Evidence map›Paper›PMID 26059070›Full record

ReviewProtein science : a publication of the Protein Society2015

Partners in crime: The role of tandem modules in gene transcription.

Rajal Sharma, Ming-Ming Zhou

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Structural features and inhibitors of bromodomains.Drug discovery today. Technologies · 2016
    Review
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.

Rajal SharmaDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, New York, 10029.
Ming-Ming ZhouDepartment of Structural and Chemical Biology, Icahn School of Medicine at Mount Sinai, New York, New York, 10029.

Funding

Teaching biomedical and pharmacological trainees to produce FAIR data for AI & ML applicationsT32GM062754 · NIGMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI SCHLESSINGER, AVNER · 2001 to 2023
$6.2M
NIGMS NIH HHS T32 GM062754
6 · The paper itself

Abstract

Histones and their modifications play an important role in the regulation of gene transcription. Numerous modifications, such as acetylation, phosphorylation, methylation, ubiquitination, and SUMOylation, have been described. These modifications almost always co-occur and thereby increase the combinatorial complexity of post-translational modification detection. The domains that recognize these histone modifications often occur in tandem in the context of larger proteins and complexes. The presence of multiple modifications can positively or negatively regulate the binding of these tandem domains, influencing downstream cellular function. Alternatively, these tandem domains can have novel functions from their independent parts. Here we summarize structural and functional information known about major tandem domains and their histone binding properties. An understanding of these interactions is key for the development of epigenetic therapy.

Indexed as

Transcription, GeneticAmino Acid MotifsAnimalsHistonesHumansProtein Processing, Post-TranslationalProtein Structure, TertiaryRegulatory Elements, TranscriptionalStructure-Activity RelationshipHistoneschromatingene transcriptionhistonepost-translational modificationsprotein modular domains

Identifiers

PMID26059070
PMCPMC4570530

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.