Evidence map›Paper›PMID 10852130›Full record

ReviewImmunologic research2000

Focal adhesion kinase functions as a receptor-proximal signaling component required for directed cell migration.

C R Hauck, C K Klingbeil, D D Schlaepfer

Open access · greenAbstract readReview
PubMed Publisher
In one paragraph

Review in Immunologic research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
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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

3 authors at 1 institution in 1 country.

C R HauckDepartment of Immunology, The Scripps Research Institute, La Jolla, CA 92037, USA.
C K Klingbeil
D D Schlaepfer
Scripps Research Institute · US

Funding

TYROSINE PHOSPHORYLATION AND INTEGRIN SIGNALINGR29CA075240 · NCI · SCRIPPS RESEARCH INSTITUTE · PI SCHLAEPFER, DAVID D · 1997 to 2001
$259k
NCI NIH HHS R29 CA75240
6 · The paper itself

Abstract

In performing host-defense functions, cells of the immune system become activated by soluble chemokine signals and must migrate through endothelial cell or solid tissue barriers to reach sites of inflammation or infection. Regulated adhesive interactions of immune cells with endothelium, extracellular matrix components, and cells of solid organs are critical control points of the overall immune response. Both the soluble chemokine and cell adhesion receptor-mediated migration signals must converge on common intracellular targets to engage the cell migration machinery. In this article, we focus on the role of focal adhesion kinase (FAK) and its homolog Pyk2 as cytoplasmic mediators of motility events in multiple cell types. We introduce the overall domain structure of the FAK and Pyk2 nonreceptor protein tyrosine kinases (PTKs), highlight some of the signals that activate these PTKs, and detail the molecules that functionally interact and signal transduction pathways that may mediate cell migration responses. Emphasis is placed on the knowledge gained from studies using FAK-null cells as a model system to decipher the role of this PTK in promoting cell motility.

Indexed as

AnimalsCell MovementFocal Adhesion Kinase 1Focal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesHumansProtein-Tyrosine KinasesSignal TransductionFocal Adhesion Kinase 1Focal Adhesion Kinase 2Focal Adhesion Protein-Tyrosine KinasesProtein-Tyrosine KinasesPTK2 protein, human

Identifiers

PMID10852130
OpenAlexW1994404829

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.