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

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr.

Proceedings of the National Academy of Sciences of the United States of America - 25 Mar 2008

Baysarowich Jennifer, Koteva Kalinka, Hughes Donald W, Ejim Linda, Griffiths Emma, Zhang Kun, Junop Murray, Wright Gerard D

Abstract excerpt

The rifamycin antibiotic rifampin is important for the treatment of tuberculosis and infections caused by multidrug-resistant Staphylococcus aureus. Recent iterations of the rifampin core structure have resulted in new drugs and drug candidates for the treatment of a much broader range of infectious diseases. This expanded use of rifamycin antibiotics has the potential to select for increased resistance. One...

Read the complete abstract on PubMed

Topics

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

Share to ADP Ribose Transferases
Share to Antibiotics, Antitubercular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Catalysis

Share to Chromatography, High Pressure Liquid

Share to Drug Resistance, Microbial

Share to Mycobacterium smegmatis

Share to Rifampin

Share to Structural Homology, Protein

Source

Open in PubMed Open full text

Identifiers

PMID: 18349144
DOI: 10.1073/pnas.0711939105
PMCID: PMC2290778

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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

Rifamycin antibiotic resistance by ADP-ribosylation: Structure and diversity of Arr.PMID 18349144Read ↗

Discovery of inhibitors for bacterial Arr enzymes ADP-ribosylating and inactivating rifamycin antibioticsSemantic proximity Read ↗

Integrative metagenomic and biochemical studies on rifamycin ADP-ribosyltransferases discovered in the sediment microbiome.Semantic proximity Read ↗

Genomic epidemiology of rifampicin ADP-ribosyltransferase (Arr) in the Bacteria domainSemantic proximity Read ↗

Inhibition of RNA Polymerase by Rifampicin and Rifamycin-Like MoleculesSemantic proximity Read ↗

A rifamycin inactivating phosphotransferase family shared by environmental and pathogenic bacteriaSemantic proximity Read ↗

C25-modified rifamycin derivatives with improved activity against Mycobacterium abscessusSemantic proximity Read ↗

Rifamycin congeners kanglemycins are active against rifampicin-resistant bacteria via a distinct mechanismSemantic proximity Read ↗

Molecular Mechanisms Underlying Antimicrobial Resistance in Mycobacteria.Semantic proximity Read ↗

Blocking Bacterial Naphthohydroquinone Oxidation and ADP-Ribosylation Improves Activity of Rifamycins against Mycobacterium abscessusSemantic proximity Read ↗

Mycobacterium abscessus HelR interacts with RNA Polymerase to confer intrinsic rifamycin resistanceSemantic proximity Read ↗

Mutations in RNA polymerase that drive the emergence of antibiotic resistance.Semantic proximity Read ↗

Structural and molecular rationale for the diversification of resistance mediated by the Antibiotic_NAT familySemantic proximity Read ↗

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