Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Role of Low-Molecular-Mass Penicillin-Binding Proteins, NagZ and AmpR in AmpC β-lactamase Regulation of Yersinia enterocolitica.

Frontiers in cellular and infection microbiology - 1 Jan 2017

Liu Chang, Li Chuchu, Chen Yuhuang, Hao Huijing, Liang Junrong, Duan Ran, Guo Zhaoke, Zhang Jing, Zhao Zhongzhi, Jing Huaiqi, Wang Xin, Shao Shihe

Abstract excerpt

Yersinia enterocolitica encodes a chromosomal AmpC β-lactamase under the regulation of the classical ampR-ampC system. To obtain a further understanding to the role of low-molecular-mass penicillin-binding proteins (LMM PBPs) including PBP4, PBP5, PBP6, and PBP7, as well as NagZ and AmpR in ampC regulation of Y. enterocolitica, series of single/multiple mutant strains were systematically constructed and the ampC...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acetylglucosaminidase
Share to beta-Lactamases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Gene Expression Regulation, Bacterial

Share to Gene Knockout Techniques

Share to Genetic Complementation Test

Share to N-Acetylmuramoyl-L-alanine Amidase

Share to Penicillin-Binding Proteins

Share to Yersinia enterocolitica

Source

Open in PubMed Open full text

Identifiers

PMID: 29021974
DOI: 10.3389/fcimb.2017.00425
PMCID: PMC5623720

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of Low-Molecular-Mass Penicillin-Binding Proteins, NagZ and AmpR in AmpC β-lactamase Regulation of Yersinia enterocolitica.PMID 29021974Read ↗

Complex Regulation Pathways of AmpC-Mediated β-Lactam Resistance in Enterobacter cloacae Complex.Semantic proximity Read ↗

Cefazolin and imipenem enhance AmpC expression and resistance in NagZ-dependent manner in Enterobacter cloacae complexSemantic proximity Read ↗

NagZ-dependent and NagZ-independent mechanisms for β-lactamase expression in Stenotrophomonas maltophilia.Semantic proximity Read ↗

Diversity and regulation of intrinsic β-lactamases from non-fermenting and other Gram-negative opportunistic pathogens.Semantic proximity Read ↗

Cefazolin and Imipenem Enhance AmpC Expression and Resistance in NagZ-Dependent Manner in Enterobacter CloacaeSemantic proximity Read ↗

Beta-lactam resistance response triggered by inactivation of a nonessential penicillin-binding protein.Semantic proximity Read ↗

Penicillin-binding proteins and beta-lactam resistance.Semantic proximity Read ↗

Cell Wall Recycling-Linked Coregulation of AmpC and PenB β-Lactamases through ampD Mutations in Burkholderia cenocepacia.Semantic proximity Read ↗

Progression of ampC amplification during de novo amoxicillin resistance development in E. coli.Semantic proximity Read ↗

Role of Pseudomonas aeruginosa low-molecular-mass penicillin-binding proteins in AmpC expression, β-lactam resistance, and peptidoglycan structure.Semantic proximity Read ↗

Chromosomal system for studying AmpC-mediated beta-lactam resistance mutation in Escherichia coli.Semantic proximity Read ↗

Inactivation of mrcA gene derepresses the basal-level expression of L1 and L2 β-lactamases in Stenotrophomonas maltophilia.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.