Evidence map›Paper›PMID 35650644›Full record

ReviewJournal of biomedical science2022

Post-translational modifications on the retinoblastoma protein.

Linbin Zhou, Danny Siu-Chun Ng, Jason C Yam, Li Jia Chen, Clement C Tham, Chi Pui Pang, Wai Kit Chu

Erratum issuedOpen access · diamondAbstract readReview
In one paragraph

Review in Journal of biomedical science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
5.7field-weighted citation impact, top 3% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 1 institution in 2 countries.

Linbin ZhouDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Danny Siu-Chun NgDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Jason C YamDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Li Jia ChenDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Clement C ThamDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Chi Pui PangDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Wai Kit ChuDepartment of Ophthalmology & Visual Sciences, The Chinese University of Hong Kong, Hong Kong, China. waikit@cuhk.edu.hk.ORCID http://orcid.org/0000-0003-2903-3247
Chinese University of Hong Kong · HK

Funding

Health and Medical Research Fund 06170896Health and Medical Research Fund 07180306Health and Medical Research Fund PR-HKCH-8
6 · The paper itself

Abstract

The retinoblastoma protein (pRb) functions as a cell cycle regulator controlling G1 to S phase transition and plays critical roles in tumour suppression. It is frequently inactivated in various tumours. The functions of pRb are tightly regulated, where post-translational modifications (PTMs) play crucial roles, including phosphorylation, ubiquitination, SUMOylation, acetylation and methylation. Most PTMs on pRb are reversible and can be detected in non-cancerous cells, playing an important role in cell cycle regulation, cell survival and differentiation. Conversely, altered PTMs on pRb can give rise to anomalies in cell proliferation and tumourigenesis. In this review, we first summarize recent findings pertinent to how individual PTMs impinge on pRb functions. As many of these PTMs on pRb were published as individual articles, we also provide insights on the coordination, either collaborations and/or competitions, of the same or different types of PTMs on pRb. Having a better understanding of how pRb is post-translationally modulated should pave the way for developing novel and specific therapeutic strategies to treat various human diseases.

Indexed as

Protein Processing, Post-TranslationalRetinoblastoma ProteinAcetylationHumansPhosphorylationUbiquitinationRetinoblastoma ProteinAcetylationMethylationPhosphorylationRetinoblastomaSUMOylationUbiquitination

Identifiers

PMID35650644
PMCPMC9161509
OpenAlexW4281677083

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.