Evidence map›Paper›PMID 35408787›Full record

ReviewInternational journal of molecular sciences2022

Recycling and Reshaping-E3 Ligases and DUBs in the Initiation of T Cell Receptor-Mediated Signaling and Response.

Clemens Cammann, Nicole Israel, Hortense Slevogt, Ulrike Seifert

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 54% 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

3 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. E3 ubiquitin ligase SKP2 limits autophagosome formation duringFrontiers in cellular and infection microbiology · 2026
    Article
  3. Review
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

4 authors at 2 institutions in 1 country.

Clemens CammannFriedrich Loeffler-Institute of Medical Microbiology-Virology, University Medicine Greifswald, 17475 Greifswald, Germany.
Nicole IsraelFriedrich Loeffler-Institute of Medical Microbiology-Virology, University Medicine Greifswald, 17475 Greifswald, Germany.
Hortense SlevogtHost Septomics Group, Centre for Innovation Competence (ZIK) Septomics, University Hospital Jena, 07745 Jena, Germany.
Ulrike SeifertFriedrich Loeffler-Institute of Medical Microbiology-Virology, University Medicine Greifswald, 17475 Greifswald, Germany.ORCID 0000-0003-1037-3487
Friedrich-Loeffler-Institut · DEMedizinische Hochschule Hannover · DE

Funding

Deutsche Forschungsgemeinschaft D539000005
6 · The paper itself

Abstract

T cell activation plays a central role in supporting and shaping the immune response. The induction of a functional adaptive immune response requires the control of signaling processes downstream of the T cell receptor (TCR). In this regard, protein phosphorylation and dephosphorylation have been extensively studied. In the past decades, further checkpoints of activation have been identified. These are E3 ligases catalyzing the transfer of ubiquitin or ubiquitin-like proteins to protein substrates, as well as specific peptidases to counteract this reaction, such as deubiquitinating enzymes (DUBs). These posttranslational modifications can critically influence protein interactions by targeting proteins for degradation by proteasomes or mediating the complex formation required for active TCR signaling. Thus, the basic aspects of T cell development and differentiation are controlled by defining, e.g., the threshold of activation in positive and negative selection in the thymus. Furthermore, an emerging role of ubiquitination in peripheral T cell tolerance has been described. Changes in the function and abundance of certain E3 ligases or DUBs involved in T cell homeostasis are associated with the development of autoimmune diseases. This review summarizes the current knowledge of E3 enzymes and their target proteins regulating T cell signaling processes and discusses new approaches for therapeutic intervention.

Indexed as

Deubiquitinating EnzymesReceptors, Antigen, T-CellSignal TransductionUbiquitin-Protein LigasesUbiquitinUbiquitinationDeubiquitinating EnzymesReceptors, Antigen, T-CellUbiquitinUbiquitin-Protein LigasesdeubiquitinationDUBsE3 ligasesSUMOT cell functionT cell receptor signalingubiquitination

Identifiers

PMID35408787
PMCPMC8998186
OpenAlexW4220954484

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.