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Collapsing retroviruses for efficient delivery of viro-toxic cargoes.

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Full-length structure of the anti-viral and pro-tumor DNA deaminase APOBEC3B.

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Updated: Sep 30, 2025

Incorporating Target Protein Structure Flexibility and Dynamics in Computational Drug Discovery Using Ensemble-Based Docking Analysis
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The current toolbox for APOBEC drug discovery.

Michael J Grillo1, Katherine F M Jones2, Michael A Carpenter3

  • 1Department of Medicinal Chemistry, University of Minnesota, Minneapolis, MN 55455, USA.

Trends in Pharmacological Sciences
|March 11, 2022
PubMed
Summary
This summary is machine-generated.

APOBEC3 enzymes drive mutations in viral infections and cancer, leading to therapy resistance. Inhibiting these enzymes could offer a new strategy to improve drug durability by preventing resistance mutations.

Keywords:
APOBECDNA deaminase inhibitorschemical probesdrug discoveryscreening

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Mutational processes, including those driven by APOBEC3 (A3) enzymes, contribute to genome evolution, immune evasion, and therapy resistance in viral infections and cancer.
  • A3 enzymes catalyze cytosine deamination to uracil in single-stranded DNA, introducing mutations that can lead to drug resistance.

Purpose of the Study:

  • To review assays for studying APOBEC3 enzymes.
  • To evaluate the potential of these assays for small-molecule drug discovery efforts aimed at developing antimutation therapies.

Main Methods:

  • The review analyzes various assays used to study A3 enzyme activity.
  • Focus is placed on assays suitable for high-throughput screening in small-molecule drug discovery.

Main Results:

  • The arsenal of assays for studying A3 enzymes has expanded significantly.
  • Existing and novel assays show potential for identifying inhibitors of A3 enzymes.

Conclusions:

  • Chemical inhibition of A3 enzymes represents a promising antimutation therapeutic strategy.
  • Expanded assay availability can accelerate the discovery of small-molecule inhibitors to improve the durability of cancer and antiviral therapies.