Evidence map›Paper›PMID 1312667›Full record

ArticleMolecular and cellular biology1992

A novel endothelial cell surface receptor tyrosine kinase with extracellular epidermal growth factor homology domains.

J Partanen, E Armstrong, T P Mäkelä, J Korhonen, M Sandberg, R Renkonen, S Knuutila, K Huebner, K Alitalo

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.

0numbers the graph read from it
0cells of the map it votes in
110citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

110 citing papers in PubMed, 356 citations in OpenAlex.

  1. Trial
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  12. Lung pericytes as mediators of inflammation.American journal of physiology. Lung cellular and molecular physiology · 2023
    Review
  13. Angiogenic signaling pathways and anti-angiogenic therapy for cancer.Signal transduction and targeted therapy · 2023
    Review
  14. Article
  15. Article
  16. Article
  17. [An update of understanding of the hepatic vascular system and new research strategies].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2022
    Review
  18. Review
  19. Article
  20. Article

50 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

9 authors at 3 institutions in 2 countries.

J PartanenDepartment of Virology, University of Helsinki, Finland.
E Armstrong
T P Mäkelä
J Korhonen
M Sandberg
R Renkonen
S Knuutila
K Huebner
K Alitalo
Pediatrics and Genetics · USTemple University · USUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Endothelial cell surfaces play key roles in several important physiological and pathological processes such as blood clotting, angiogenic responses, and inflammation. Here we describe the cloning and characterization of tie, a novel type of human endothelial cell surface receptor tyrosine kinase. The extracellular domain of the predicted tie protein product has an exceptional multidomain structure consisting of a cluster of three epidermal growth factor homology motifs embedded between two immunoglobulinlike loops, which are followed by three fibronectin type III repeats next to the transmembrane region. Additionally, a cDNA form lacking the first of the three epidermal growth factor homology domains was isolated, suggesting that alternative splicing creates different tie-type receptors. Cells transfected with tie cDNA expression vector produce glycosylated polypeptides of 117 kDa which are reactive to antisera raised against the tie carboxy terminus. The tie gene was located in chromosomal region 1p33 to 1p34. Expression of the tie gene appeared to be restricted in some cell lines; large amounts of tie mRNA were detected in endothelial cell lines and in some myeloid leukemia cell lines with erythroid and megakaryoblastoid characteristics. In addition, mRNA in situ studies further indicated the endothelial expression of the tie gene. The tie receptor tyrosine kinase may have evolved for multiple protein-protein interactions, possibly including cell adhesion to the vascular endothelium.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCell LineCell MembraneChromosome MappingCloning, MolecularEndothelium, VascularEpidermal Growth FactorFibronectinsGenesImmunoglobulin GMiceMolecular Sequence DataNucleic Acid HybridizationProtein ConformationEpidermal Growth FactorFibronectinsImmunoglobulin GProtein-Tyrosine KinasesReceptors, Cell SurfaceRNA, Messenger

Identifiers

PMID1312667
PMCPMC369613
OpenAlexW2161700314

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.