Evidence map›Paper›PMID 33093171›Full record

ArticleThe Journal of biological chemistry2020

Unique active-site and subsite features in the arabinogalactan-degrading GH43 exo-β-1,3-galactanase from

Kaori Matsuyama, Naomi Kishine, Zui Fujimoto, Naoki Sunagawa, Toshihisa Kotake, Yoichi Tsumuraya, Masahiro Samejima, Kiyohiko Igarashi, Satoshi Kaneko

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.4field-weighted citation impact, top 36% 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

4 citing papers in PubMed, 12 citations in OpenAlex.

  1. Crystal structure of endo-β-1,6-galactanase from Streptomyces avermitilis.Acta crystallographica. Section D, Structural biology · 2026
    Article
  2. Article
  3. Frontiers in plant science · 2022
    Article
  4. Review
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 5 institutions in 2 countries.

Kaori MatsuyamaDepartment of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Japan.
Naomi KishineAdvanced Analysis Center, National Agriculture and Food Research Organization (NARO), Tsukuba, Ibaraki, Japan.
Zui FujimotoAdvanced Analysis Center, National Agriculture and Food Research Organization (NARO), Tsukuba, Ibaraki, Japan.
Naoki SunagawaDepartment of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Japan.
Toshihisa KotakeDepartment of Biochemistry and Molecular Biology, Faculty of Science, Saitama University, Saitama, Japan.
Yoichi TsumurayaDepartment of Biochemistry and Molecular Biology, Faculty of Science, Saitama University, Saitama, Japan.
Masahiro SamejimaDepartment of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Japan; Faculty of Engineering, Shinshu University, Nagano, Japan.
Kiyohiko IgarashiDepartment of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo, Japan; VTT Technical Research Centre of Finland, Espoo, Finland. Electronic address: aquarius@mail.ecc.u-tokyo.ac.jp.
Satoshi KanekoDepartment of Subtropical Bioscience and Biotechnology, Faculty of Agriculture, University of the Ryukyus, Nishihara, Okinawa, Japan.
The University of Tokyo · JPNational Agriculture and Food Research Organization · JPSaitama University · JPShinshu University · JPUniversity of the Ryukyus · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Arabinogalactan proteins (AGPs) are plant proteoglycans with functions in growth and development. However, these functions are largely unexplored, mainly because of the complexity of the sugar moieties. These carbohydrate sequences are generally analyzed with the aid of glycoside hydrolases. The exo-β-1,3-galactanase is a glycoside hydrolase from the basidiomycete

Indexed as

Amino Acid SequenceCatalytic DomainCrystallography, X-RayFungal ProteinsGalactansGalactoseGlycoside HydrolasesMannansPhanerochaeteSequence HomologySubstrate Specificityarabinogalactanarabinogalactan endo-1,4-beta-galactosidaseFungal ProteinsGalactansgalactomannanGalactoseGlycoside HydrolasesMannansarabinogalactan-proteinbiodegradationcarbohydrate-binding module family 35carbohydrate-binding module family 35 exo-β-13-galactanasecarbohydrate-binding proteincarbohydrate metabolismenzyme structureexo-β-1,3-galactanaseglycoside hydrolase family 43Phanerochaete chrysosporiumplant cell wall

Identifiers

PMID33093171
PMCPMC7939473
OpenAlexW3093610343

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.