Evidence map›Paper›PMID 28337317›Full record

ArticleACS medicinal chemistry letters2017

Structural Requirements of HDAC Inhibitors: SAHA Analogues Modified at the C2 Position Display HDAC6/8 Selectivity.

Ahmed T Negmeldin, Geetha Padige, Anton V Bieliauskas, Mary Kay H Pflum

Open access · greenAbstract read
In one paragraph

Article in ACS medicinal chemistry letters, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

14 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Review
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  4. Review
  5. Review
  6. Phosphorus containing analogues of SAHA as inhibitors of HDACs.Journal of enzyme inhibition and medicinal chemistry · 2022
    Article
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  8. Article
  9. Review
  10. Article
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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 at 1 institution in 1 country.

Ahmed T NegmeldinDepartment of Chemistry, Wayne State University , 5101 Cass Avenue, Detroit, Michigan 48202, United States.
Geetha PadigeDepartment of Chemistry, Wayne State University , 5101 Cass Avenue, Detroit, Michigan 48202, United States.
Anton V BieliauskasDepartment of Chemistry, Wayne State University , 5101 Cass Avenue, Detroit, Michigan 48202, United States.
Mary Kay H PflumDepartment of Chemistry, Wayne State University , 5101 Cass Avenue, Detroit, Michigan 48202, United States.
Wayne State University · US

Funding

Identification of Histone Deacetylase Substrates using Trapping MutantsR01GM121061 · NIGMS · WAYNE STATE UNIVERSITY · PI PFLUM, MARY KAY H · 2016 to 2018
$829k
NIGMS NIH HHS R01 GM121061
6 · The paper itself

Abstract

Histone deacetylase (HDAC) proteins are epigenetic regulators that deacetylate protein substrates, leading to subsequent changes in cell function. HDAC proteins are implicated in cancers, and several HDAC inhibitors have been approved by the FDA as anticancer drugs, including SAHA (suberoylanilide hydroxamic acid; Vorinostat and Zolinza). Unfortunately, SAHA inhibits most HDAC isoforms, which limits its use as a pharmacological tool and may lead to side effects in the clinic. In this work SAHA analogues substituted at the C2 position were synthesized and screened for HDAC isoform selectivity

Indexed as

HDAC6 HDAC8 selective inhibitorHDAC inhibitorHDAC isoform selectivityHistone deacetylaseVorinostat

Identifiers

PMID28337317
PMCPMC5346987
OpenAlexW2586788206

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.