Evidence map›Paper›PMID 32067866›Full record

ReviewBioorganic & medicinal chemistry letters2020

Structural determinants of affinity and selectivity in the binding of inhibitors to histone deacetylase 6.

Jeremy D Osko, David W Christianson

Open access · greenAbstract readReview
In one paragraph

Review in Bioorganic & medicinal chemistry letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.7field-weighted citation impact, top 9% of its field
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

19 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Intepirdine Derivatives Possessing Dual 5HT6 Antagonism / HDAC6 Inhibitory Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025
    Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Design, synthesis, biological andBiomedical reports · 2025
    Article
  10. Article
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  12. Article
  13. Article
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  15. Article
  16. Article
  17. Review
  18. Binding of inhibitors to active-site mutants of CD1, the enigmatic catalytic domain of histone deacetylase 6.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  19. Article
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

2 authors at 1 institution in 1 country.

Jeremy D OskoRoy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104-6323, United States.
David W ChristiansonRoy and Diana Vagelos Laboratories, Department of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104-6323, United States. Electronic address: chris@sas.upenn.edu.
University of Pennsylvania · US

Funding

Structure and Function of MetalloenzymesR01GM049758 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI CHRISTIANSON, DAVID W · 1994 to 2025
$7.6M
NIGMS NIH HHS R01 GM049758
6 · The paper itself

Abstract

Histone deacetylase 6 (HDAC6) is associated with multiple neurological disorders as well as aggressive cancers, making its selective inhibition highly desirable for therapeutic purposes. The basic molecular design of an effective HDAC6 inhibitor consists of a zinc-binding group, a linker, and a capping group capable of making interactions at the mouth of the active site. To date, more than 50 high-resolution X-ray crystal structures of HDAC6-inhibitor complexes have been reported, many of which reveal intermolecular interactions that contribute to isozyme affinity and selectivity. Here, we review the key features of HDAC6 inhibitor design illuminated by these structural studies.

Indexed as

AnimalsBinding SitesHistone Deacetylase 6Histone Deacetylase InhibitorsHumansModels, MolecularMolecular StructureZebrafishZebrafish ProteinsHDAC6 protein, humanHDAC6 protein, zebrafishHistone Deacetylase 6Histone Deacetylase InhibitorsZebrafish ProteinsEnzymeInhibitorX-ray crystallography

Identifiers

PMID32067866
PMCPMC7067655
OpenAlexW3006674793

What OpenQuestion holds

Textmetadata
LicenceTDM
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.