Evidence map›Paper›PMID 27609516›Full record

ArticleThe Journal of biological chemistry2016

Single-molecule Imaging Analysis of Binding, Processive Movement, and Dissociation of Cellobiohydrolase Trichoderma reesei Cel6A and Its Domains on Crystalline Cellulose.

Akihiko Nakamura, Tomoyuki Tasaki, Daiki Ishiwata, Mayuko Yamamoto, Yasuko Okuni, Akasit Visootsat, Morice Maximilien, Hiroyuki Noji, Taku Uchiyama, Masahiro Samejima and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
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  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023
    Review
  9. Acoustic force spectroscopy reveals subtle differences in cellulose unbinding behavior of carbohydrate-binding modules.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Convergent evolution of processivity in bacterial and fungal cellulases.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Novel Endotype Xanthanase from Xanthan-DegradingApplied and environmental microbiology · 2019
    Article
  20. 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

12 authors at 7 institutions in 4 countries.

Akihiko NakamuraFrom the Okazaki Institute for Integrative Bioscience and.
Tomoyuki Tasakithe Department of Applied Chemistry, Graduate School of Engineering, University of Tokyo, Tokyo 113-8656, Japan.
Daiki IshiwataFrom the Okazaki Institute for Integrative Bioscience and.
Mayuko YamamotoFrom the Okazaki Institute for Integrative Bioscience and.
Yasuko OkuniFrom the Okazaki Institute for Integrative Bioscience and.
Akasit Visootsatthe Department of Biochemistry, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand.
Morice Maximilienthe National Chemical Engineering Institute in Paris, Paris 75005, France.
Hiroyuki Nojithe Department of Applied Chemistry, Graduate School of Engineering, University of Tokyo, Tokyo 113-8656, Japan.
Taku Uchiyamathe Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan, and.
Masahiro Samejimathe Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan, and.
Kiyohiko Igarashithe Department of Biomaterial Sciences, Graduate School of Agricultural and Life Sciences, University of Tokyo, Tokyo 113-8657, Japan, and.
Ryota IinoFrom the Okazaki Institute for Integrative Bioscience and iino@ims.ac.jp.
The University of Tokyo · JPOkazaki Institute for Integrative Bioscience · JPChimie ParisTech · FRInstitute for Molecular Science · JPKasetsart University · THThe Graduate University for Advanced Studies, SOKENDAI · JPVTT Technical Research Centre of Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Trichoderma reesei Cel6A (TrCel6A) is a cellobiohydrolase that hydrolyzes crystalline cellulose into cellobiose. Here we directly observed the reaction cycle (binding, surface movement, and dissociation) of single-molecule intact TrCel6A, isolated catalytic domain (CD), cellulose-binding module (CBM), and CBM and linker (CBM-linker) on crystalline cellulose I

Indexed as

CelluloseCellulose 1,4-beta-CellobiosidaseFungal ProteinsProtein DomainsTrichodermaCelluloseCellulose 1,4-beta-CellobiosidaseFungal Proteinscellulasecelluloseenzyme kineticsenzyme mechanismmicroscopic imagingmolecular motorprocessivityprotein domainsingle-molecule biophysics

Identifiers

PMID27609516
PMCPMC5077181
OpenAlexW2515936062

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.