Evidence map›Paper›PMID 36161872›Full record

ReviewBiochemistry2022

Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation.

Diego Garrido Ruiz, Angelica Sandoval-Perez, Amith Vikram Rangarajan, Emma L Gunderson, Matthew P Jacobson

Open access · hybridAbstract readReview
In one paragraph

Review in Biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

70 citing papers in PubMed, 138 citations in OpenAlex.

  1. EvoMut: A computational framework for engineering oxidative stability in proteins.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Review
  4. Article
  5. Redox signals and oxidative stress in the control of mitochondrial protein import.Protein science : a publication of the Protein Society · 2026
    Review
  6. Article
  7. Cysteine thiol-to-sulfonate oxidation induces unfolding for the functional switching of the extracellular HMGB1 protein.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Medical Gas Plasma Inactivates Adenoviruses via Capsid Oxidation.Small (Weinheim an der Bergstrasse, Germany) · 2026
    Article
  14. Mining lysine post-translational modification sites by integrating protein language model representations with structural context.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

10 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Diego Garrido RuizDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States.
Angelica Sandoval-PerezDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States.
Amith Vikram RangarajanDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States.
Emma L GundersonDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States.
Matthew P JacobsonDepartment of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States.
University of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cysteine side chains can exist in distinct oxidation states depending on the pH and redox potential of the environment, and cysteine oxidation plays important yet complex regulatory roles. Compared with the effects of post-translational modifications such as phosphorylation, the effects of oxidation of cysteine to sulfenic, sulfinic, and sulfonic acid on protein structure and function remain relatively poorly characterized. We present an analysis of the role of cysteine reactivity as a regulatory factor in proteins, emphasizing the interplay between electrostatics and redox potential as key determinants of the resulting oxidation state. A review of current computational approaches suggests underdeveloped areas of research for studying cysteine reactivity through molecular simulations.

Indexed as

CysteineProteinsBiophysicsOxidation-ReductionSulfenic AcidsSulfonic AcidsCysteineProteinsSulfenic AcidsSulfonic Acids

Identifiers

PMID36161872
PMCPMC9583617
OpenAlexW4297093846

What Socratic 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 Socratic graph.