Evidence map›Paper›PMID 27693891›Full record

ReviewCurrent opinion in chemical biology2016

Convergent biosynthetic pathways to β-lactam antibiotics.

Craig A Townsend

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.6field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. β-Lactams from the Ocean.Marine drugs · 2023
    Review
  7. Structural Studies of Modular Nonribosomal Peptide Synthetases.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  8. Review
  9. ThnL, a B12-dependent radicalProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Antibiotic Discovery and Resistance: The Chase and the Race.Antibiotics (Basel, Switzerland) · 2022
    Review
  12. Article
  13. Article
  14. Competing off-loading mechanisms of meropenem from an l,d-transpeptidase reduce antibiotic effectiveness.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Activation modes in biocatalytic radical cyclization reactions.Journal of industrial microbiology & biotechnology · 2021
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

1 author at 1 institution in 1 country.

Craig A TownsendDepartment of Chemistry, Johns Hopkins University, 3400 N. Charles Street, Baltimore, MD 21218, USA. Electronic address: ctownsend@jhu.edu.
Johns Hopkins University · US

Funding

Biosynthesis of Beta-Lactam AntibioticsR37AI014937 · NIAID · JOHNS HOPKINS UNIVERSITY · PI TOWNSEND, CRAIG ARTHUR · 2004 to 2013
$5.2M
Biosynthesis of Beta Lactam AntibioticsR01AI121072 · NIAID · JOHNS HOPKINS UNIVERSITY · PI TOWNSEND, CRAIG ARTHUR · 2016 to 2025
$4.9M
B LACTAM AND AMINO ACID DERIVED ANTIBIOTIC BIOSYNTHESISR01AI014937 · NIAID · JOHNS HOPKINS UNIVERSITY · PI TOWNSEND, CRAIG A · 1985 to 2003
$1.5M
Biosynthesis of Beta-Lactam AntibioticsR56AI014937 · NIAID · JOHNS HOPKINS UNIVERSITY · PI TOWNSEND, CRAIG ARTHUR · 2014 to 2014
$383k
NIAID NIH HHS R01 AI014937NIAID NIH HHS R01 AI121072NIAID NIH HHS R37 AI014937NIAID NIH HHS R56 AI014937
6 · The paper itself

Abstract

Five naturally-occurring families of β-lactams have inspired a class of drugs that constitute >60% of the antimicrobials used in human medicine. Their biosynthetic pathways reveal highly individualized synthetic strategies that yet converge on a common azetidinone ring assembled in structural contexts that confer selective binding and inhibition of d,d-transpeptidases that play essential roles in bacterial cell wall (peptidoglycan) biosynthesis. These enzymes belong to a single 'clan' of evolutionarily distinct serine hydrolases whose active site geometry and mechanism of action is specifically matched by these antibiotics for inactivation that is kinetically competitive with their native function. Unusual enzyme-mediated reactions and catalytic multitasking in these pathways are discussed with particular attention to the diverse ways the β-lactam itself is generated, and more broadly how the intrinsic reactivity of this core structural element is modulated in natural systems through the introduction of ring strain and electronic effects.

Indexed as

Anti-Bacterial Agentsbeta-LactamsCatalysisHumansKineticsAnti-Bacterial Agentsbeta-Lactams

Identifiers

PMID27693891
PMCPMC5161666
OpenAlexW2527387730

What OpenQuestion holds

Textmetadata
LicenceTDM
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.