Unraveling the Catalytic Mechanism and Substrate Selectivity of HDAC10: A Dual-Filter Approach for Polyamine Deacetylation.

Shengyang Cai, Jingwei Weng, Igor Ying Zhang, Yichun Zhu

Abstract read

In one paragraph

Article in JACS Au, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors.

Shengyang CaiShanghai Key Laboratory of Bioactive Small Molecules, Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Fudan University Shanghai Medical College, Shanghai 200032, China.ORCID https://orcid.org/0009-0006-7341-7802

Jingwei WengFudan Research Center for Chemical Theory, Department of Chemistry, Institute of Biomedical Sciences and Multiscale Research Institute of Complex Systems, Fudan University, Shanghai 200438, China.ORCID https://orcid.org/0000-0002-4639-7600

Igor Ying ZhangFudan Research Center for Chemical Theory, Shanghai Key Laboratory of Molecular Catalysis and Innovation Materials, Collaborative Innovation Centre of Chemistry for Energy Materials, MOE Laboratory for Computational Physical Science, Department of Chemistry, Fudan University, Shanghai 200433, China.ORCID https://orcid.org/0000-0002-8703-1912

Yichun ZhuShanghai Key Laboratory of Bioactive Small Molecules, Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Fudan University Shanghai Medical College, Shanghai 200032, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The histone deacetylase (HDAC) family plays a crucial role in regulating acetylation-dependent cellular processes, with dysregulation linked to diseases ranging from cancer to neurodegeneration. HDAC10, the sole polyamine deacetylase in the HDAC family, uniquely influences pathologies such as tumor immunity, autophagy, inflammation, virus infection, silicosis,

Indexed as

deacetylation mechanismdensity functional theoryextended ONIOMhistone deacetylasesubstrate selectivity

Identifiers

PMID41001657

DOI10.1021/jacsau.5c00842

PMCPMC12458008

What OpenQuestion holds

Textmetadata

LicenceCC BY-NC-ND

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Registered trials

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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.