ArticleOpen biology2017
Structural and functional analysis of
Article in Open biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 20 citations in OpenAlex.
- Article
- Insights into mechanisms of ubiquitin ADP-ribosylation reversal.Biochemical Society transactions · 2024Review
- Structural characterization of macro domain-containing Thoeris antiphage defense systems.Science advances · 2024Article
- Crystal structure and biochemical activity of the macrodomain from rubella virus p150.Journal of virology · 2024Article
- Review
- Binding Adaptation of GS-441524 Diversifies Macro Domains and Downregulates SARS-CoV-2 de-MARylation Capacity.Journal of molecular biology · 2022Article
- Reversible modification of mitochondrial ADP/ATP translocases by pairedProceedings of the National Academy of Sciences of the United States of America · 2022Article
- NMR study of macro domains (MDs) from betacoronavirus: backbone resonance assignments of SARS-CoV and MERS-CoV MDs in the free and the ADPr-bound state.Biomolecular NMR assignments · 2022Article
- Article
- ADP-ribose and analogues bound to the deMARylating macrodomain from the bat coronavirus HKU4.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021Review
- Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential.Open biology · 2020Article
- (ADP-ribosyl)hydrolases: structure, function, and biology.Genes & development · 2020Review
- Deciphering the Nucleotide and RNA Binding Selectivity of the Mayaro Virus Macro Domain.Journal of molecular biology · 2019Article
- Conformational plasticity of the VEEV macro domain is important for binding of ADP-ribose.Journal of structural biology · 2019Article
- An uncharacterized FMAG_01619 protein from Fusobacterium mortiferum ATCC 9817 demonstrates that some bacterial macrodomains can also act as poly-ADP-ribosylhydrolases.Scientific reports · 2019Article
- Comparative inhibitory profile and distribution of bacterial PARPs, using Clostridioides difficile CD160 PARP as a model.Scientific reports · 2018Article
- Quantitative Determination of MAR Hydrolase Residue Specificity In Vitro by Tandem Mass Spectrometry.Methods in molecular biology (Clifton, N.J.) · 2018Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Macrodomains are ubiquitous conserved domains that bind or transform ADP-ribose (ADPr) metabolites. In humans, they are involved in transcription, X-chromosome inactivation, neurodegeneration and modulating PARP1 signalling, making them potential targets for therapeutic agents. Unfortunately, some aspects related to the substrate binding and catalysis of MacroD-like macrodomains still remain unclear, since mutation of the proposed catalytic aspartate does not completely abolish enzyme activity. Here, we present a functional and structural characterization of a macrodomain from the extremely halotolerant and alkaliphilic bacterium
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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.