Evidence map›Paper›PMID 42018283›Full record

ReviewEssays in biochemistry2025

The Ubiquitin Script: writing protein fates in chains.

Devanshi Gupta, Subbareddy Maddika

Abstract readReview
In one paragraph

Review in Essays in biochemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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.

Devanshi GuptaLaboratory of Cell Death & Cell Survival, Centre for DNA Fingerprinting and Diagnostics (CDFD), Uppal, Hyderabad, 500039, India.ORCID 0000-0003-4946-401X
Subbareddy MaddikaLaboratory of Cell Death & Cell Survival, Centre for DNA Fingerprinting and Diagnostics (CDFD), Uppal, Hyderabad, 500039, India.ORCID 0000-0002-5880-391X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ubiquitination is a fundamental post-translational modification that orchestrates a wide range of cellular processes. This modification is executed through a cascade of enzymatic steps involving E1 activating enzymes, E2 conjugating enzymes, and E3 ligases. Among these, E2 enzymes and specific E3 ligases primarily dictate the type of ubiquitin linkage formed. Ubiquitination system can form chains of ubiquitin on any of its seven lysine residues or its N-terminal methionine, each generating a distinct three-dimensional topology. These structurally diverse polyubiquitin chains are selectively recognized by ubiquitin receptors, influencing substrate stability, localization, and interactions. These topologically diverse polyubiquitin chains function as discrete molecular signals, each with distinct physiological outcomes. This review focuses on key developments in our understanding of how specific ubiquitin linkage types participate in various cellular pathways and their implications on the fate and function of the protein.

Indexed as

PolyubiquitinUbiquitinAnimalsHumansProtein Processing, Post-TranslationalUbiquitinationUbiquitin-Protein LigasesPolyubiquitinUbiquitinUbiquitin-Protein Ligasesprotein degradationubiquitinubiquitin chainubiquitin linkage

Identifiers

PMID42018283
PMCPMC13137688

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.