Evidence map›Paper›PMID 33203705›Full record

ArticleThe Journal of biological chemistry

The role of cysteines in the structure and function of OGG1.

Katarina Wang, Marah Maayah, Joann B Sweasy, Khadijeh S Alnajjar

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.3field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 42 citations in OpenAlex.

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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 at 2 institutions in 1 country.

Katarina WangDepartment of Therapeutic Radiology, Yale School of Medicine, New Haven, Connecticut, USA.
Marah MaayahDepartment of Therapeutic Radiology, Yale School of Medicine, New Haven, Connecticut, USA.
Joann B SweasyDepartment of Cellular and Molecular Medicine, The University of Arizona Cancer Center, Tucson, Arizona, USA.
Khadijeh S AlnajjarDepartment of Cellular and Molecular Medicine, The University of Arizona Cancer Center, Tucson, Arizona, USA. Electronic address: ksalnajjar@arizona.edu.
University of Arizona · USYale University · US

Funding

SUBSTRATE SPECIFICITY OF THE BER OXIDATIVE DNA GLYCOSYLASESP01CA098993 · NCI · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI LEE, ANDREA J · 2004 to 2021
$25.9M
The role of cysteines in the response of 8-oxoguanine glycosylase (OGG1) to oxidative stressK99ES029555 · NIEHS · UNIVERSITY OF ARIZONA · PI ALNAJJAR, KHADIJEH · 2019 to 2020
$198k
NCI NIH HHS P01 CA098993NIEHS NIH HHS K99 ES029555
6 · The paper itself

Abstract

8-Oxoguanine glycosylase (OGG1) is a base excision repair enzyme responsible for the recognition and removal of 8-oxoguanine, a commonly occurring oxidized DNA modification. OGG1 prevents the accumulation of mutations and regulates the transcription of various oxidative stress-response genes. In addition to targeting DNA, oxidative stress can affect proteins like OGG1 itself, specifically at cysteine residues. Previous work has shown that the function of OGG1 is sensitive to oxidants, with the cysteine residues of OGG1 being the most likely site of oxidation. Due to the integral role of OGG1 in maintaining cellular homeostasis under oxidative stress, it is important to understand the effect of oxidants on OGG1 and the role of cysteines in its structure and function. In this study, we investigate the role of the cysteine residues in the function of OGG1 by mutating and characterizing each cysteine residue. Our results indicate that the cysteines in OGG1 fall into four functional categories: those that are necessary for (1) glycosylase activity (C146 and C255), (2) lyase activity (C140S, C163, C241, and C253), and (3) structural stability (C253) and (4) those with no known function (C28 and C75). These results suggest that under conditions of oxidative stress, cysteine can be targeted for modifications, thus altering the response of OGG1 and affecting its downstream cellular functions.

Indexed as

CysteineDNA GlycosylasesDNA RepairElectrophoretic Mobility Shift AssayOxidation-ReductionOxidative StressCysteineDNA Glycosylases8-oxoguanine glycosylasebase excision repaircysteine oxidationDNA repairoxidative stress

Identifiers

PMID33203705
PMCPMC7948458
OpenAlexW3102421218

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.