Evidence map›Paper›PMID 9096335›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Essential role of the tyrosine kinase substrate phospholipase C-gamma1 in mammalian growth and development.

Q S Ji, G E Winnier, K D Niswender, D Horstman, R Wisdom, M A Magnuson, G Carpenter

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

90 citing papers in PubMed, 263 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Optogenetic control of PLC-γ1 activity polarizes cell motility.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. FGF-based drug discovery: advances and challenges.Nature reviews. Drug discovery · 2025
    Review
  9. Review
  10. A gain-of-function variation in PLCG1 causes a new immune dysregulation disease.The Journal of allergy and clinical immunology · 2023
    Article
  11. Review
  12. Molecular regulation of PLCβ signaling.Methods in enzymology · 2023
    Review
  13. Predictive and Therapeutic Implications of a Novel PLCγ1/SHP2-Driven Mechanism of Cetuximab Resistance in Metastatic Colorectal Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2022
    Article
  14. Article
  15. Review
  16. Article
  17. Developmental Perspectives on Arterial Fate Specification.Frontiers in cell and developmental biology · 2021
    Review
  18. Article
  19. Review
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 1 country.

Q S JiDepartment of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
G E Winnier
K D Niswender
D Horstman
R Wisdom
M A Magnuson
G Carpenter
Vanderbilt University · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
MEDICAL SCIENTIST TRAINING PROGRAMT32GM007347 · NIGMS · VANDERBILT UNIVERSITY · PI WILLIAMS, CHRISTOPHER S. · 1985 to 2023
$26.3M
Transcriptional networks of pancreas endocrine cell differentiationU19DK042502 · NIDDK · VANDERBILT UNIVERSITY · PI MAGNUSON, MARK A · 2001 to 2010
$21.5M
TRANSGENIC MICE COREP01DK042502 · NIDDK · VANDERBILT UNIVERSITY · PI MAGNUSON, MARK A · 1990 to 2000
$994k
MOLECULAR MECHANISMS OF TRANSFORMATION BY AP-1 PROTEINSR01CA064118 · NCI · VANDERBILT UNIVERSITY · PI WISDOM, RONALD M · 1995 to 2002
$777k
STUDIES OF EGF-RECEPTORS DYNAMICSP01CA043720 · NCI · VANDERBILT UNIVERSITY · PI CARPENTER, GRAHAM F · 1987 to 1997
–
NCI NIH HHS CA43720NCI NIH HHS CA64118NCI NIH HHS P30 CA068485NIDDK NIH HHS DK42502NIDDK NIH HHS P01 DK042502NIDDK NIH HHS U19 DK042502NIGMS NIH HHS T32 GM007347
6 · The paper itself

Abstract

The activation of many tyrosine kinases leads to the phosphorylation and activation of phospholipase C-gamma1 (PLC-gamma1). To examine the biological function of this protein, homologous recombination has been used to selectively disrupt the Plcg1 gene in mice. Homozygous disruption of Plcg1 results in embryonic lethality at approximately embryonic day (E) 9.0. Histological analysis indicates that Plcg1 (-/-) embryos appear normal at E 8.5 but fail to continue normal development and growth beyond E 8.5-E9.0. These results clearly demonstrate that PLC-gamma1 with, by inference, its capacity to mobilize second messenger molecules is an essential signal transducing molecule whose absence is not compensated by other signaling pathways or other genes encoding PLC isozymes.

Indexed as

AnimalsCells, CulturedEmbryonic and Fetal DevelopmentGene TargetingGenotypeHeterozygoteIsoenzymesMicePhospholipase C gammaProtein-Tyrosine KinasesSignal TransductionStem CellsSubstrate SpecificityType C PhospholipasesIsoenzymesPhospholipase C gammaProtein-Tyrosine KinasesType C Phospholipases

Identifiers

PMID9096335
PMCPMC20311
OpenAlexW2110620302

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.