pyogenic bacterial infections in humans with MyD88 deficiency

Helical assembly in the death domain (DD) superfamily

Structure and autoregulation of the insulin-like growth factor 1 receptor kinase

Crystal structures of IRAK-4 kinase in complex with inhibitors: a serine/threonine kinase with tyrosine as a gatekeeper

Cutting Edge: IL-1 receptor-associated kinase 4 structures reveal novel features and multiple conformations

Small-molecule inhibition and activation-loop trans-phosphorylation of the IGF1 receptor

Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase

Helical assembly in the MyD88–IRAK4–IRAK2 complex in TLR/IL-1R signalling

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10.1016/J.MOLCEL.2014.08.006

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