Evidence map›Paper›PMID 31666327›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2019

The dissociation mechanism of processive cellulases.

Josh V Vermaas, Riin Kont, Gregg T Beckham, Michael F Crowley, Mikael Gudmundsson, Mats Sandgren, Jerry Ståhlberg, Priit Väljamäe, Brandon C Knott

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
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  5. Article
  6. Single-molecule tracking reveals dual front door/back door inhibition of Cel7A cellulase by its product cellobiose.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023
    Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
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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 2 institutions in 2 countries.

Josh V VermaasBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.ORCID 0000-0003-3139-6469
Riin KontInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia 51010.
Gregg T BeckhamNational Bioenergy Center, National Renewable Energy Laboratory, Golden, CO 80401.ORCID 0000-0002-3480-212X
Michael F CrowleyBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401.
Mikael GudmundssonDepartment of Molecular Sciences, Swedish University of Agricultural Sciences, SE-75651 Uppsala, Sweden.
Mats SandgrenDepartment of Molecular Sciences, Swedish University of Agricultural Sciences, SE-75651 Uppsala, Sweden.
Jerry StåhlbergDepartment of Molecular Sciences, Swedish University of Agricultural Sciences, SE-75651 Uppsala, Sweden.
Priit VäljamäeInstitute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia 51010.ORCID 0000-0002-1035-9493
Brandon C KnottBiosciences Center, National Renewable Energy Laboratory, Golden, CO 80401; brandon.knott@nrel.gov.
National Renewable Energy Laboratory · USUniversity of Tartu · EE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cellulase enzymes deconstruct recalcitrant cellulose into soluble sugars, making them a biocatalyst of biotechnological interest for use in the nascent lignocellulosic bioeconomy. Cellobiohydrolases (CBHs) are cellulases capable of liberating many sugar molecules in a processive manner without dissociating from the substrate. Within the complete processive cycle of CBHs, dissociation from the cellulose substrate is rate limiting, but the molecular mechanism of this step is unknown. Here, we present a direct comparison of potential molecular mechanisms for dissociation via Hamiltonian replica exchange molecular dynamics of the model fungal CBH,

Indexed as

Binding SitesCatalytic DomainCellulasesCelluloseFungal ProteinsKineticsMolecular Dynamics SimulationTrichodermaCellulasesCelluloseFungal Proteinsbiofuelscellulasescrystal structuremolecular mechanismmolecular simulation

Identifiers

PMID31666327
PMCPMC6859361
OpenAlexW2982675097

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.