Evidence map›Paper›PMID 18795236›Full record

ReviewImmunologic research2008

Regulation of T cell integrin function by adapter proteins.

Rebecca G Baker, Gary A Koretzky

Abstract readReview
PubMed Publisher
In one paragraph

Review in Immunologic research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

7 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. The tail of integrin activation.Trends in biochemical sciences · 2011
    Review
  7. 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.

Rebecca G BakerLeonard and Madlyn Abramson Family Cancer Research Institute, University of Pennsylvania School of Medicine, Philadelphia, PA, 19104, USA.
Gary A Koretzky
University of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Integrins are cell surface heterodimers that bind adhesion molecules expressed on other cells or in the extracellular matrix. Integrin-mediated interactions are critical for T cell development in the thymus, migration of T cells in the periphery, and induction of T cell effector functions. In resting T cells, integrins are maintained in a low affinity state. Engagement of the T cell receptor or chemokine receptors increases integrin affinity, enabling integrins to bind their ligands and initiate a signaling cascade resulting in altered cell morphology and motility. Our laboratory is interested how adapter proteins, mediators of intracellular signal transduction, regulate both signals from the T cell receptor to integrins (inside-out signaling) and (outside-in) signals from integrins into the cell.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsHumansIntegrinsModels, BiologicalReceptors, Antigen, T-CellReceptors, ChemokineSignal TransductionT-LymphocytesAdaptor Proteins, Signal TransducingIntegrinsReceptors, Antigen, T-CellReceptors, Chemokine

Identifiers

PMID18795236
OpenAlexW2054151692

What OpenQuestion holds

Textmetadata
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.