Evidence map›Paper›PMID 34346105›Full record

ArticleProteins2022

Structural elements determining the transglycosylating activity of glycoside hydrolase family 57 glycogen branching enzymes.

Gang Xiang, Hans Leemhuis, Marc Jos Elise Cornelis van der Maarel

Open access · hybridAbstract read
In one paragraph

Article in Proteins, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

6 citing papers in PubMed, 14 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

3 authors at 1 institution in 1 country.

Gang XiangBioproduct Engineering, Engineering and Technology institute Groningen (ENTEG), University of Groningen, Groningen, the Netherlands.
Hans LeemhuisBioproduct Engineering, Engineering and Technology institute Groningen (ENTEG), University of Groningen, Groningen, the Netherlands.
Marc Jos Elise Cornelis van der MaarelBioproduct Engineering, Engineering and Technology institute Groningen (ENTEG), University of Groningen, Groningen, the Netherlands.ORCID 0000-0002-3173-0001
University of Groningen · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycoside hydrolase family 57 glycogen branching enzymes (GH57GBE) catalyze the formation of an α-1,6 glycosidic bond between α-1,4 linked glucooliogosaccharides. As an atypical family, a limited number of GH57GBEs have been biochemically characterized so far. This study aimed at acquiring a better understanding of the GH57GBE family by a systematic sequence-based bioinformatics analysis of almost 2500 gene sequences and determining the branching activity of several native and mutant GH57GBEs. A correlation was found in a very low or even no branching activity with the absence of a flexible loop, a tyrosine at the loop tip, and two β-strands.

Indexed as

1,4-alpha-Glucan Branching EnzymeBacterial ProteinsGlycoside HydrolasesAmyloseGlycogenGlycosylationModels, MolecularProtein Conformation1,4-alpha-Glucan Branching EnzymeAmyloseBacterial ProteinsGlycogenGlycoside Hydrolasesamyloseglycogenglycogen branching enzymesglycoside hydrolase family 57

Identifiers

PMID34346105
PMCPMC9291813
OpenAlexW3171206736

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.