Evidence map›Paper›PMID 30084398›Full record

ArticleActa crystallographica. Section F, Structural biology communications2018

Structure of a Talaromyces pinophilus GH62 arabinofuranosidase in complex with AraDNJ at 1.25 Å resolution.

Olga V Moroz, Lukasz F Sobala, Elena Blagova, Travis Coyle, Wei Peng, Kristian B R Mørkeberg Krogh, Keith A Stubbs, Keith S Wilson, Gideon J Davies

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Article
  2. Carbohydrate structure hits the groove.Acta crystallographica. Section F, Structural biology communications · 2018
    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

9 authors at 3 institutions in 3 countries.

Olga V MorozYork Structural Biology Laboratory, Department of Chemistry, The University of York, York YO10 5DD, England.
Lukasz F SobalaYork Structural Biology Laboratory, Department of Chemistry, The University of York, York YO10 5DD, England.
Elena BlagovaYork Structural Biology Laboratory, Department of Chemistry, The University of York, York YO10 5DD, England.
Travis CoyleSchool of Molecular Sciences, The University of Western Australia (M313), 35 Stirling Highway, Crawley, WA 6009, Australia.
Wei PengFungal Diversity, Novozymes A/S, China Headquarters, 14 Xinxi Road, Shangdi Zone, Haidian District, Beijing 100085, People's Republic of China.
Kristian B R Mørkeberg KroghProtein Biochemistry and Stability, Novozymes A/S, Krogshøjvej 36, 2880 Bagsværd, Denmark.
Keith A StubbsSchool of Molecular Sciences, The University of Western Australia (M313), 35 Stirling Highway, Crawley, WA 6009, Australia.
Keith S WilsonYork Structural Biology Laboratory, Department of Chemistry, The University of York, York YO10 5DD, England.
Gideon J DaviesYork Structural Biology Laboratory, Department of Chemistry, The University of York, York YO10 5DD, England.ORCID 0000-0002-7343-776X
University of York · GBNovozymes (Denmark) · DKThe University of Western Australia · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The enzymatic hydrolysis of complex plant biomass is a major societal goal of the 21st century in order to deliver renewable energy from nonpetroleum and nonfood sources. One of the major problems in many industrial processes, including the production of second-generation biofuels from lignocellulose, is the presence of `hemicelluloses' such as xylans which block access to the cellulosic biomass. Xylans, with a polymeric β-1,4-xylose backbone, are frequently decorated with acetyl, glucuronyl and arabinofuranosyl `side-chain' substituents, all of which need to be removed for complete degradation of the xylan. As such, there is interest in side-chain-cleaving enzymes and their action on polymeric substrates. Here, the 1.25 Å resolution structure of the Talaromyces pinophilus arabinofuranosidase in complex with the inhibitor AraDNJ, which binds with a K

Indexed as

CrystallizationEnzyme InhibitorsGlycoside HydrolasesProtein Structure, SecondaryProtein Structure, TertiaryRecombinant ProteinsTalaromycesalpha-N-arabinofuranosidaseEnzyme InhibitorsGlycoside HydrolasesRecombinant Proteinsarabinofuranosidasebiofuelsenzyme inhibitorsenzymesglycosidasesTalaromyces pinophilus

Identifiers

PMID30084398
PMCPMC6096477
OpenAlexW2884034665

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.