Evidence map›Paper›PMID 27435901›Full record

ReviewAngewandte Chemie (International ed. in English)2016

New Structural Data Reveal the Motion of Carrier Proteins in Nonribosomal Peptide Synthesis.

Tiia Kittilä, Aurelio Mollo, Louise K Charkoudian, Max J Cryle

Open access · hybridAbstract readReview
In one paragraph

Review in Angewandte Chemie (International ed. in English), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
7.0field-weighted citation impact, top 3% 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

18 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Review
  3. Antimicrobial Activity ofInternational journal of molecular sciences · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  11. Article
  12. Engineering of the Filamentous FungusFrontiers in microbiology · 2018
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. 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

4 authors at 3 institutions in 3 countries.

Tiia KittiläDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120, Heidelberg, Germany.
Aurelio MolloDepartment of Chemistry, Haverford College, Haverford, PA, 19041, USA.
Louise K CharkoudianDepartment of Chemistry, Haverford College, Haverford, PA, 19041, USA. lcharkou@haverford.edu.
Max J CryleDepartment of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Jahnstrasse 29, 69120, Heidelberg, Germany. max.cryle@monash.edu.ORCID 0000-0002-9739-6157
Haverford College · USDiscovery Institute · USMax Planck Institute for Medical Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nonribosomal peptide synthetases (NRPSs) are one of the most promising resources for the production of new bioactive molecules. The mechanism of NRPS catalysis is based around sequential catalytic domains: these are organized into modules, where each module selects, modifies, and incorporates an amino acid into the growing peptide. The intermediates formed during NRPS catalysis are delivered between enzyme centers by peptidyl carrier protein (PCP) domains, which makes PCP interactions and movements crucial to NRPS mechanism. PCP movement has been linked to the domain alternation cycle of adenylation (A) domains, and recent complete NRPS module structures provide support for this hypothesis. However, it appears as though the A domain alternation alone is insufficient to account for the complete NRPS catalytic cycle and that the loaded state of the PCP must also play a role in choreographing catalysis in these complex and fascinating molecular machines.

Indexed as

BiocatalysisCarrier ProteinsModels, MolecularMolecular ConformationPeptidesPeptide SynthasesProtein ConformationCarrier Proteinsnon-ribosomal peptide synthasePeptidesPeptide Synthasesbiosynthesisenzymesnonribosomal peptide synthetasespeptidyl carrier proteinprotein structures

Identifiers

PMID27435901
PMCPMC5113783
OpenAlexW2495622733

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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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.