(Q36666117)

English

Ubiquitin regulates caspase recruitment domain-mediated signaling by nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2.

scientific article published on 8 January 2013

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21 February 2020

Ubiquitin regulates caspase recruitment domain-mediated signaling by nucleotide-binding oligomerization domain-containing proteins NOD1 and NOD2 (English)

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21 February 2020

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21 February 2020

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21 February 2020

Robert C. Piper

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21 February 2020

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S Ramaswamy

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21 February 2020

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8 January 2013

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21 February 2020

Journal of Biological Chemistry

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21 February 2020

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21 February 2020

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21 February 2020

6890-6902

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21 February 2020

The role of ubiquitylation in immune defence and pathogen evasion

1 reference

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1 reference

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30 September 2017

Ubiquitin makes its mark on immune regulation

1 reference

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Expanding role of ubiquitination in NF-κB signaling

1 reference

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WD40 Repeat Propellers Define a Ubiquitin-Binding Domain that Regulates Turnover of F Box Proteins

1 reference

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Reconstitution of the RIG-I pathway reveals a signaling role of unanchored polyubiquitin chains in innate immunity

1 reference

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1 reference

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30 September 2017

NOD2 stimulation induces autophagy in dendritic cells influencing bacterial handling and antigen presentation

1 reference

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30 September 2017

Nod1 and Nod2 direct autophagy by recruiting ATG16L1 to the plasma membrane at the site of bacterial entry

1 reference

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30 September 2017

Ubiquitin-binding domains - from structures to functions

1 reference

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30 September 2017

Direct activation of protein kinases by unanchored polyubiquitin chains

1 reference

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30 September 2017

XIAP mediates NOD signaling via interaction with RIP2

1 reference

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30 September 2017

ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways

1 reference

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Approaching the asymptote: 20 years later

1 reference

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30 September 2017

Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2.

1 reference

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30 September 2017

Evaluation of Nod-like receptor (NLR) effector domain interactions

1 reference

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30 September 2017

Ubiquitylation in innate and adaptive immunity.

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3591598

30 September 2017

Probabilistic interaction network of evidence algorithm and its application to complete labeling of peak lists from protein NMR spectroscopy

1 reference

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30 September 2017

Retinoic acid-induced gene-1 (RIG-I) associates with the actin cytoskeleton via caspase activation and recruitment domain-dependent interactions

1 reference

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30 September 2017

Roles of RIG-I N-terminal tandem CARD and splice variant in TRIM25-mediated antiviral signal transduction

1 reference

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30 September 2017

The Atg16L complex specifies the site of LC3 lipidation for membrane biogenesis in autophagy

1 reference

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30 September 2017

I-TASSER server for protein 3D structure prediction

1 reference

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30 September 2017

Monomer/dimer transition of the caspase-recruitment domain of human Nod1

1 reference

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30 September 2017

A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation

1 reference

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Intracellular NOD-like receptors in host defense and disease

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The Atg5 Atg12 conjugate associates with innate antiviral immune responses

1 reference

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The NOD2-RICK complex signals from the plasma membrane.

1 reference

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Crystal structure of the Nod1 caspase activation and recruitment domain

1 reference

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Solution structure of NOD1 CARD and mutational analysis of its interaction with the CARD of downstream kinase RICK

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The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO

1 reference

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An essential role for NOD1 in host recognition of bacterial peptidoglycan containing diaminopimelic acid

1 reference

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Nod1 detects a unique muropeptide from gram-negative bacterial peptidoglycan

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1 reference

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Nod1, a CARD protein, enhances pro-interleukin-1beta processing through the interaction with pro-caspase-1

1 reference

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1 reference

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1 reference

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NLR functions beyond pathogen recognition

1 reference

https://pubmed.ncbi.nlm.nih.gov/23300079

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1074/JBC.M112.413781

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23300079%20AND%20SRC:MED&resulttype=core&format=json

21 February 2020

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23300079%20AND%20SRC:MED&resulttype=core&format=json

21 February 2020

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:23300079%20AND%20SRC:MED&resulttype=core&format=json

21 February 2020

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