Evidence map›Paper›PMID 34938409›Full record

ArticleComputational and structural biotechnology journal2021

The bone-degrading enzyme machinery: From multi-component understanding to the treatment of residues from the meat industry.

Laura Fernandez-Lopez, Sergio Sanchez-Carrillo, Antonio García-Moyano, Erik Borchert, David Almendral, Sandra Alonso, Isabel Cea-Rama, Noa Miguez, Øivind Larsen, Johannes Werner and 7 more

Open access · goldAbstract read
In one paragraph

Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 40% 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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. 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

17 authors at 7 institutions in 4 countries.

Laura Fernandez-LopezCSIC, Institute of Catalysis, 28049 Madrid, Spain.
Sergio Sanchez-CarrilloCSIC, Institute of Catalysis, 28049 Madrid, Spain.
Antonio García-MoyanoNORCE Norwegian Research Centre, P.O. Box 22 Nygårdstangen, 5838 Bergen, Norway.
Erik BorchertGEOMAR Helmholtz Centre for Ocean Research, 24148 Kiel, Germany.
David AlmendralCSIC, Institute of Catalysis, 28049 Madrid, Spain.
Sandra AlonsoCSIC, Institute of Catalysis, 28049 Madrid, Spain.
Isabel Cea-RamaInstitute of Physical Chemistry "Rocasolano", CSIC, 28006 Madrid, Spain.
Noa MiguezCSIC, Institute of Catalysis, 28049 Madrid, Spain.
Øivind LarsenNORCE Norwegian Research Centre, P.O. Box 22 Nygårdstangen, 5838 Bergen, Norway.
Johannes WernerHigh Performance and Cloud Computing Group, Zentrum für Datenverarbeitung (ZDV), Eberhard Karls University of Tübingen, 72074 Tübingen, Germany.
Kira S MakarovaNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, 20892 MD, USA.
Francisco J PlouCSIC, Institute of Catalysis, 28049 Madrid, Spain.
Thomas G DahlgrenNORCE Norwegian Research Centre, P.O. Box 22 Nygårdstangen, 5838 Bergen, Norway.
Julia Sanz-AparicioInstitute of Physical Chemistry "Rocasolano", CSIC, 28006 Madrid, Spain.
Ute HentschelGEOMAR Helmholtz Centre for Ocean Research, 24148 Kiel, Germany.
Gro Elin Kjæreng BjergaNORCE Norwegian Research Centre, P.O. Box 22 Nygårdstangen, 5838 Bergen, Norway.
Manuel FerrerCSIC, Institute of Catalysis, 28049 Madrid, Spain.
Instituto de Catálisis y Petroleoquímica · ESNORCE Research AS · NOInstituto de Química Física Blas Cabrera · ESChristian-Albrechts-Universität zu Kiel · DEGEOMAR Helmholtz Centre for Ocean Research Kiel · DENational Institutes of Health · USUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many microorganisms feed on the tissue and recalcitrant bone materials from dead animals, however little is known about the collaborative effort and characteristics of their enzymes. In this study, microbial metagenomes from symbionts of the marine bone-dwelling worm

Indexed as

Bone degradationBone microbiomeCollagenaseCOLL, collagenases (peptidases families U32 and M9)DNS, dinitrosalicylic acidFALGPA, N-[3-(2-furyl)acryloyl]-L-leucyl-glycyl-L-prolyl-L-alanineGlycosidaseHEPES, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acidHMM, Hidden Markov ModelsHPAEC-PAD, High performance anion-exchange chromatography with pulsed amperometric detectionMAG, Metagenome Assembled GenomeMetagenomicsNeu5Ac-GM2, N-acetyl-galactose-β-1,4-[N-acetylneuraminidate-α-2,3-]-galactose-β-1,4-glucose-α-ceramideNeu5Ac-GM3, Neu5Acα2-3Galβ1-4Glcβ1-ceramideNi-NTA, nickel-nitrilotriacetic acidOsedax mucoflorisPEPT, peptidase (families S1, S8, S53, M61)pNP-NAβGal, pNP-N-acetyl-β-galactosaminidepNP-NAβGlu, pNP-N-acetyl-β-glucosaminidepNP-Neu5Ac, 2-O-(p-nitrophenyl)-α-acetylneuraminic acidpNP-sugars, p-nitrophenyl-sugarspNP-αAFur, pNP-α-arabinofuranosidepNP-αAPyr, pNP-α-arabinopyranosidepNP-αFuc, pNP-α-fucopyranosidepNP-αGal, pNP-α-galactopyranosidepNP-αGlu, pNP-α-glucopyranosidepNP-αMal, pNP-α-maltosidepNP-αMan, pNP-α-mannopyranosidepNP-αRham, pNP-α-rhamnopyranosidepNP-αXyl, pNP-α-xylopyranosidepNP-βAPyr, pNP-β-arabinopyranosidepNP-βCel, pNP-β-cellobiosidepNP-βFuc, pNP-β-fucopyranosidepNP-βGal, pNP-β-galactopyranosidepNP-βGlucur, pNP-β-glucuronidepNP-βGlu, pNP-β-glucopyranosidepNP-βLac, pNP-β-lactosidepNP-βMan, pNP-β-mannopyranosidepNP-βXyl, pNP-β-xylopyranosideRHAM, α-rhamnosidasesSIAL, sialidasesαFUC, α-fucosidasesαGAL, α-galactosidasesαMAN, α-mannosidasesαNAG, α-N-acetyl-hexosaminidasesβGAL, β-galactosidasesβGLU, β-glucosidasesβNAG, β-N-acetyl-hexosaminidases

Identifiers

PMID34938409
PMCPMC8645421
OpenAlexW3216137819

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.