Evidence map›Paper›PMID 10037798›Full record

ArticleThe Journal of cell biology1999

Matrix valency regulates integrin-mediated lymphoid adhesion via Syk kinase.

D G Stupack, E Li, S A Silletti, J A Kehler, R L Geahlen, K Hahn, G R Nemerow, D A Cheresh

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

19 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  6. Review
  7. Article
  8. Synthetic multivalent ligands as probes of signal transduction.Angewandte Chemie (International ed. in English) · 2006
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Role of alpha(v) integrins in adenovirus cell entry and gene delivery.Microbiology and molecular biology reviews : MMBR · 1999
    Review
  19. 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

8 authors at 2 institutions in 1 country.

D G StupackDepartment of Immunology, The Scripps Research Institute, La Jolla, California 92037, USA.
E Li
S A Silletti
J A Kehler
R L Geahlen
K Hahn
G R Nemerow
D A Cheresh
Purdue University West Lafayette · USScripps Research Institute · US

Funding

AV INTEGRINS AND ADENOVIRUS INTERNALIZATIONR01HL054352 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI NEMEROW, GLEN R · 1995 to 2016
$7.5M
REGULATION OF TUMOR CELL ATTACHMENT BY SURFACE ANTIGENSR01CA045726 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHERESH, DAVID A · 1988 to 2017
$7.4M
VEGF and PDGF in angiogenesis and tumor progressionR37CA050286 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHERESH, DAVID A · 1999 to 2013
$6.3M
ROLE OF CELL INTEGRINS IN ADENOVIRAL CONJUNCTIVITISR01EY011431 · NEI · SCRIPPS RESEARCH INSTITUTE, THE · PI NEMEROW, GLEN R · 1997 to 2012
$4.9M
TYROSINE PROTEIN KINASES AND LYMPHOCYTE ACTIVATIONR01CA037372 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI GEAHLEN, ROBERT L · 1985 to 2011
$3.5M
STRUCTURAL AND FUNCTIONAL STUDIES--INTEGERIN-DEPENDENTR01CA050286 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI CHERESH, DAVID A · 1989 to 2018
$1.9M
NCI NIH HHS CA 45726NCI NIH HHS CA 50286NCI NIH HHS R01 CA037372NCI NIH HHS R01 CA045726NCI NIH HHS R01 CA050286NCI NIH HHS R37 CA050286NEI NIH HHS R01 EY011431NHLBI NIH HHS HL-54352NHLBI NIH HHS R01 HL054352
6 · The paper itself

Abstract

Lymphocytes accumulate within the extracellular matrix (ECM) of tumor, wound, or inflammatory tissues. These tissues are largely comprised of polymerized adhesion proteins such as fibrin and fibronectin or their fragments. Nonactivated lymphoid cells attach preferentially to polymerized ECM proteins yet are unable to attach to monomeric forms or fragments of these proteins without previous activation. This adhesion event depends on the appropriate spacing of integrin adhesion sites. Adhesion of nonactivated lymphoid cells to polymeric ECM components results in activation of the antigen receptor-associated Syk kinase that accumulates in adhesion-promoting podosomes. In fact, activation of Syk by antigen or agonists, as well as expression of an activated Syk mutant in lymphoid cells, facilitates their adhesion to monomeric ECM proteins or their fragments. These results reveal a cooperative interaction between signals emanating from integrins and antigen receptors that can serve to regulate stable lymphoid cell adhesion and retention within a remodeling ECM.

Indexed as

Cell AdhesionCell LineEnzyme PrecursorsExtracellular MatrixHumansInflammationIntegrinsIntracellular Signaling Peptides and ProteinsLigandsLymphocytesNeoplasmsProtein-Tyrosine KinasesSignal TransductionSyk KinaseWound HealingEnzyme PrecursorsIntegrinsIntracellular Signaling Peptides and ProteinsLigandsProtein-Tyrosine KinasesSyk KinaseSYK protein, human

Identifiers

PMID10037798
PMCPMC2132930
OpenAlexW2047686369

What OpenQuestion holds

Texttitle and abstract
LicenceCC BY-NC-SA
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.