Article in Nature communications, 2025. 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.
Olivier SoubiasCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.
Xiaoying JianLaboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.
Rebekah A JacksonCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.ORCID http://orcid.org/0000-0002-9195-3186
Yue ZhangCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.ORCID http://orcid.org/0000-0003-4367-4470
Eric M RosenbergLaboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA.ORCID http://orcid.org/0000-0001-9016-3839
Benjamin J HuUnit of Membrane Chemical Physics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.
Jess LiCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA.ORCID http://orcid.org/0000-0001-7708-8555
Frank HeinrichDepartment of Physics Carnegie Mellon University, Pittsburgh, PA, USA.
Alexander J SodtUnit of Membrane Chemical Physics, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD, USA.ORCID http://orcid.org/0000-0002-5570-8212
Paul A RandazzoLaboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD, USA. randazzp@mail.nih.gov.ORCID http://orcid.org/0000-0001-5349-0881
R Andrew ByrdCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Frederick, MD, USA. byrdra@nih.gov.ORCID http://orcid.org/0000-0003-3625-4232
Funding
Regulation of ADP-ribosylation factorZIABC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 2009 to 2025
$27.9M
Investigation of Protein-Protein Interactions in the ERAD Ubiquitylation PathwayZIABC011131 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, ROBERT · 2009 to 2024
$12.0M
Structural Biology of GTPase Activating ProteinsZIABC011419 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, ROBERT · 2011 to 2024
$8.4M
Molecular simulations of lipid curvature stress and its effect on transmembrane proteinsZIAHD008955 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI SODT, ALEXANDER · 2016 to 2025
$6.2M
Methods DevelopmentZIABC011132 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI BYRD, ROBERT · 2009 to 2024
$4.6M
REGULATION OF ADP-RIBOSYLATION FACTORZ01BC007365 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI RANDAZZO, PAUL A · 1996 to 2008
$3.3M
Mechanisms of Protein Self-Assembly Coupled to Membrane Mechanics in the Cell.R35GM133644 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI JOHNSON, MARGARET ELLEN · 2019 to 2023
$2.0M
Intramural NIH HHS Z01 BC007365Intramural NIH HHS ZIA BC007365Intramural NIH HHS ZIA BC011131Intramural NIH HHS ZIA BC011132Intramural NIH HHS ZIA BC011419Intramural NIH HHS ZIA HD008955NIGMS NIH HHS R35 GM133644U.S. Department of Health & Human Services | NIH | National Cancer Institute (NCI) ZIABC007365U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35GM133644
6 · The paper itself
Abstract
GTPase-activating proteins are important regulators of small GTPases; among these, ASAP1 stimulates GTP hydrolysis on Arf1 and is implicated in cancer progression. ASAP1 contains a Pleckstrin Homology (PH) domain essential for maximum Arf·GTP hydrolysis. The prevailing view of PH domains is that they regulate proteins through passive mechanisms like membrane recruitment. In sharp contrast, we show that the PH domain of ASAP1 actively contributes to Arf1 GTP hydrolysis. By combining NMR, molecular dynamics simulations, kinetic assays, and mutational analysis, we find that the PH domain binds Arf·GTP at the membrane, to establish an active state primed for GTP hydrolysis. We identify key residues on the PH domain and Arf that drive this allosteric mechanism, which mathematical modeling shows contributes as much to GTPase activation as membrane recruitment. The finding that PH domains directly modulate small GTPases has broad implications for the Ras and Rho oncoprotein families.
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.
An active allosteric mechanism in ASAP1-mediated Arf1 GTP hydrolysis redefines PH domain function. · full record | OpenQuestion