Evidence map›Paper›PMID 20602996›Full record

ReviewCell2010

Cell signaling by receptor tyrosine kinases.

Mark A Lemmon, Joseph Schlessinger

Registry-linked trialOpen access · bronzeAbstract readReview
In one paragraph

Review in Cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT07511062 (Axatilimab Combined With Decitabine/Venetoclax for the Treatment of TP53-mutated/Deleted AML Patients), which is not on this map. Cited by 2,452 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
2,452citing papers in PubMed, 2 pooled it
196.7field-weighted citation impact, top 1% 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.

NCT07511062 phase1not yet recruitingnot on this mapstarted 2026, after this paper: background citation

Axatilimab Combined With Decitabine/Venetoclax for the Treatment of TP53-mutated/Deleted AML Patients

TypeinterventionalSponsorNorthside Hospital, Inc.Ran2026 to 2030Enrolled32ConditionsAcute Myeloid Leukemia, TP53 Gene MutationArmsDecitabine, Venetoclax, Axatilimab
3 · Its place in the literature

Who cites it

2,452 citing papers in PubMed, 2 syntheses or guidelines pooled it, 7,809 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Modulating pseudokinase conformation from the ATP-binding site.Structure (London, England : 1993) · 2026
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Panitumumab-Based EGFR Blockade in SMARCB1-Deficient Renal Medullary Carcinoma: Preclinical Basis and Prospective Clinical Activity.Clinical cancer research : an official journal of the American Association for Cancer Research · 2026
    Article

2,392 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 1 country.

Mark A LemmonDepartment of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059, USA. mlemmon@mail.med.upenn.edu <mlemmon@mail.med.upenn.edu>
Joseph Schlessinger
University of Pennsylvania · USYale University · US

Funding

Research Core: Biochemistry and histology/histomorphometryP50AR054086 · NIAMS · YALE UNIVERSITY · PI DEMAY, MARIE · 2006 to 2010
$8.5M
ERBB RECEPTOR HOMO- AND HETERO- DIMERIZATIONR01CA079992 · NCI · UNIVERSITY OF PENNSYLVANIA · PI LEMMON, MARK A · 1999 to 2013
$3.7M
Docking protein FRS2 in FGF signalingR01AR051448 · NIAMS · YALE UNIVERSITY · PI SCHLESSINGER, JOSEPH · 2004 to 2008
$1.7M
FGF RECEPTOR SIGNALING IN BONE DEVELOPMENTR01AR051886 · NIAMS · YALE UNIVERSITY · PI SCHLESSINGER, JOSEPH · 2005 to 2009
$1.7M
Mechanisms of ErbB2/HER2/Neu ActivationR01CA096768 · NCI · UNIVERSITY OF PENNSYLVANIA · PI LEMMON, MARK A. · 2002 to 2006
$1.4M
Mechanisms of invertebrate EGF receptor inhibitionR01CA125432 · NCI · UNIVERSITY OF PENNSYLVANIA · PI LEMMON, MARK A · 2007 to 2011
$1.2M
NCI NIH HHS R01 CA079992NCI NIH HHS R01-CA079992NCI NIH HHS R01 CA096768NCI NIH HHS R01-CA096768NCI NIH HHS R01 CA125432NCI NIH HHS R01-CA125432NIAMS NIH HHS P50 AR054086NIAMS NIH HHS P50-AR054086NIAMS NIH HHS R01 AR051448NIAMS NIH HHS R01-AR051448NIAMS NIH HHS R01 AR051886NIAMS NIH HHS R01-AR051886
6 · The paper itself

Abstract

Recent structural studies of receptor tyrosine kinases (RTKs) have revealed unexpected diversity in the mechanisms of their activation by growth factor ligands. Strategies for inducing dimerization by ligand binding are surprisingly diverse, as are mechanisms that couple this event to activation of the intracellular tyrosine kinase domains. As our understanding of these details becomes increasingly sophisticated, it provides an important context for therapeutically countering the effects of pathogenic RTK mutations in cancer and other diseases. Much remains to be learned, however, about the complex signaling networks downstream from RTKs and how alterations in these networks are translated into cellular responses.

Indexed as

Signal TransductionAnimalsEnzyme ActivationHumansNeoplasmsReceptor Protein-Tyrosine KinasesReceptor Protein-Tyrosine Kinases

Identifiers

PMID20602996
PMCPMC2914105
OpenAlexW2028415754

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

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.