Evidence map›Paper›PMID 25527502›Full record

ArticleThe Journal of biological chemistry2015

The use of carbohydrate binding modules (CBMs) to monitor changes in fragmentation and cellulose fiber surface morphology during cellulase- and Swollenin-induced deconstruction of lignocellulosic substrates.

Keith Gourlay, Jinguang Hu, Valdeir Arantes, Merja Penttilä, Jack N Saddler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  4. CombinedFrontiers in bioengineering and biotechnology · 2019
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  5. Review
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  13. Bacterial expansins and related proteins from the world of microbes.Applied microbiology and biotechnology · 2015
    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

5 authors at 2 institutions in 2 countries.

Keith GourlayFrom the Forest Products Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada and.
Jinguang HuFrom the Forest Products Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada and.
Valdeir ArantesFrom the Forest Products Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada and.
Merja Penttiläthe VTT Technical Research Centre of Finland, Metallimiehenkuja 2 (Espoo), FI-02044 VTT, Finland.
Jack N SaddlerFrom the Forest Products Biotechnology/Bioenergy Group, Department of Wood Science, Faculty of Forestry, University of British Columbia, Vancouver, British Columbia V6T 1Z4, Canada and jack.saddler@ubc.ca.
University of British Columbia · CAVTT Technical Research Centre of Finland · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Although the actions of many of the hydrolytic enzymes involved in cellulose hydrolysis are relatively well understood, the contributions that amorphogenesis-inducing proteins might contribute to cellulose deconstruction are still relatively undefined. Earlier work has shown that disruptive proteins, such as the non-hydrolytic non-oxidative protein Swollenin, can open up and disaggregate the less-ordered regions of lignocellulosic substrates. Within the cellulosic fraction, relatively disordered, amorphous regions known as dislocations are known to occur along the length of the fibers. It was postulated that Swollenin might act synergistically with hydrolytic enzymes to initiate biomass deconstruction within these dislocation regions. Carbohydrate binding modules (CBMs) that preferentially bind to cellulosic substructures were fluorescently labeled. They were imaged, using confocal microscopy, to assess the distribution of crystalline and amorphous cellulose at the fiber surface, as well as to track changes in surface morphology over the course of enzymatic hydrolysis and fiber fragmentation. Swollenin was shown to promote targeted disruption of the cellulosic structure at fiber dislocations.

Indexed as

CellulaseCelluloseLigninMicroscopy, ConfocalProtein BindingX-Ray DiffractionCellulaseCelluloseLigninlignocelluloseAmorphogenesisCarbohydrate Binding Modules (CBMs)CellulaseCelluloseCellulose Binding ModulesConfocal MicroscopyEnzymeFiber DislocationsFragmentationFungiMicrobiologySwollenin

Identifiers

PMID25527502
PMCPMC4317003
OpenAlexW2051092819

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.