Evidence map›Paper›PMID 28097217›Full record

ArticleScience advances2017

Amylose recognition and ring-size determination of amylomaltase.

Christian Roth, Nicole Weizenmann, Nicola Bexten, Wolfram Saenger, Wolfgang Zimmermann, Timm Maier, Norbert Sträter

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.7field-weighted citation impact, top 8% 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

29 citing papers in PubMed, 70 citations in OpenAlex.

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  11. Complete genome analysis ofFrontiers in microbiology · 2023
    Article
  12. Article
  13. Article
  14. Production of Large-Ring Cyclodextrins by Amylomaltases.Molecules (Basel, Switzerland) · 2022
    Review
  15. Article
  16. Review
  17. Article
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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

7 authors at 4 institutions in 3 countries.

Christian RothInstitut für Bioanalytische Chemie, Universität Leipzig, Deutscher Platz 5, 04103 Leipzig, Germany.; Department of Chemistry, University of York, Heslington, York, YO10 5DD, U.K.ORCID 0000-0001-5806-0987
Nicole WeizenmannInstitut für Biochemie, Universität Leipzig, Johannisallee 21-23, 04103 Leipzig, Germany.
Nicola BextenInstitut für Chemie-Kristallographie, Freie Universität Berlin, Takustrasse 6, 14195 Berlin, Germany.
Wolfram SaengerInstitut für Chemie-Kristallographie, Freie Universität Berlin, Takustrasse 6, 14195 Berlin, Germany.
Wolfgang ZimmermannInstitut für Biochemie, Universität Leipzig, Johannisallee 21-23, 04103 Leipzig, Germany.ORCID 0000-0002-5730-6663
Timm MaierBiozentrum, Universität Basel, Biozentrum, Klingelbergstrasse 50/70, CH-4056 Basel, Switzerland.
Norbert SträterInstitut für Bioanalytische Chemie, Universität Leipzig, Deutscher Platz 5, 04103 Leipzig, Germany.ORCID 0000-0002-2001-0500
Leipzig University · DEFreie Universität Berlin · DEUniversity of Basel · CHUniversity of York · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Starch is a major carbon and energy source throughout all kingdoms of life. It consists of two carbohydrate polymers, branched amylopectin and linear amylose, which are sparingly soluble in water. Hence, the enzymatic breakdown by glycoside hydrolases (GHs) is of great biological and societal importance. Amylomaltases (AMs) are GHs specialized in the hydrolysis of α-1,4-linked sugar chains such as amylose. They are able to catalyze an intramolecular transglycosylation of a bound sugar chain yielding polymeric sugar rings, the cycloamyloses (CAs), consisting of 20 to 100 glucose units. Despite a wealth of data on short oligosaccharide binding to GHs, no structural evidence is available for their interaction with polymeric substrates that better represent the natural polysaccharide. We have determined the crystal structure of

Indexed as

AmyloseBacterial ProteinsBiocatalysisCrystallography, X-RayGlycogen Debranching Enzyme SystemGlycosylationProtein DomainsStructure-Activity RelationshipThermus4 alpha-glucanotransferaseAmyloseBacterial ProteinsGlycogen Debranching Enzyme Systemcarbohydrate recognitioncarbohydratescrystal structureglycosyl transferasesStarch

Identifiers

PMID28097217
PMCPMC5235332
OpenAlexW2571970995

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.