Evidence map›Paper›PMID 32816991›Full record

ArticleThe Journal of biological chemistry2020

Domain architecture divergence leads to functional divergence in binding and catalytic domains of bacterial and fungal cellobiohydrolases.

Akihiko Nakamura, Daiki Ishiwata, Akasit Visootsat, Taku Uchiyama, Kenji Mizutani, Satoshi Kaneko, Takeshi Murata, Kiyohiko Igarashi, Ryota Iino

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

10 citing papers in PubMed, 28 citations in OpenAlex.

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  10. A Swollenin FromFrontiers in microbiology · 2021
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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

9 authors at 6 institutions in 1 country.

Akihiko NakamuraDepartment of Applied Life Sciences, Faculty of Agriculture, Shizuoka University, Shizuoka, Shizuoka, Japan. Electronic address: aki-naka@shizuoka.ac.jp.
Daiki IshiwataDepartment of Functional Molecular Science, School of Physical Sciences, SOKENDAI (The Graduate University for Advanced Studies), Hayama, Kanagawa, Japan; Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki, Aichi, Japan.
Akasit VisootsatDepartment of Functional Molecular Science, School of Physical Sciences, SOKENDAI (The Graduate University for Advanced Studies), Hayama, Kanagawa, Japan; Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki, Aichi, Japan.
Taku UchiyamaDepartment of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Japan.
Kenji MizutaniGraduate School of Medical Life Science, Yokohama City University, Tsurumi, Yokohama, Japan.
Satoshi KanekoDepartment of Subtropical Biochemistry and Biotechnology, Faculty of Agriculture, University of the Ryukyus, Nishihara, Okinawa, Japan.
Takeshi MurataDepartment of Chemistry, Graduate School of Science, Chiba University, Inage, Chiba, Japan.
Kiyohiko IgarashiDepartment of Biomaterials Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Japan.
Ryota IinoDepartment of Functional Molecular Science, School of Physical Sciences, SOKENDAI (The Graduate University for Advanced Studies), Hayama, Kanagawa, Japan; Institute for Molecular Science, National Institutes of Natural Sciences, Okazaki, Aichi, Japan. Electronic address: iino@ims.ac.jp.
National Institutes of Natural Sciences · JPThe University of Tokyo · JPChiba University · JPShizuoka University · JPUniversity of the Ryukyus · JPYokohama City University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellobiohydrolases directly convert crystalline cellulose into cellobiose and are of biotechnological interest to achieve efficient biomass utilization. As a result, much research in the field has focused on identifying cellobiohydrolases that are very fast. Cellobiohydrolase A from the bacterium

Indexed as

Bacterial ProteinsBinding SitesCatalytic DomainCellulomonasCelluloseCellulose 1,4-beta-CellobiosidaseCrystallography, X-RayFungal ProteinsHypocrealesModels, MolecularProtein BindingProtein ConformationProtein DomainsSubstrate SpecificityBacterial ProteinsCelluloseCellulose 1,4-beta-CellobiosidaseFungal Proteinscarbohydrate-binding proteincellulaseCellulomonas fimicelluloseglycoside hydrolaseglycoside hydrolase family 6microscopic imagingmolecular imagingprocessivitysingle-molecule biophysicssingle-molecule observationTrichoderma reesei

Identifiers

PMID32816991
PMCPMC7586223
OpenAlexW3069000996

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.