The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning (Q24652742)

Agata L Starosta

4

0 references

Paola Fucini

Paola Fucini

6

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Frank Schluenzen

Frank Schluenzen

2

0 references

Daniel N. Wilson

Daniel N Wilson

1

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author name string

Joerg M Harms

Proceedings of the National Academy of Sciences of the United States of America

3

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language of work or name

English

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publication date

9 September 2008

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published in

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volume

105

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issue

36

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page(s)

13339-44

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cites work

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Inhibition of peptide bond formation by pleuromutilins: the structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with tiamulin

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Ribosomal RNA is the target for oxazolidinones, a novel class of translational inhibitors

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The site of action of oxazolidinone antibiotics in living bacteria and in human mitochondria.

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Resistance mutations in 23 S rRNA identify the site of action of the protein synthesis inhibitor linezolid in the ribosomal peptidyl transferase center

21 January 2018

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21 January 2018

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The protein synthesis inhibitors, oxazolidinones and chloramphenicol, cause extensive translational inaccuracy in vivo

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21 January 2018

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The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release.

21 January 2018

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tRNA selection and kinetic proofreading in translation

21 January 2018

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Peptidyl-tRNA regulates the GTPase activity of translation factors

21 January 2018

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Processing of X-ray diffraction data collected in oscillation mode

21 January 2018

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Mutations in ribosomal protein L3 and 23S ribosomal RNA at the peptidyl transferase centre are associated with reduced susceptibility to tiamulin in Brachyspira spp. isolates.

21 January 2018

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21 January 2018

Identifiers

DOI

10.1073/PNAS.0804276105

1 reference

3437042

ADS bibcode

2008PNAS..10513339W

0 references

3437042

1 reference

1 reference

1 reference