Evidence map›Paper›PMID 21513984›Full record

ArticleMolecular immunology2011

Fyn binds to and phosphorylates T cell immunoglobulin and mucin domain-1 (Tim-1).

Miranda L Curtiss, Bruce S Hostager, Elizabeth Stepniak, Melody Singh, Natalie Manhica, Judit Knisz, Geri Traver, Paul D Rennert, John D Colgan, Paul B Rothman

Open access · greenAbstract read
In one paragraph

Article in Molecular immunology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. G protein αAmerican journal of physiology. Renal physiology · 2016
    Article
  7. Article
  8. Review
  9. Immune Regulation and Antitumor Effect of TIM-1.Journal of immunology research · 2016
    Review
  10. Review
  11. Article
  12. Article
  13. 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

10 authors at 2 institutions in 1 country.

Miranda L CurtissDepartment of Internal Medicine, University of Iowa Carver College of Medicine. 200 Hawkins Drive, Iowa City, IA 52242, USA. miranda-curtiss@uiowa.edu
Bruce S Hostager
Elizabeth Stepniak
Melody Singh
Natalie Manhica
Judit Knisz
Geri Traver
Paul D Rennert
John D Colgan
Paul B Rothman
University of Iowa · USBiogen (United States) · US

Funding

Multidisciplinary Lung Research Career Development ProgramT32HL007638 · NHLBI · UNIVERSITY OF IOWA · PI WELSH, MICHAEL J., ZABNER, JOSEPH · 1986 to 2020
$16.9M
MEDICAL SCIENTIST TRAINING PROGRAMT32GM007337 · NIGMS · UNIVERSITY OF IOWA · PI GEYER, PAMELA K., LENTZ, STEVEN R · 1985 to 2020
$15.9M
IL-4 Signal TransductionR01AI054821 · NIAID · UNIVERSITY OF IOWA · PI COLGAN, JOHN D · 2003 to 2013
$3.6M
Regulation of Atopic Immune Responses by the Prolyl lsomerase Cyclophillin AR01AI067489 · NIAID · UNIVERSITY OF IOWA · PI COLGAN, JOHN D · 2006 to 2010
$1.8M
Role of SOCS-1 in Regulation of IgER01AI077516 · NIAID · UNIVERSITY OF IOWA · PI ROTHMAN, PAUL B · 2009 to 2010
$750k
Role of the developmental regulator Gon4-like in B lymphopoiesisR56AI093737 · NIAID · UNIVERSITY OF IOWA · PI COLGAN, JOHN D · 2011 to 2011
$378k
NHLBI NIH HHS T32 HL07638NIAID NIH HHS R01 AI054821NIAID NIH HHS R01 AI067489NIAID NIH HHS R01 AI077516NIAID NIH HHS R56 AI093737NIGMS NIH HHS T32 GM007337
6 · The paper itself

Abstract

The gene encoding T cell immunoglobulin and mucin domain-1 (Tim-1) is linked to atopy and asthma susceptibility in mice and humans. Tim-1 is a transmembrane protein expressed on activated lymphocytes and appears to have a role as a co-stimulatory receptor in T cells. The protein has not been shown to have enzymatic activity but contains a site within its cytoplasmic tail predicted to be a target for tyrosine kinases. Here, we show that Tim-1 can associate with the kinase Fyn, a member of the Src family of tyrosine kinases. This association does not require Fyn's kinase activity and is independent of the phosphorylation of a conserved tyrosine present within the cytoplasmic tail of Tim-1. Fyn is necessary for phosphorylation of this tyrosine in Tim-1 and the phosphorylation of Tim-1 varies with the levels of Fyn present in cells. These data suggest a role for Fyn in the signaling downstream of Tim-1.

Indexed as

AnimalsB-LymphocytesCell LineEpithelial CellsHepatitis A Virus Cellular Receptor 1HumansMembrane GlycoproteinsMiceMice, Inbred BALB CPhosphorylationProto-Oncogene Proteins c-fynReceptors, VirusRNA, Small InterferingSignal TransductionT-LymphocytesFYN protein, humanHAVCR1 protein, humanHepatitis A Virus Cellular Receptor 1Membrane GlycoproteinsProto-Oncogene Proteins c-fynReceptors, VirusRNA, Small Interfering

Identifiers

PMID21513984
PMCPMC3109159
OpenAlexW1993580683

What OpenQuestion holds

Textmetadata
LicenceTDM
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.