Evidence map›Paper›PMID 31460310›Full record

ArticleACS omega2019

Investigating the Deoxyribonuclease Activity of CRM197 with Site-Directed Mutagenesis.

Nathalie Bravo-Bautista, Hieu Hoang, Anusha Joshi, Jennifer Travis, Melissa Wooten, Nathan J Wymer

Open access · goldAbstract read
In one paragraph

Article in ACS omega, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.1field-weighted citation impact, top 53% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. Monomeric crystal structure of the vaccine carrier protein CRMActa crystallographica. Section F, Structural biology communications · 2023
    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

6 authors at 1 institution in 1 country.

Nathalie Bravo-BautistaDepartment of Chemistry and Biochemistry, Department of Biological and Biomedical Sciences, and Department of Pharmaceutical Sciences, North Carolina Central University, Durham, North Carolina 27707, United States.
Hieu HoangDepartment of Chemistry and Biochemistry, Department of Biological and Biomedical Sciences, and Department of Pharmaceutical Sciences, North Carolina Central University, Durham, North Carolina 27707, United States.
Anusha JoshiDepartment of Chemistry and Biochemistry, Department of Biological and Biomedical Sciences, and Department of Pharmaceutical Sciences, North Carolina Central University, Durham, North Carolina 27707, United States.
Jennifer TravisDepartment of Chemistry and Biochemistry, Department of Biological and Biomedical Sciences, and Department of Pharmaceutical Sciences, North Carolina Central University, Durham, North Carolina 27707, United States.
Melissa WootenDepartment of Chemistry and Biochemistry, Department of Biological and Biomedical Sciences, and Department of Pharmaceutical Sciences, North Carolina Central University, Durham, North Carolina 27707, United States.
Nathan J WymerDepartment of Chemistry and Biochemistry, Department of Biological and Biomedical Sciences, and Department of Pharmaceutical Sciences, North Carolina Central University, Durham, North Carolina 27707, United States.
North Carolina Central University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein cross-reactive material 197 (CRM197) is known to catalyze the hydrolytic cleavage of DNA (DNase activity). A suspected metal-binding site (S109, T111, and E112) and suspected DNA-binding motif (T89, K90, and V91) were predicted within the CRM197 protein X-ray crystal structure (4AE0) using METSITE and DNABindProt, respectively. Between these two predicted sites is a groove (K103, E116, T120, E122, F123, and R126) that may assist in DNase activity. Alanine scanning was performed at these sites to determine which amino acids might be important for DNase activity. These mutations individually or in combination either maintained or increased the overall DNase activity compared to the unmodified CRM197. Mutation at the suspected metal-binding site showed similar fluctuations to the overall DNase activity whether the DNase assays were run with Mg

Identifiers

PMID31460310
PMCPMC6682014
OpenAlexW2958892576

What OpenQuestion holds

Textmetadata
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.