Evidence map›Paper›PMID 27748440›Full record

ArticleScientific reports2016

Binding of cellulose binding modules reveal differences between cellulose substrates.

Suvi Arola, Markus B Linder

Abstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
–field-weighted citation impact
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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Carbohydrate-binding modules enhance HThe Journal of biological chemistry · 2024
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. 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

2 authors.

Suvi ArolaSchool of Science, Aalto University, P. O. Box 11100, FI-00076, Aalto, Finland.
Markus B LinderSchool of Chemical Technology, Aalto University, P.O. Box 16100, FI-00076, Aalto, Finland.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The interaction between cellulase enzymes and their substrates is of central importance to several technological and scientific challenges. Here we report that the binding of cellulose binding modules (CBM) from Trichoderma reesei cellulases Cel6A and Cel7A show a major difference in how they interact with substrates originating from wood compared to bacterial cellulose. We found that the CBM from TrCel7A recognizes the two substrates differently and as a consequence shows an unexpected way of binding. We show that the substrate has a large impact on the exchange rate of the studied CBM, and moreover, CBM-TrCel7A seems to have an additional mode of binding on wood derived cellulose but not on cellulose originating from bacterial source. This mode is not seen in double CBM (DCBM) constructs comprising both CBM-TrCel7A and CBM-TrCel6A. The linker length of DCBMs affects the binding properties, and slows down the exchange rates of the proteins and thus, can be used to analyze the differences between the single CBM. These results have impact on the cellulase research and offer new understanding on how these industrially relevant enzymes act.

Indexed as

Binding SitesCatalytic DomainCellulaseCelluloseCellulose 1,4-beta-CellobiosidaseEndo-1,4-beta XylanasesFungal ProteinsProtein BindingSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationStructure-Activity RelationshipSubstrate SpecificityThermodynamicsTrichodermaCellulaseCelluloseCellulose 1,4-beta-CellobiosidaseEndo-1,4-beta XylanasesFungal Proteins

Identifiers

PMID27748440
PMCPMC5066208

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Registered trials

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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.