Evidence map›Paper›PMID 29779664›Full record

ArticleMethods in enzymology2018

PKS-NRPS Enzymology and Structural Biology: Considerations in Protein Production.

Meredith A Skiba, Finn P Maloney, Qingyun Dan, Amy E Fraley, Courtney C Aldrich, Janet L Smith, W Clay Brown

Abstract read
In one paragraph

Article in Methods in enzymology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Frontiers in bioengineering and biotechnology · 2021
    Review
  8. Article
  9. Review
  10. 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

7 authors.

Meredith A SkibaUniversity of Michigan, Ann Arbor, MI, United States.
Finn P MaloneyUniversity of Michigan, Ann Arbor, MI, United States.
Qingyun DanUniversity of Michigan, Ann Arbor, MI, United States.
Amy E FraleyUniversity of Michigan, Ann Arbor, MI, United States.
Courtney C AldrichUniversity of Minnesota, Minneapolis, MN, United States.
Janet L SmithUniversity of Michigan, Ann Arbor, MI, United States. Electronic address: janetsmith@umich.edu.
W Clay BrownUniversity of Michigan, Ann Arbor, MI, United States. Electronic address: wclayb@umich.edu.

Funding

Cellular Biotechnology Training Program (CBTP)T32GM008353 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCHWENDEMAN, ANNA · 1991 to 2021
$9.3M
STRUCTURE AND FUNCTION OF A PURINE BIOSYNTHETIC ENZYMER01DK042303 · NIDDK · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SMITH, JANET L. · 1990 to 2024
$6.6M
Molecular Analysis of Modular Polyketide SynthasesR01GM076477 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHERMAN, DAVID H, SMITH, JANET L. · 2006 to 2018
$5.2M
Biosynthetic Analysis of Marine Cyanobacterial PathwaysR01CA108874 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI GERWICK, WILLIAM HENRY, SHERMAN, DAVID H · 2006 to 2015
$3.4M
Cellular Biotechnology Training Program (CBTP) - Years 31-35T32GM145304 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Guizhi Zhu · 2022 to 2026
$2.6M
Design of Antituberculosis Agents that Target Siderophore BiosynthesisR01AI070219 · NIAID · UNIVERSITY OF MINNESOTA · PI ALDRICH, COURTNEY C · 2006 to 2013
$2.2M
NCI NIH HHS R01 CA108874NIAID NIH HHS R01 AI070219NIDDK NIH HHS R01 DK042303NIGMS NIH HHS R01 GM076477NIGMS NIH HHS T32 GM008353NIGMS NIH HHS T32 GM145304
6 · The paper itself

Abstract

The structural diversity and complexity of marine natural products have made them a rich and productive source of new bioactive molecules for drug development. The identification of these new compounds has led to extensive study of the protein constituents of the biosynthetic pathways from the producing microbes. Essential processes in the dissection of biosynthesis have been the elucidation of catalytic functions and the determination of 3D structures for enzymes of the polyketide synthases and nonribosomal peptide synthetases that carry out individual reactions. The size and complexity of these proteins present numerous difficulties in the process of going from gene to structure. Here, we review the problems that may be encountered at the various steps of this process and discuss some of the solutions devised in our and other labs for the cloning, production, purification, and structure solution of complex proteins using Escherichia coli as a heterologous host.

Indexed as

Acyl Carrier ProteinBacteriaBacterial Outer Membrane ProteinsCloning, MolecularCodonCrystallizationCulture MediaEscherichia coliEscherichia coli ProteinsPeptide SynthasesPlasmidsPolyketide SynthasesPromoter Regions, GeneticProtein DomainsProtein EngineeringRecombinant ProteinsAcyl Carrier ProteinBacterial Outer Membrane ProteinsCodonCulture MediaEscherichia coli Proteinsnon-ribosomal peptide synthasePeptide SynthasesPolyketide SynthasesRecombinant ProteinstraN protein, E coliChaperonesCoexpressionCyanobacteriaNonribosomal peptide synthetasePolyketide synthaseProtein crystallizationProtein foldingProtein productionProtein purificationProtein solubility

Identifiers

PMID29779664
PMCPMC5992914

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.