ArticleChemical science2017
The GTPase hGBP1 converts GTP to GMP in two steps
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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.
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Who cites it
11 citing papers in PubMed, 37 citations in OpenAlex.
- Surveying Enzyme Crystal Structures Reveals the Commonality of Active-Site Solvent Accessibility and Enzymatic Water Networks.ACS omega · 2025Article
- Hybrid Quantum Mechanical/Molecular Mechanical Methods For Studying Energy Transduction in Biomolecular Machines.Annual review of biophysics · 2023Review
- Domain motions, dimerization, and membrane interactions of the murine guanylate binding protein 2.Scientific reports · 2023Article
- Short hydrogen-bond network confined on COF surfaces enables ultrahigh proton conductivity.Nature communications · 2022Article
- Human guanylate binding proteins: nanomachines orchestrating host defense.The FEBS journal · 2021Review
- Article
- Recent Advances in Understanding Biological GTP Hydrolysis through Molecular Simulation.ACS omega · 2020Review
- Large-scale, dynamin-like motions of the human guanylate binding protein 1 revealed by multi-resolution simulations.PLoS computational biology · 2019Article
- Molecular Mechanism of ATP Hydrolysis in an ABC Transporter.ACS central science · 2018Article
- Simulating Protein Mediated Hydrolysis of ATP and Other Nucleoside Triphosphates by Combining QM/MM Molecular Dynamics with Advances in Metadynamics.Journal of chemical theory and computation · 2017Article
- Metal Fluorides: Tools for Structural and Computational Analysis of Phosphoryl Transfer Enzymes.Topics in current chemistry (Cham) · 2017Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
GTPases play a crucial role in the regulation of many biological processes by catalyzing the hydrolysis of GTP into GDP. The focus of this work is on the dynamin-related large GTPase human guanine nucleotide binding protein-1 (hGBP1) which is able to hydrolyze GTP even to GMP. Here, we studied the largely unknown mechanisms of both GTP and GDP hydrolysis steps utilizing accelerated
Identifiers
What OpenQuestion holds
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.