Evidence map›Paper›PMID 28401144›Full record

ArticleFrontiers in chemistry2017

Insights into the Activity Change of Spore Photoproduct Lyase Induced by Mutations at a Peripheral Glycine Residue.

Linlin Yang, Lei Li

Open access · goldAbstract read
In one paragraph

Article in Frontiers in chemistry, 2017. 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
0.2field-weighted citation impact, top 45% 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. 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

2 authors at 2 institutions in 1 country.

Linlin YangDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University Indianapolis Indianapolis, IN, USA.
Lei LiDepartment of Chemistry and Chemical Biology, Indiana University-Purdue University IndianapolisIndianapolis, IN, USA; Department of Dermatology, Indiana University School of MedicineIndianapolis, IN, USA.
Indiana University – Purdue University Indianapolis · USUniversity of Indianapolis · US

Funding

Enzyme Catalysis of Toluene Degradation and Unusual DNA Photoproduct RepairR00ES017177 · NIEHS · INDIANA UNIVERSITY INDIANAPOLIS · PI LI, LEI · 2009 to 2011
$747k
Enzyme Catalysis of Toluene Degradation and Unusual DNA Photoproduct RepairK99ES017177 · NIEHS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LI, LEI · 2008 to 2009
$167k
NIEHS NIH HHS K99 ES017177NIEHS NIH HHS R00 ES017177
6 · The paper itself

Abstract

UV radiation triggers the formation of 5-thyminyl-5,6-dihydrothymine, i.e., the spore photoproduct (SP), in the genomic DNA of bacterial endospores. These SPs, if not repaired in time, may lead to genome instability and cell death. SP is mainly repaired by spore photoproduct lyase (SPL) during spore outgrowth via an unprecedented protein-harbored radical transfer pathway that is composed of at least a cysteine and two tyrosine residues. This mechanism is consistent with the recently solved SPL structure that shows all three residues are located in proximity and thus able to participate in the radical transfer process during the enzyme catalysis. In contrast, an earlier

Indexed as

mutationprotein structureradical SAM enzymesradical transferspore photoproduct lyase

Identifiers

PMID28401144
PMCPMC5368176
OpenAlexW2600003067

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.