Evidence map›Paper›PMID 20522549›Full record

ReviewThe Journal of biological chemistry2010

Thiazolyl peptide antibiotic biosynthesis: a cascade of post-translational modifications on ribosomal nascent proteins.

Christopher T Walsh, Michael G Acker, Albert A Bowers

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
8.3field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 93 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Enzymatic Cascade Reactions in Biosynthesis.Angewandte Chemie (International ed. in English) · 2019
    Review
  6. Review
  7. Review
  8. Review
  9. Natural [4 + 2]-Cyclases.Chemical reviews · 2017
    Review
  10. Review
  11. Article
  12. Review
  13. Recombinant thiopeptides containing noncanonical amino acids.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Christopher T WalshDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115, USA. christopher_walsh@hms.harvard.edu
Michael G Acker
Albert A Bowers
Harvard University · US

Funding

Treatments for Nipah Virus InfectionU54AI057159 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI KASPER, DENNIS L. · 2003 to 2013
$113.7M
Modular Enzymatic Assembly Lines for AntibioticsR01GM020011 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI WALSH, CHRISTOPHER T · 1985 to 2013
$8.2M
Biomimetic Synthesis of the CommunesinsF32CA136283 · NCI · HARVARD MEDICAL SCHOOL · PI BOWERS, ALBERT · 2008 to 2009
$97k
NCI NIH HHS CA136283NIAID NIH HHS U54 AI057 159NIGMS NIH HHS R01 GM020011PHS HHS GIM 20011
6 · The paper itself

Abstract

Antibiotics of the thiocillin, GE2270A, and thiostrepton class, which block steps in bacterial protein synthesis, contain a trithiazolyl (tetrahydro)pyridine core that provides the architectural constraints for high affinity binding to either the 50 S ribosomal subunit or elongation factor Tu. These mature antibiotic scaffolds arise from a cascade of post-translational modifications on 50-60-residue prepeptide precursors that trim away the N-terminal leader sequences (approximately 40 residues) while the C-terminal 14-18 residues are converted into the mature scaffold. In the producing microbes, the genes encoding the prepeptide open reading frames are flanked in biosynthetic clusters by genes encoding post-translational modification enzymes that carry out lantibiotic-type dehydrations of Ser and Thr residues to dehydroamino acid side chains, cyclodehydration and oxidation of cysteines to thiazoles, and condensation of two dehydroalanine residues en route to the (tetrahydro)pyridine core. The trithiazolyl pyridine framework thus arises from post-translational modification of the peptide backbone of three Cys and two Ser residues of the prepeptide.

Indexed as

Protein Processing, Post-TranslationalAnti-Bacterial AgentsBacteriaHumansPeptidesRibosomal ProteinsThiazolesAnti-Bacterial AgentsPeptidesRibosomal ProteinsThiazoles

Identifiers

PMID20522549
PMCPMC2934618
OpenAlexW2092055760

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.