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Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance

Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_umu_180216

Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance

About this item

Full title

Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance

Publisher

New York: Nature Publishing Group US

Journal title

Nature chemical biology, 2021-04, Vol.17 (4), p.412-420

Language

English

Formats

Publication information

Publisher

New York: Nature Publishing Group US

More information

Scope and Contents

Contents

Many antibiotics inhibit bacterial growth by binding to the ribosome and interfering with protein biosynthesis. Macrolides represent one of the most successful classes of ribosome-targeting antibiotics. The main clinically relevant mechanism of resistance to macrolides is dimethylation of the 23S rRNA nucleotide A2058, located in the drug-binding s...

Alternative Titles

Full title

Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_swepub_primary_oai_DiVA_org_umu_180216

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_swepub_primary_oai_DiVA_org_umu_180216

Other Identifiers

ISSN

1552-4450,1552-4469

E-ISSN

1552-4469

DOI

10.1038/s41589-020-00715-0

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