Evidence map›Paper›PMID 10066831›Full record

ReviewMicrobiology and molecular biology reviews : MMBR1999

Cdc42: An essential Rho-type GTPase controlling eukaryotic cell polarity.

D I Johnson

Open access · bronzeAbstract readReview
In one paragraph

Review in Microbiology and molecular biology reviews : MMBR, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 239 papers.

0numbers the graph read from it
0cells of the map it votes in
239citing papers in PubMed
15.1field-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.

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

239 citing papers in PubMed, 547 citations in OpenAlex.

  1. Polarization as a Process: The Potential of Process Ontology for Understanding Cellular Symmetry Breaking.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
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  13. Allosteric inactivation of an engineered optogenetic GTPase.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  14. TMEM161B modulates radial glial scaffolding in neocortical development.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
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  17. Innovations in Evaluating Statin Benefit and Efficacy inInternational journal of molecular sciences · 2022
    Review
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179 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

1 author at 1 institution in 1 country.

D I JohnsonDepartment of Microbiology & Molecular Genetics and the Markey Center for Molecular Genetics, University of Vermont, Burlington, Vermont 05405, USA.dijohnso@zoo.uvm.edu
University of Vermont · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cdc42p is an essential GTPase that belongs to the Rho/Rac subfamily of Ras-like GTPases. These proteins act as molecular switches by responding to exogenous and/or endogenous signals and relaying those signals to activate downstream components of a biological pathway. The 11 current members of the Cdc42p family display between 75 and 100% amino acid identity and are functional as well as structural homologs. Cdc42p transduces signals to the actin cytoskeleton to initiate and maintain polarized gorwth and to mitogen-activated protein morphogenesis. In the budding yeast Saccharomyces cerevisiae, Cdc42p plays an important role in multiple actin-dependent morphogenetic events such as bud emergence, mating-projection formation, and pseudohyphal growth. In mammalian cells, Cdc42p regulates a variety of actin-dependent events and induces the JNK/SAPK protein kinase cascade, which leads to the activation of transcription factors within the nucleus. Cdc42p mediates these processes through interactions with a myriad of downstream effectors, whose number and regulation we are just starting to understand. In addition, Cdc42p has been implicated in a number of human diseases through interactions with its regulators and downstream effectors. While much is known about Cdc42p structure and functional interactions, little is known about the mechanism(s) by which it transduces signals within the cell. Future research should focus on this question as well as on the detailed analysis of the interactions of Cdc42p with its regulators and downstream effectors.

Indexed as

Cell PolarityActinsAmino Acid SequenceAnimalsBacterial Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell CycleCell Cycle ProteinsCytoskeletonEukaryotic CellsFluorescent Antibody TechniqueGTP-Binding ProteinsGTP PhosphohydrolasesHumansMolecular Sequence DataProtein KinasesActinsBacterial Proteinscdc42 GTP-Binding Protein, Saccharomyces cerevisiaeCell Cycle ProteinsGTP-Binding ProteinsGTP PhosphohydrolasesProtein KinasesTranscription Factors

Identifiers

PMID10066831
PMCPMC98957
OpenAlexW2102748451

What OpenQuestion holds

Texttitle and abstract
measurements read1
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.