Evidence map›Paper›PMID 42830998›Full record

ArticleBiochemistry and biophysics reports2026

Membrane-associated HDAC11: A potential new therapeutic targeting compartment in cancer cells.

Payel Das

Abstract read
In one paragraph

Article in Biochemistry and biophysics reports, 2026. 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

1 author.

Payel DasDepartment of Biochemistry & Molecular Medicine, George Washington University, Washington, D.C., 20037, USA.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Histone deacetylase 11 (HDAC11), the sole member of class IV histone deacetylases, has emerged as a novel and promising therapeutic target in cancer owing to its unique structural and enzymatic properties. Unlike other HDAC family members, HDAC11 exhibits predominant lysine defatty-acylase activity and has been implicated in tumor progression, immune regulation, and metastasis in a cancer type-dependent manner. However, the subcellular localization-specific targeting proteins for therapy have the advantage of minimized off-target and side effects. The localization of HDAC11 in cancer cells remains poorly understood. In this study, I investigated the localization of endogenous HDAC11 in breast cancer cells using biochemical subcellular fractionation. Consistent with previous reports, HDAC11 was detected in nuclear and cytoplasmic fractions. Unexpectedly, HDAC11 was also consistently detected in membrane-enriched fractions across the cell lines examined. This observation identifies a previously unrecognized membrane-associated pool of endogenous HDAC11 in cancer cells. The presence of HDAC11 within membrane fractions suggests potential non-canonical functions beyond epigenetic regulation. This finding could expand the current understanding of HDAC11 biology and provide a foundation for future studies aimed at defining its membrane-associated interactome, substrates, and therapeutic relevance.

Indexed as

Breast cancerHDAC11Membrane fractionMitochondriaSubcellular localization

Identifiers

PMID42830998
PMCPMC13634446

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.