Evidence map›Paper›PMID 33202645›Full record

ReviewInternational journal of molecular sciences2020

Mammalian PRC1 Complexes: Compositional Complexity and Diverse Molecular Mechanisms.

Zhuangzhuang Geng, Zhonghua Gao

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

48 citing papers in PubMed, 71 citations in OpenAlex.

  1. Cross-species incompatibilities offer new insights into the functional consequences of satellite DNA evolution.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2026
    Review
  2. Article
  3. Review
  4. Article
  5. The Many Faces of SetDB1.Epigenomes · 2026
    Review
  6. Review
  7. Physical models reveal indirect reader protein interactions that facilitate epigenetic crosstalk.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Research square · 2025
    Article
  11. Article
  12. Review
  13. Prion-like Properties of Short Isoforms of Human Chromatin Modifier PHC3.International journal of molecular sciences · 2025
    Article
  14. Article
  15. X and Y Differences in Melanoma Survival Between the Sexes.Pigment cell & melanoma research · 2025
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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.

Zhuangzhuang GengDepartments of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, PA 17033, USA.
Zhonghua GaoDepartments of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, PA 17033, USA.
Pennsylvania State University · US

Funding

Epigenetic regulation of cell identity by PRC1 complexesR35GM133496 · NIGMS · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI GAO, ZHONGHUA · 2019 to 2023
$2.1M
NIGMS NIH HHS R35 GM133496NIGMS NIH HHS R35GM133496
6 · The paper itself

Abstract

Polycomb group (PcG) proteins function as vital epigenetic regulators in various biological processes, including pluripotency, development, and carcinogenesis. PcG proteins form multicomponent complexes, and two major types of protein complexes have been identified in mammals to date, Polycomb Repressive Complexes 1 and 2 (PRC1 and PRC2). The PRC1 complexes are composed in a hierarchical manner in which the catalytic core, RING1A/B, exclusively interacts with one of six Polycomb group RING finger (PCGF) proteins. This association with specific PCGF proteins allows for PRC1 to be subdivided into six distinct groups, each with their own unique modes of action arising from the distinct set of associated proteins. Historically, PRC1 was considered to be a transcription repressor that deposited monoubiquitylation of histone H2A at lysine 119 (H2AK119ub1) and compacted local chromatin. More recently, there is increasing evidence that demonstrates the transcription activation role of PRC1. Moreover, studies on the higher-order chromatin structure have revealed a new function for PRC1 in mediating long-range interactions. This provides a different perspective regarding both the transcription activation and repression characteristics of PRC1. This review summarizes new advancements regarding the composition of mammalian PRC1 and accompanying explanations of how diverse PRC1-associated proteins participate in distinct transcription regulation mechanisms.

Indexed as

AnimalsChromatinHistonesHumansPolycomb Repressive Complex 1Polycomb Repressive Complex 2Transcription, GeneticUbiquitinationChromatinHistonesPolycomb Repressive Complex 1Polycomb Repressive Complex 2chromatin structurePRC1transcription regulation

Identifiers

PMID33202645
PMCPMC7697839
OpenAlexW3098199698

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.