Antibacterial potency of type VI amidase effector toxins is dependent on substrate topology and cellular context.
E. coli
biochemistry
chemical biology
cognate immunity
deep mutational scanning
host–microbe interaction
infectious disease
microbiology
peptidoglycan
topology
type VI amidase effector
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
28 06 2022
28 06 2022
Historique:
received:
22
05
2022
accepted:
23
06
2022
pubmed:
29
6
2022
medline:
12
7
2022
entrez:
28
6
2022
Statut:
epublish
Résumé
Members of the bacterial
Identifiants
pubmed: 35762582
doi: 10.7554/eLife.79796
pii: 79796
pmc: PMC9270033
doi:
pii:
Substances chimiques
Anti-Bacterial Agents
0
Bacterial Proteins
0
Peptidoglycan
0
Amidohydrolases
EC 3.5.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIAID NIH HHS
ID : R01 AI132851
Pays : United States
Informations de copyright
© 2022, Radkov et al.
Déclaration de conflit d'intérêts
AR, AS, SF, CH, HS, RK, SM, ST, CM, JB, ZZ, LS, WH, WV, AR, JS, SA, PB, BH No competing interests declared, SC currently the President and CEO of Arcadia Science, a for-profit research company focused on non-model organisms. While work presented in this manuscript is not related and will not be continued at Arcadia, I thought it would be prudent to declare this position which may be perceived by some as a competing interest
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