The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants
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The structural biology of Toll-like receptorsStructural and Functional Analysis of a Plant Resistance Protein TIR Domain Reveals Interfaces for Self-Association, Signaling, and AutoregulationCrystal structure of Toll-like receptor adaptor MAL/TIRAP reveals the molecular basis for signal transduction and disease protectionMolecular mechanisms for the subversion of MyD88 signaling by TcpC from virulent uropathogenic Escherichia coliStructural Insights into TIR Domain Specificity of the Bridging Adaptor Mal in TLR4 SignalingStructures and interface mapping of the TIR domain-containing adaptor molecules involved in interferon signalingMechanism of Bacterial Interference with TLR4 Signaling by Brucella Toll/Interleukin-1 Receptor Domain-containing Protein TcpBSubversion of innate immune signaling through molecular mimicryIn silico approach to inhibition of signaling pathways of Toll-like receptors 2 and 4 by ST2LCrystallization, X-ray diffraction analysis and preliminary structure determination of the TIR domain from the flax resistance protein L6.TIR domain-containing adaptor SARM is a late addition to the ongoing microbe-host dialog.Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of the TIR domain from the Brucella melitensis TIR-domain-containing protein TcpB.Crystallization and preliminary X-ray diffraction analyses of the TIR domains of three TIR-NB-LRR proteins that are involved in disease resistance in Arabidopsis thalianaStructure and Function of the TIR Domain from the Grape NLR Protein RPV1.TIR-only protein RBA1 recognizes a pathogen effector to regulate cell death in Arabidopsis.Similar Structures but Different Roles - An Updated Perspective on TLR Structures.Animal NLRs provide structural insights into plant NLR function.Multiple functional self-association interfaces in plant TIR domainsThe role of TIR-NBS and TIR-X proteins in plant basal defense responses.Structure of a prokaryotic SEFIR domain reveals two novel SEFIR-SEFIR interaction modes.
P2860
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P2860
The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The crystal structure of a TIR ...... elical region unique to plants
@ast
The crystal structure of a TIR ...... elical region unique to plants
@en
The crystal structure of a TIR ...... elical region unique to plants
@nl
type
label
The crystal structure of a TIR ...... elical region unique to plants
@ast
The crystal structure of a TIR ...... elical region unique to plants
@en
The crystal structure of a TIR ...... elical region unique to plants
@nl
prefLabel
The crystal structure of a TIR ...... elical region unique to plants
@ast
The crystal structure of a TIR ...... elical region unique to plants
@en
The crystal structure of a TIR ...... elical region unique to plants
@nl
P2093
P2860
P356
P1433
P1476
The crystal structure of a TIR ...... elical region unique to plants
@en
P2093
Eugenio Santelli
Lieh Yoon Low
Siew Leong Chan
Takashi Mukasa
P2860
P304
P356
10.1002/PRO.275
P577
2010-01-01T00:00:00Z