Evidence map›Paper›PMID 21875984›Full record

ReviewCold Spring Harbor perspectives in biology2011

The thrombospondins.

Josephine C Adams, Jack Lawler

Open access · bronzeAbstract readReview
In one paragraph

Review in Cold Spring Harbor perspectives in biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 291 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
291citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

291 citing papers in PubMed, 2 syntheses or guidelines pooled it, 468 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Trial
  4. Angiogenesis in Lung Regeneration and Aging.Arteriosclerosis, thrombosis, and vascular biology · 2026
    Review
  5. Physiological and Proteomic Responses to Chronic Stress and the Effects ofAnimals : an open access journal from MDPI · 2026
    Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Multiregional profiling revealsScience advances · 2026
    Article
  12. Sex Disparity in Systemic Sclerosis-Associated Pulmonary Fibrosis.International journal of molecular sciences · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. From a single C-mannose to multiple C-mannosyltransferases.The Journal of biological chemistry · 2026
    Review
  17. Article
  18. Article
  19. Article
  20. Review

231 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Josephine C AdamsSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom. jo.adams@bristol.ac.uk
Jack Lawler
Harvard University · USUniversity of Bristol · GB

Funding

THROMBOSPONIN-4R01HL049081 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI LAWLER, JOHN W · 1994 to 2010
$3.8M
Inhibition of angiogenesis by thrombospondin-1 (A2)R01CA130895 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI LAWLER, JOHN W · 2009 to 2012
$1.4M
British Heart FoundationNCI NIH HHS CA130895NCI NIH HHS R01 CA130895NHLBI NIH HHS HL049081NHLBI NIH HHS R01 HL049081Wellcome Trust
6 · The paper itself

Abstract

Thrombospondins are evolutionarily conserved, calcium-binding glycoproteins that undergo transient or longer-term interactions with other extracellular matrix components. They share properties with other matrix molecules, cytokines, adaptor proteins, and chaperones, modulate the organization of collagen fibrils, and bind and localize an array of growth factors or proteases. At cell surfaces, interactions with an array of receptors activate cell-dependent signaling and phenotypic outcomes. Through these dynamic, pleiotropic, and context-dependent pathways, mammalian thrombospondins contribute to wound healing and angiogenesis, vessel wall biology, connective tissue organization, and synaptogenesis. We overview the domain organization and structure of thrombospondins, key features of their evolution, and their cell biology. We discuss their roles in vivo, associations with human disease, and ongoing translational applications. In many respects, we are only beginning to appreciate the important roles of these proteins in physiology and pathology.

Indexed as

Amino Acid SequenceAnimalsCell MovementCell ProliferationDrosophilaEvolution, MolecularGenetic Predisposition to DiseaseHumansMiceMice, KnockoutMolecular Sequence DataProtein Structure, TertiarySequence AlignmentSignal TransductionThrombospondinsThrombospondins

Identifiers

PMID21875984
PMCPMC3179333
OpenAlexW4211045489

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.