Evidence map›Paper›PMID 33628788›Full record

ReviewBioMed research international2021

Recent Advances in Predicting Protein S-Nitrosylation Sites.

Qian Zhao, Jiaqi Ma, Fang Xie, Yu Wang, Yu Zhang, Hui Li, Yuan Sun, Liqi Wang, Mian Guo, Ke Han

Abstract readReview
In one paragraph

Review in BioMed research international, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Biological Mechanisms ofAntioxidants (Basel, Switzerland) · 2021
    Review
  6. 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

10 authors.

Qian ZhaoSchool of Computer and Information Engineering, Heilongjiang Provincial Key Laboratory of Electronic Commerce and Information Processing, Harbin University of Commerce, Harbin 150028, China.
Jiaqi MaSchool of Computer and Information Engineering, Heilongjiang Provincial Key Laboratory of Electronic Commerce and Information Processing, Harbin University of Commerce, Harbin 150028, China.ORCID https://orcid.org/0000-0003-1428-1264
Fang XieSchool of Computer and Information Engineering, Heilongjiang Provincial Key Laboratory of Electronic Commerce and Information Processing, Harbin University of Commerce, Harbin 150028, China.
Yu WangSchool of Computer and Information Engineering, Heilongjiang Provincial Key Laboratory of Electronic Commerce and Information Processing, Harbin University of Commerce, Harbin 150028, China.
Yu ZhangSchool of Computer and Information Engineering, Heilongjiang Provincial Key Laboratory of Electronic Commerce and Information Processing, Harbin University of Commerce, Harbin 150028, China.
Hui LiSchool of Computer and Information Engineering, Heilongjiang Provincial Key Laboratory of Electronic Commerce and Information Processing, Harbin University of Commerce, Harbin 150028, China.
Yuan SunSchool of Pharmacy, Center of Pharmaceutical Engineering and Technology, Harbin University of Commerce, Harbin 150076, China.
Liqi WangSchool of Computer and Information Engineering, Heilongjiang Provincial Key Laboratory of Electronic Commerce and Information Processing, Harbin University of Commerce, Harbin 150028, China.
Mian GuoDepartment of Neurosurgery, The Second Affiliated Hospital of Harbin Medical University, Harbin 150086, China.
Ke HanSchool of Computer and Information Engineering, Heilongjiang Provincial Key Laboratory of Electronic Commerce and Information Processing, Harbin University of Commerce, Harbin 150028, China.ORCID https://orcid.org/0000-0003-0279-4150

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein S-nitrosylation (SNO) is a process of covalent modification of nitric oxide (NO) and its derivatives and cysteine residues. SNO plays an essential role in reversible posttranslational modifications of proteins. The accurate prediction of SNO sites is crucial in revealing a certain biological mechanism of NO regulation and related drug development. Identification of the sites of SNO in proteins is currently a very hot topic. In this review, we briefly summarize recent advances in computationally identifying SNO sites. The challenges and future perspectives for identifying SNO sites are also discussed. We anticipate that this review will provide insights into research on SNO site prediction.

Indexed as

Computational BiologyNitroso CompoundsProtein Processing, Post-TranslationalProteinsSequence Analysis, ProteinCysteineDatabases, ProteinNitric OxideCysteineNitric OxideNitroso CompoundsProteins

Identifiers

PMID33628788
PMCPMC7892234

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.