Evidence map›Paper›PMID 31999086›Full record

ArticleACS chemical biology2020

The Kinetic and Molecular Basis for the Interaction of LexA and Activated RecA Revealed by a Fluorescent Amino Acid Probe.

Zachary M Hostetler, Michael B Cory, Chloe M Jones, E James Petersson, Rahul M Kohli

Open access · greenAbstract read
In one paragraph

Article in ACS chemical biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Snapshots ofiScience · 2025
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Non-Canonical Amino Acids in Analyses of Protease Structure and Function.International journal of molecular sciences · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Exploration of inhibitors of the bacterial LexA repressor-protease.Bioorganic & medicinal chemistry letters · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Synthesis and characterization of fluorescent amino acid dimethylaminoacridonylalanine.ARKIVOC : free online journal of organic chemistry · 2021
    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

5 authors at 1 institution in 1 country.

Zachary M HostetlerGraduate Group in Cell and Molecular Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Michael B CoryGraduate Group in Biochemistry and Molecular Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
Chloe M JonesGraduate Group in Biochemistry and Molecular Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.
E James PeterssonDepartment of Chemistry, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0003-3854-9210
Rahul M KohliDepartment of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, United States.ORCID 0000-0002-7689-5678
University of Pennsylvania · US

Funding

Predoctoral Training at the Chemistry-Biology InterfaceT32GM071339 · NIGMS · WISTAR INSTITUTE · PI MARMORSTEIN, RONEN, SPEICHER, DAVID W. · 2005 to 2019
$3.2M
Predoctoral Training at the Chemistry-Biology InterfaceT32GM133398 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Ronen Marmorstein, Ernest James Petersson · 2020 to 2026
$2.4M
Training in Microbial Pathogenesis and GenomicsT32AI141393 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI GOULIAN, MARK D, ZHU, JUN · 2019 to 2023
$1.3M
The Molecular Basis for the Bacterial SOS SignalR01GM127593 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KOHLI, RAHUL MANU, PETERSSON, ERNEST JAMES · 2018 to 2021
$1.2M
Protocol Driven Hemodynamic Support in Septic ShockK23GM071399 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI SEVRANSKY, JONATHAN E · 2005 to 2009
$671k
NIAID NIH HHS T32 AI141393NIGMS NIH HHS K23 GM071399NIGMS NIH HHS R01 GM127593NIGMS NIH HHS T32 GM071339NIGMS NIH HHS T32 GM133398
6 · The paper itself

Abstract

The bacterial DNA damage response (the SOS response) is a key pathway involved in antibiotic evasion and a promising target for combating acquired antibiotic resistance. Activation of the SOS response is controlled by two proteins: the repressor LexA and the DNA damage sensor RecA. Following DNA damage, direct interaction between RecA and LexA leads to derepression of the SOS response. However, the exact molecular details of this interaction remain unknown. Here, we employ the fluorescent unnatural amino acid acridonylalanine (Acd) as a minimally perturbing probe of the

Indexed as

Amino AcidsAnti-Bacterial AgentsBacterial ProteinsBinding SitesDNA-Binding ProteinsDNA DamageDrug Resistance, MicrobialEscherichia coliEscherichia coli ProteinsFluorescent DyesKineticsLexA Repressor ProteinModels, MolecularProtein BindingProtein ConformationRec A RecombinasesAmino AcidsAnti-Bacterial AgentsBacterial ProteinsDNA-Binding ProteinsEscherichia coli ProteinsFluorescent DyesLexA Repressor ProteinrecA protein, E coliRec A RecombinasesSerine Endopeptidases

Identifiers

PMID31999086
PMCPMC7230020
OpenAlexW3003340460

What OpenQuestion holds

Textmetadata
LicenceTDM
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.