Evidence map›Paper›PMID 11868935›Full record

ReviewImmunologic research2002

Interactions of integrins with their partner proteins in leukocyte membranes.

Howard R Petty, Randall G Worth, Robert F Todd

Abstract readReview
PubMed Publisher
In one paragraph

Review in Immunologic research, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Inside-Out Control of Fc-Receptors.Frontiers in immunology · 2019
    Review
  6. IL-3 up-regulates and activates human eosinophil CD32 and αMβ2 integrin causing degranulation.Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology · 2017
    Article
  7. Integrins in the Spotlight of Cancer.International journal of molecular sciences · 2016
    Review
  8. Article
  9. Scavenger receptors and β-glucan receptors participate in the recognition of yeasts by murine macrophages.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2012
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Exposure of acidic residues as a danger signal for recognition of fibrinogen and other macromolecules by integrin alphaXbeta2.Proceedings of the National Academy of Sciences of the United States of America · 2005
    Article
  20. 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

3 authors at 3 institutions in 1 country.

Howard R PettyDepartment of Biological Sciences, Wayne State University, Detroit, MI 48202, USA. hpetty@biology.biosci.wayne.edu
Randall G Worth
Robert F Todd
University of Michigan–Ann Arbor · USUniversity of Pennsylvania · USWayne State University · US

Funding

WATCHING TARGET CELL OXIDATION AND CYTOLYSISR01AI027409 · NIAID · WAYNE STATE UNIVERSITY · PI PETTY, HOWARD R · 1989 to 2001
$334k
NIAID NIH HHS AI27409
6 · The paper itself

Abstract

Integrins participate in many aspects of immunologic and inflammatory responses, especially those involving cell migration, adherence, and activation. Although leukocyte integrins such as complement receptor type 3 (CR3) are known to carry out certain functions without the intervention of other plasma membrane receptors, many plasma membrane proteins are now known to physically interact and functionally cooperate with integrins. Several of these interactions are highly dynamic within cell membranes; thus integrin-partner protein interactions change during certain physiological processes. This allows an extraordinary adaptability of the system to prime and promote proinflammatory signaling. Since our discovery of the CR3-FcgammaRIIIB interaction, the plasma membrane protein repertoire of beta1, beta2, and beta3 integrins has grown to include: FcgammaRIIA (CD32), uPAR (urokinase-type plasminogen activator receptor; CD87), CD14, voltage-gated K+channels (Kv1.3), integrin-associated protein (IAP), CD98, tetraspans (TM4SF), insulin receptors, and PDGFbeta receptors. In this article we will highlight certain features of this growing field of research, especially with regard to their relevance in immunology and inflammation.

Indexed as

AnimalsCell MembraneFusion Regulatory Protein-1GlycosylphosphatidylinositolsHumansIntegrinsLeukocytesLipopolysaccharide ReceptorsMacrophage-1 AntigenMembrane ProteinsModels, ImmunologicalPorinsReceptors, Cell SurfaceReceptors, IgGSignal TransductionUrokinase-Type Plasminogen ActivatorFusion Regulatory Protein-1GlycosylphosphatidylinositolsIntegrinsLipopolysaccharide ReceptorsMacrophage-1 AntigenMembrane ProteinsPorinsReceptors, Cell SurfaceReceptors, IgGUrokinase-Type Plasminogen ActivatorVoltage-Dependent Anion Channels

Identifiers

PMID11868935
OpenAlexW2003766294

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.