Evidence map›Paper›PMID 39702281›Full record

ReviewCancer cell international2024

The evolution of S-nitrosylation detection methodology and the role of protein S-nitrosylation in various cancers.

Feng Liang, Min Wang, Jiannan Li, Jie Guo

Abstract readReview
In one paragraph

Review in Cancer cell international, 2024. 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. Review
  2. Review
  3. Review
  4. Review
  5. Review
  6. Article
  7. 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

4 authors.

Feng Liang *Department of General Surgery, The Second Hospital of Jilin University, Changchun, China.
Min Wang *Department of General Surgery, The Second Hospital of Jilin University, Changchun, China.
Jiannan LiDepartment of General Surgery, The Second Hospital of Jilin University, Changchun, China.
Jie GuoDepartment of Radiation Oncology, The Second Hospital of Jilin University, Changchun, China. guojie@jlu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

S-nitrosylation (SNO) modification, a nitric oxide (NO)-mediated post-translational modification (PTM) of proteins, plays an important role in protein microstructure, degradation, activity, and stability. Due to the presence of reducing agents, the SNO modification process mediated by NO derivatives is often reversible and unstable. This reversible transformation between SNO modification and denitrification often influences the structure, activity, and function of proteins. The reversibility of SNO modifications also poses a challenge when verifying changes in the biological functions of proteins. Moreover, SNO modification of key signaling pathway proteins, such as caspase-3, NF-κB, and Bcl-2, can affect tumor proliferation, invasion, and apoptosis. The SNO-modified proteins play important roles in both promoting and inhibiting cancer, which indirectly confirms the duality and complexity of SNO modification functions. This article reviews the biological significance of various SNO-modified proteins in different cancers, providing a theoretical basis for determining whether the related changes of SNO-modified proteins are universal in cancers. Additionally, this review presents a comprehensive and detailed summary of the evolution of detection methods for SNO-modified proteins, providing a possible methodological basis for future research on SNO-modified proteins.

Indexed as

CancerCysteineS-nitrosylation

Identifiers

PMID39702281
PMCPMC11660716

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.