Evidence map›Paper›PMID 38740643›Full record

ArticleCellular and molecular life sciences : CMLS2024

Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP.

Srihari Shankar, Ti Weng Chew, Vishnu Priyanka Reddy Chichili, Boon Chuan Low, J Sivaraman

Abstract read
In one paragraph

Article in Cellular and molecular life sciences : CMLS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
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

1 citing paper in PubMed.

  1. 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

5 authors.

Srihari ShankarDepartment of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore.ORCID https://orcid.org/0000-0003-2540-969X
Ti Weng ChewMechanobiology Institute, National University of Singapore, Singapore, 117411, Singapore.
Vishnu Priyanka Reddy ChichiliDepartment of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore.
Boon Chuan LowDepartment of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore. dbslowbc@nus.edu.sg.ORCID https://orcid.org/0000-0003-0756-096X
J SivaramanDepartment of Biological Sciences, National University of Singapore, 14 Science Drive 4, Singapore, 117543, Singapore. dbsjayar@nus.edu.sg.ORCID http://orcid.org/0000-0001-9781-5326

Funding

Ministry of Education - Singapore A-8000477-00-00Ministry of Education - Singapore AcRF Tier 3 Grant MOE 2016-T3-1-002Ministry of Education - Singapore R154-000-C07-114
6 · The paper itself

Abstract

p50RhoGAP is a key protein that interacts with and downregulates the small GTPase RhoA. p50RhoGAP is a multifunctional protein containing the BNIP-2 and Cdc42GAP Homology (BCH) domain that facilitates protein-protein interactions and lipid binding and the GAP domain that regulates active RhoA population. We recently solved the structure of the BCH domain from yeast p50RhoGAP (

Indexed as

GTPase-Activating ProteinsProlineSchizosaccharomyces pombe ProteinsAmino Acid SequenceConserved SequenceHumansModels, MolecularProtein BindingProtein DomainsrhoA GTP-Binding ProteinSchizosaccharomycesTyrosineARHGAP1 protein, humanGTPase-Activating ProteinsProlinerhoA GTP-Binding ProteinSchizosaccharomyces pombe ProteinsTyrosineBCH domainGTPase-activating proteinRhoScaffoldStructure

Identifiers

PMID38740643
PMCPMC11090974

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.