Evidence map›Paper›PMID 25874689›Full record

ArticlePloS one2015

The characterization of modified starch branching enzymes: toward the control of starch chain-length distributions.

Cheng Li, Alex Chi Wu, Rob Marc Go, Jacob Malouf, Mark S Turner, Alpeshkumar K Malde, Alan E Mark, Robert G Gilbert

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

9 citing papers in PubMed, 35 citations in OpenAlex.

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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

8 authors at 3 institutions in 2 countries.

Cheng LiTongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan, Hubei, China; Centre for Nutrition and Food Science, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Brisbane, QLD, Australia.
Alex Chi WuTongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan, Hubei, China; Centre for Nutrition and Food Science, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Brisbane, QLD, Australia.
Rob Marc GoCentre for Nutrition and Food Science, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Brisbane, QLD, Australia.
Jacob MaloufCentre for Nutrition and Food Science, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Brisbane, QLD, Australia.
Mark S TurnerCentre for Nutrition and Food Science, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Brisbane, QLD, Australia; School of Agriculture and Food Sciences, The University of Queensland, Brisbane, QLD, Australia.
Alpeshkumar K MaldeSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.
Alan E MarkSchool of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, QLD, Australia.
Robert G GilbertTongji School of Pharmacy, Huazhong University of Science and Technology, Wuhan, Hubei, China; Centre for Nutrition and Food Science, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Brisbane, QLD, Australia.
University of Queensland · AUAgriculture and Food · AUARC Centre of Excellence for Plant Success in Nature and Agriculture · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Starch is a complex branched glucose polymer whose branch molecular weight distribution (the chain-length distribution, CLD) influences nutritionally important properties such as digestion rate. Chain-stopping in starch biosynthesis is by starch branching enzyme (SBE). Site-directed mutagenesis was used to modify SBEIIa from Zea mays (mSBEIIa) to produce mutants, each differing in a single conserved amino-acid residue. Products at different times from in vitro branching were debranched and the time evolution of the CLD measured by size-exclusion chromatography. The results confirm that Tyr352, Glu513, and Ser349 are important for mSBEIIa activity while Arg456 is important for determining the position at which the linear glucan is cut. The mutant mSBEIIa enzymes have different activities and suggest the length of the transferred chain can be varied by mutation. The work shows analysis of the molecular weight distribution can yield information regarding the enzyme branching sites useful for development of plants yielding starch with improved functionality.

Indexed as

Mutation1,4-alpha-Glucan Branching EnzymeAmino Acid SubstitutionCarbohydrate SequenceChromatography, GelCloning, MolecularEnzyme AssaysEscherichia coliGene ExpressionMolecular Dynamics SimulationMolecular Sequence DataMolecular WeightMutagenesis, Site-DirectedPlant ProteinsProtein EngineeringRecombinant Proteins1,4-alpha-Glucan Branching EnzymePlant ProteinsRecombinant ProteinsStarch

Identifiers

PMID25874689
PMCPMC4395411
OpenAlexW1974282986

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.