Evidence map›Paper›PMID 23249187›Full record

ReviewCritical reviews in biochemistry and molecular biology

Structural analysis of protein-protein interactions in type I polyketide synthases.

Wei Xu, Kangjian Qiao, Yi Tang

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
4.1field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. 3 Biotech · 2021
    Review
  7. Article
  8. Article
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  10. Review
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  12. Article
  13. Biosynthesis of Oxytetracycline byFood technology and biotechnology · 2017
    Review
  14. Review
  15. Article
  16. Article
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  18. Review
  19. 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.

Wei XuDepartment of Chemical and Biomolecular Engineering, University of California, Los Angeles, CA 90095, USA.
Kangjian Qiao
Yi Tang
University of California, Los Angeles · US

Funding

Characterization and Engineering of Fungal Megasynthases in Escherichia coliR01GM085128 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TANG, YI · 2008 to 2016
$2.1M
NIGMS NIH HHS 1R01GM085128NIGMS NIH HHS R01 GM085128
6 · The paper itself

Abstract

Polyketide synthases (PKSs) are responsible for synthesizing a myriad of natural products with agricultural, medicinal relevance. The PKSs consist of multiple functional domains of which each can catalyze a specified chemical reaction leading to the synthesis of polyketides. Biochemical studies showed that protein-substrate and protein-protein interactions play crucial roles in these complex regio-/stereo-selective biochemical processes. Recent developments on X-ray crystallography and protein NMR techniques have allowed us to understand the biosynthetic mechanism of these enzymes from their structures. These structural studies have facilitated the elucidation of the sequence-function relationship of PKSs and will ultimately contribute to the prediction of product structure. This review will focus on the current knowledge of type I PKS structures and the protein-protein interactions in this system.

Indexed as

AnimalsCatalytic DomainCrystallography, X-RayHumansMammalsNuclear Magnetic Resonance, BiomolecularPolyketide SynthasesProtein ConformationProtein Interaction Domains and MotifsPolyketide Synthases

Identifiers

PMID23249187
PMCPMC3844684
OpenAlexW2079555388

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.