Evidence map›Paper›PMID 20359453›Full record

ReviewAdvances in applied microbiology2010

Thermostable enzymes as biocatalysts in the biofuel industry.

Carl J Yeoman, Yejun Han, Dylan Dodd, Charles M Schroeder, Roderick I Mackie, Isaac K O Cann

Abstract readReview
In one paragraph

Review in Advances in applied microbiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing 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

96 citing papers in PubMed.

  1. Review
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  6. A Stochastic Landscape Approach for Protein Folding State Classification.Journal of chemical theory and computation · 2024
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36 more citing papers are in PubMed but not listed here.

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

6 authors.

Carl J YeomanInstitute for Genomic Biology, University of Illinois, Urbana, Illinois, USA.
Yejun Han
Dylan Dodd
Charles M Schroeder
Roderick I Mackie
Isaac K O Cann

Funding

Biochemical Characterization of Specificity for Family 3 Glycoside HydrolasesF30DK084726 · NIDDK · UNIVERSITY OF ILLINOIS AT URBANA-CHAMPAIGN · PI DODD, DYLAN · 2009 to 2013
$170k
NIDDK NIH HHS F30 DK084726
6 · The paper itself

Abstract

Lignocellulose is the most abundant carbohydrate source in nature and represents an ideal renewable energy source. Thermostable enzymes that hydrolyze lignocellulose to its component sugars have significant advantages for improving the conversion rate of biomass over their mesophilic counterparts. We review here the recent literature on the development and use of thermostable enzymes for the depolymerization of lignocellulosic feedstocks for biofuel production. Furthermore, we discuss the protein structure, mechanisms of thermostability, and specific strategies that can be used to improve the thermal stability of lignocellulosic biocatalysts.

Indexed as

BiocatalysisBiofuelsEnzyme StabilityHot TemperatureBiomassEsterasesGlycoside HydrolasesLigninProtein ConformationBiofuelsEsterasesGlycoside HydrolasesLigninlignocellulose

Identifiers

PMID20359453
PMCPMC4561533

What OpenQuestion holds

Textmetadata
LicenceTDM
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.