Evidence map›Paper›PMID 25787087›Full record

ReviewBiopolymers2015

KDM1 class flavin-dependent protein lysine demethylases.

Jonathan M Burg, Jennifer E Link, Brittany S Morgan, Frederick J Heller, Amanda E Hargrove, Dewey G McCafferty

Open access · greenAbstract readReview
In one paragraph

Review in Biopolymers, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

35 citing papers in PubMed, 65 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Jonathan M BurgDepartment of Chemistry, Duke University, Durham, NC, 27708.
Jennifer E LinkDepartment of Chemistry, Duke University, Durham, NC, 27708.
Brittany S MorganDepartment of Chemistry, Duke University, Durham, NC, 27708.
Frederick J HellerDepartment of Chemistry, Duke University, Durham, NC, 27708.
Amanda E HargroveDepartment of Chemistry, Duke University, Durham, NC, 27708.
Dewey G McCaffertyDepartment of Chemistry, Duke University, Durham, NC, 27708.
Duke University · US

Funding

Pharmacological Sciences Training ProgramT32GM007105 · NIGMS · DUKE UNIVERSITY · PI KUHN, CYNTHIA M · 1985 to 2019
$9.0M
Structural Biology and Biphysics Training ProgramT32GM008487 · NIGMS · DUKE UNIVERSITY · PI OAS, TERRENCE GILBERT · 1994 to 2014
$2.9M
Mechanistic Analyses of Protein DeacetylationR01GM065539 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI MCCAFFERTY, DEWEY G · 2002 to 2006
$1.3M
NIGMS NIH HHS R01 GM065539NIGMS NIH HHS R01-GM65539NIGMS NIH HHS T32 GM007105NIGMS NIH HHS T32 GM008487NIGMS NIH HHS T32-GM 7105-39NIGMS NIH HHS T32-GM 8487-19
6 · The paper itself

Abstract

Flavin-dependent, lysine-specific protein demethylases (KDM1s) are a subfamily of amine oxidases that catalyze the selective posttranslational oxidative demethylation of methyllysine side chains within protein and peptide substrates. KDM1s participate in the widespread epigenetic regulation of both normal and disease state transcriptional programs. Their activities are central to various cellular functions, such as hematopoietic and neuronal differentiation, cancer proliferation and metastasis, and viral lytic replication and establishment of latency. Interestingly, KDM1s function as catalytic subunits within complexes with coregulatory molecules that modulate enzymatic activity of the demethylases and coordinate their access to specific substrates at distinct sites within the cell and chromatin. Although several classes of KDM1-selective small molecule inhibitors have been recently developed, these pan-active site inhibition strategies lack the ability to selectively discriminate between KDM1 activity in specific, and occasionally opposing, functional contexts within these complexes. Here we review the discovery of this class of demethylases, their structures, chemical mechanisms, and specificity. Additionally, we review inhibition of this class of enzymes as well as emerging interactions with coregulatory molecules that regulate demethylase activity in highly specific functional contexts of biological and potential therapeutic importance.

Indexed as

Protein Processing, Post-TranslationalAnimalsCell DifferentiationEnzyme InhibitorsHematopoietic Stem CellsHistone DemethylasesHumansNeoplasmsNeural Stem CellsEnzyme InhibitorsHistone DemethylasesKDM1A protein, humanEpigeneticKDM1AKDM1BLSD1LSD2

Identifiers

PMID25787087
PMCPMC4747437
OpenAlexW2104295875

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.