ArticleScientific reports2020
YqfB protein from Escherichia coli: an atypical amidohydrolase active towards N
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Biology of host-dependent restriction-modification in prokaryotes.EcoSal Plus · 2025Review
- A new role for PHYHD1 and related dioxygenases: demethylation of 2'-O-methylated nucleosides.Nucleic acids research · 2025Article
- Role ofMicroorganisms · 2025Article
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- The role and mechanism of NAT10-mediated ac4C modification in tumor development and progression.MedComm · 2024Review
- RudS: bacterial desulfidase responsible for tRNA 4-thiouridine de-modification.Nucleic acids research · 2024Article
- Characterization of winged helix domain fusion endonucleases as N6-methyladenine-dependent type IV restriction systems.Frontiers in microbiology · 2024Article
- Gut microbiome-derived hydrolases-an underrated target of natural product metabolism.Frontiers in cellular and infection microbiology · 2024Review
- Cytidine deaminases catalyze the conversion ofScience advances · 2023Article
- Bacterial amidohydrolases and modified 5-fluorocytidine compounds: Novel enzyme-prodrug pairs.PloS one · 2023Article
- Comparative Analysis of Mesophilic YqfB-Type Amidohydrolases.Biomolecules · 2022Article
- Deduction and exploration of the evolution and function of vertebrate GFPT family.Genes & genomics · 2022Article
- Functionalized Protein Nanotubes Based on the Bacteriophage vB_KleM-RaK2 Tail Sheath Protein.Nanomaterials (Basel, Switzerland) · 2021Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human activating signal cointegrator homology (ASCH) domain-containing proteins are widespread and diverse but, at present, the vast majority of those proteins have no function assigned to them. This study demonstrates that the 103-amino acid Escherichia coli protein YqfB, previously identified as hypothetical, is a unique ASCH domain-containing amidohydrolase responsible for the catabolism of N
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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.