Fluorescent probe displacement assays reveal unique nucleic acid binding properties of human nudix enzymes

Author:

Ray Atreyei,Frick David N.ORCID

Funder

National Institutes of Health

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference49 articles.

1. The MutT proteins or “Nudix” hydrolases, a family of versatile, widely distributed, “housecleaning” enzymes;Bessman;J. Biol. Chem.,1996

2. A cryptic activity in the Nudix hydrolase superfamily;Bessman;Protein Sci.,2019

3. A comprehensive structural, biochemical and biological profiling of the human NUDIX hydrolase family;Carreras-Puigvert;Nat. Commun.,2017

4. The complex enzymology of mRNA decapping: enzymes of four classes cleave pyrophosphate bonds;Kramer;Wiley Interdiscip. Rev. RNA,2018

5. MutT protein specifically hydrolyses a potent mutagenic substrate for DNA synthesis;Maki;Nature,1992

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1. Contribution of Nudt12 enzyme to differentially methylated dinucleotides of 5’RNA cap structure;Biochimica et Biophysica Acta (BBA) - General Subjects;2023-09

2. ONE-seq: epitranscriptome and gene-specific profiling of NAD-capped RNA;Nucleic Acids Research;2022-12-07

3. Is Location Everything? Regulation of the Endothelial CCM Signaling Complex;Frontiers in Cardiovascular Medicine;2022-07-11

4. Nudix hydrolase NUDT19 regulates mitochondrial function and ATP production in murine hepatocytes;Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids;2022-06

5. Insight into the Binding and Hydrolytic Preferences of hNudt16 Based on Nucleotide Diphosphate Substrates;International Journal of Molecular Sciences;2021-10-10

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