Evidence map›Paper›PMID 29213319›Full record

ArticleBiotechnology for biofuels2017

Natural diversity of glycoside hydrolase family 48 exoglucanases: insights from structure.

Roman Brunecky, Markus Alahuhta, Deanne W Sammond, Qi Xu, Mo Chen, David B Wilson, John W Brady, Michael E Himmel, Yannick J Bomble, Vladimir V Lunin

Open access · goldAbstract read
In one paragraph

Article in Biotechnology for biofuels, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

3 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Metabolic engineering ofBiotechnology for biofuels · 2019
    Article
  3. EngineeringBiotechnology for biofuels · 2019
    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

10 authors at 2 institutions in 1 country.

Roman BruneckyBiosciences Center, National Renewable Energy Laboratory, 15013 Denver West Parkway, Golden, CO 80401 USA.
Markus AlahuhtaBiosciences Center, National Renewable Energy Laboratory, 15013 Denver West Parkway, Golden, CO 80401 USA.
Deanne W SammondBiosciences Center, National Renewable Energy Laboratory, 15013 Denver West Parkway, Golden, CO 80401 USA.
Qi XuBiosciences Center, National Renewable Energy Laboratory, 15013 Denver West Parkway, Golden, CO 80401 USA.
Mo ChenDepartment of Food Science, Cornell University, Ithaca, NY USA.
David B WilsonBiochemistry, Molecular and Cell Biology, Cornell University, Ithaca, NY USA.
John W BradyDepartment of Food Science, Cornell University, Ithaca, NY USA.
Michael E HimmelBiosciences Center, National Renewable Energy Laboratory, 15013 Denver West Parkway, Golden, CO 80401 USA.
Yannick J BombleBiosciences Center, National Renewable Energy Laboratory, 15013 Denver West Parkway, Golden, CO 80401 USA.ORCID 0000-0001-7624-8000
Vladimir V LuninBiosciences Center, National Renewable Energy Laboratory, 15013 Denver West Parkway, Golden, CO 80401 USA.
National Laboratory of the Rockies · USCornell University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycoside hydrolase (GH) family 48 is an understudied and increasingly important exoglucanase family found in the majority of bacterial cellulase systems. Moreover, many thermophilic enzyme systems contain GH48 enzymes. Deletion of GH48 enzymes in these microorganisms results in drastic reduction in biomass deconstruction. Surprisingly, given their importance for these microorganisms, GH48s have intrinsically low cellulolytic activity but even in low ratios synergize greatly with GH9 endoglucanases. In this study, we explore the structural and enzymatic diversity of these enzymes across a wide range of temperature optima. We have crystallized one new GH48 module from

Indexed as

CellulaseCircular dichroismGH48Molecular modelingX-ray crystallography

Identifiers

PMID29213319
PMCPMC5707792
OpenAlexW2770191769

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.