The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer. - Test2 - elhamkhani - TriplyDB

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

http://www.wikidata.org/entity/Q27681792

about

TRIM21: a cytosolic Fc receptor with broad antibody isotype specificity Cyclophilin A stabilizes the HIV-1 capsid through a novel non-canonical binding site.Structural insights into the TRIM family of ubiquitin E3 ligases Structural studies of postentry restriction factors reveal antiparallel dimers that enable avid binding to the HIV-1 capsid lattice Solution structure of the microtubule-targeting COS domain of MID1 The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulation Mechanism of TRIM25 Catalytic Activation in the Antiviral RIG-I Pathway.Primate TRIM5 proteins form hexagonal nets on HIV-1 capsids.Mechanism of B-box 2 domain-mediated higher-order assembly of the retroviral restriction factor TRIM5α.Closing the net on retroviruses Functional role of TRIM E3 ligase oligomerization and regulation of catalytic activity.Restriction of HIV-1 by rhesus TRIM5α is governed by alpha helices in the Linker2 region.Crystal structure of cytomegalovirus IE1 protein reveals targeting of TRIM family member PML via coiled-coil interactions.The effect of exon 7 deletion during the evolution of TRIMCyp fusion proteins on viral restriction, cytoplasmic body formation and multimerization.Crystal structure of TRIM20 C-terminal coiled-coil/B30.2 fragment: implications for the recognition of higher order oligomers Evolutionary and Functional Analysis of Old World Primate TRIM5 Reveals the Ancient Emergence of Primate Lentiviruses and Convergent Evolution Targeting a Conserved Capsid Interface RING Dimerization Links Higher-Order Assembly of TRIM5α to Synthesis of K63-Linked Polyubiquitin.A Novel Entry/Uncoating Assay Reveals the Presence of at Least Two Species of Viral Capsids During Synchronized HIV-1 Infection.The E3 Ubiquitin Ligase TRIM9 Is a Filopodia Off Switch Required for Netrin-Dependent Axon Guidance.Characterization of Recombinant Human Cytomegaloviruses Encoding IE1 Mutants L174P and 1-382 Reveals that Viral Targeting of PML Bodies Perturbs both Intrinsic and Innate Immune Responses TRIM5α-Mediated Ubiquitin Chain Conjugation Is Required for Inhibition of HIV-1 Reverse Transcription and Capsid Destabilization.A putative SUMO interacting motif in the B30.2/SPRY domain of rhesus macaque TRIM5α important for NF-κB/AP-1 signaling and HIV-1 restriction The ubiquitin ligase TRIM25 targets ERG for degradation in prostate cancer.HIV suppression by host restriction factors and viral immune evasion.Dynamic conformational changes in the rhesus TRIM5α dimer dictate the potency of HIV-1 restriction.Overlapping and distinct molecular determinants dictating the antiviral activities of TRIM56 against flaviviruses and coronavirus.Post-translational Control of Intracellular Pathogen Sensing Pathways.TRIM proteins and diseases.Ubiquitin enzymes in the regulation of immune responses.The Human CMV IE1 Protein: An Offender of PML Nuclear Bodies.The TRIMendous Role of TRIMs in Virus-Host Interactions.Structural basis for the recognition and degradation of host TRIM proteins by Salmonella effector SopA.Characterisation of assembly and ubiquitylation by the RBCC motif of Trim5α RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination.Structure and catalytic activation of the TRIM23 RING E3 ubiquitin ligase.TRIM5α SPRY/coiled-coil interactions optimize avid retroviral capsid recognition.A general model for retroviral capsid pattern recognition by TRIM5 proteins.The three-fold axis of the HIV-1 capsid lattice is the species-specific binding interface for TRIM5α.Conserved structural and functional aspects of the tripartite motif gene family point towards therapeutic applications in multiple diseases.Herpesvirus deconjugases inhibit the IFN response by promoting TRIM25 autoubiquitination and functional inactivation of the RIG-I signalosome.

P2860

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P2860

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

http://www.wikidata.org/entity/Q27681792

description

2014 nî lūn-bûn

@nan

2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի փետրվարին 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

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer

@nl

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

@ast

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

@en

type

label

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer

@nl

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

@ast

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

@en

prefLabel

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer

@nl

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

@ast

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

@en

P1433

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PNAS.1318962111

P1433

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

P1476

The tripartite motif coiled-coil is an elongated antiparallel hairpin dimer.

@en

P2093

Jacint G Sanchez

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

Jordan M Welker

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

Katarzyna Okreglicka

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

Owen Pornillos

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

Wesley I Sundquist

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

P2860

Genomic analysis of the TRIM family reveals two groups of genes with distinct evolutionary properties

Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain

The tripartite motif family identifies cell compartments.

TRIM5 is an innate immune sensor for the retrovirus capsid lattice

Unique features of TRIM5alpha among closely related human TRIM family members

Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs

Molecular basis of coiled-coil formation

Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis

Structure of the rhesus monkey TRIM5 PRYSPRY domain, the HIV capsid recognition module

BIRC7–E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer

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2494-2499

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scholarly article

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204683

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P356

10.1073/PNAS.1318962111

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P407

P433

7

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P478

111

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P50

Viswanathan Chandrasekaran

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2014-02-03T00:00:00Z

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P5875

260253938

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24550273

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P932

3932864

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