Evidence map›Paper›PMID 22522061›Full record

ReviewBiochimica et biophysica acta2012

Ubiquitination and phosphorylation in the regulation of NOD2 signaling and NOD2-mediated disease.

Justine T Tigno-Aranjuez, Derek W Abbott

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

34 citing papers in PubMed, 54 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Review
  5. Structure-activity relationship in NOD2 agonistic muramyl dipeptides.European journal of medicinal chemistry · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Nod2 Deficiency Augments Th17 Responses and Exacerbates Autoimmune Arthritis.Journal of immunology (Baltimore, Md. : 1950) · 2018
    Article
  14. Review
  15. Article
  16. Article
  17. NOD2 and inflammation: current insights.Journal of inflammation research · 2018
    Review
  18. Ubiquitination regulation of inflammatory responses through NF-κB pathway.American journal of translational research · 2018
    Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Justine T Tigno-AranjuezDepartment of Pathology, Case Western Reserve University, USA.
Derek W Abbott
Case Western Reserve University · US

Funding

Ubiquitination Pathways Mediating Chronic Intestinal InflammationP01DK091222 · NIDDK · CASE WESTERN RESERVE UNIVERSITY · PI COMINELLI, FABIO · 2011 to 2020
$16.5M
Innate Immune Signal Transduction Specificity in Inflammatory DiseaseR01GM086550 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI ABBOTT, DEREK W · 2009 to 2020
$3.8M
Feedback regulation of innate immune signaling at mucosal surfacesR21AI076886 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI ABBOTT, DEREK W · 2008 to 2009
$432k
The Role of NEMO Ubiquitination in EDA-IDR21AI091637 · NIAID · CASE WESTERN RESERVE UNIVERSITY · PI ABBOTT, DEREK W · 2011 to 2012
$432k
NIAID NIH HHS R21 AI076886NIAID NIH HHS R21 AI091637NIDDK NIH HHS P01 DK091222NIGMS NIH HHS R01 GM086550NIGMS NIH HHS R01 GM086550S1
6 · The paper itself

Abstract

The immune system is exquisitely balanced. It has the ability to effectively respond to and control infections while at the same time preventing inappropriate responses to self and environmental antigens. When this response goes awry, either through a failure to activate the immune response, or failure to terminate it, inflammatory pathology results. Posttranslational modifications (PTMs) such as ubiquitination and phosphorylation help ensure that the delicate balance underlying immune signal transduction is maintained. Ubiquitination and phosphorylation affect localization, activity, stability, and interactions of various components of the immune signal transduction machinery. Moreover, ubiquitination and phosphorylation are tightly linked, with one PTM affecting the other. Therefore, in order to find potential therapies for many immune-related pathologies, it is necessary to understand not only how the immune response is activated by ubiquitination and phosphorylation, but also how it is regulated by these PTMs at different stages of the response. An excellent system to study such activation and regulation is the NOD2 pathway. Dysregulation of NOD2 signaling is involved in the pathogenesis of a variety of inflammatory disorders including Crohn's disease, early onset sarcoidosis, and Blau syndrome. More recently NOD2 has been implicated in the development of autoimmune disease, allergy and asthma. This review will focus on what is currently known about how ubiquitination and phosphorylation regulate NOD2 signaling with particular emphasis on novel in vitro substrates which may serve as potential in vivo therapeutic targets for hyperactive NOD2 states. This article is part of a Special Issue entitled: Ubiquitin Drug Discovery and Diagnostics.

Indexed as

Signal TransductionUbiquitinationCrohn DiseaseGenetic Predisposition to DiseaseHumansNod2 Signaling Adaptor ProteinPhosphorylationNOD2 protein, humanNod2 Signaling Adaptor Protein

Identifiers

PMID22522061
PMCPMC3404158
OpenAlexW2009263681

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.