Evidence map›Paper›PMID 30181215›Full record

ArticleThe Journal of biological chemistry2018

Structural features of a bacterial cyclic α-maltosyl-(1→6)-maltose (CMM) hydrolase critical for CMM recognition and hydrolysis.

Masaki Kohno, Takatoshi Arakawa, Hiromi Ota, Tetsuya Mori, Tomoyuki Nishimoto, Shinya Fushinobu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 28% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
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

6 authors at 4 institutions in 4 countries.

Masaki KohnoFrom the Department of Biotechnology and.
Takatoshi ArakawaFrom the Department of Biotechnology and.ORCID 0000-0001-6496-5440
Hiromi Otathe Advanced Science Research Center, Okayama University, 3-1-1 Tsushima-Naka, Kita-ku, Okayama 700-8530, Japan.
Tetsuya Morithe R&D Division, Hayashibara Co., Ltd., 675-1 Fujisaki, Naka-ku, Okayama 702-8006, and.
Tomoyuki Nishimotothe R&D Division, Hayashibara Co., Ltd., 675-1 Fujisaki, Naka-ku, Okayama 702-8006, and.
Shinya FushinobuFrom the Department of Biotechnology and asfushi@mail.ecc.u-tokyo.ac.jp.ORCID 0000-0003-1346-6435
Department of Biotechnology · INHayashibara (Japan) · JPCollaborative Research Group · AUOkayama University of Science · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cyclic α-maltosyl-(1→6)-maltose (CMM,

Indexed as

Amino Acid SequenceArthrobacterCatalytic DomainCrystallography, X-RayGlycoside HydrolasesHydrolysisMacrocyclic CompoundsModels, MolecularOligosaccharidesProtein ConformationSequence Homologycyclic maltosyl-1-6-maltose hydrolase, Arthrobacter globiformiscyclo(-6)-glucopyranosyl-1-4-glucopyranosyl-1-6-glucopyranosyl-1-4-glucopyranosyl-(1-)Glycoside HydrolasesMacrocyclic CompoundsOligosaccharidesamylasecarbohydrate degradationcarbohydrate metabolismCMM catabolismcrystal structurecyclic oligosaccharidescyclodextrinsglycoside hydrolasehydrolytic enzymeneopullulanaseoligosaccharideX-ray crystallography

Identifiers

PMID30181215
PMCPMC6204909
OpenAlexW2890007595

What OpenQuestion holds

Textmetadata
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.