Evidence map›Paper›PMID 31656228›Full record

ArticleThe Journal of biological chemistry2019

Engineering chitinolytic activity into a cellulose-active lytic polysaccharide monooxygenase provides insights into substrate specificity.

Marianne Slang Jensen, Geir Klinkenberg, Bastien Bissaro, Piotr Chylenski, Gustav Vaaje-Kolstad, Hans Fredrik Kvitvang, Guro Kruge Nærdal, Håvard Sletta, Zarah Forsberg, Vincent G H Eijsink

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

15 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. A single-domain expansin-like protein fromProceedings of the National Academy of Sciences of the United States of America · 2026
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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

10 authors at 2 institutions in 1 country.

Marianne Slang JensenFaculty of Chemistry, Biotechnology and Food Science, NMBU-Norwegian University of Life Sciences, NO-1432 Ås, Norway.
Geir KlinkenbergSINTEF Industry, Department of Biotechnology and Nanomedicine, NO-7465 Trondheim, Norway.
Bastien BissaroFaculty of Chemistry, Biotechnology and Food Science, NMBU-Norwegian University of Life Sciences, NO-1432 Ås, Norway.
Piotr ChylenskiFaculty of Chemistry, Biotechnology and Food Science, NMBU-Norwegian University of Life Sciences, NO-1432 Ås, Norway.
Gustav Vaaje-KolstadFaculty of Chemistry, Biotechnology and Food Science, NMBU-Norwegian University of Life Sciences, NO-1432 Ås, Norway.
Hans Fredrik KvitvangSINTEF Industry, Department of Biotechnology and Nanomedicine, NO-7465 Trondheim, Norway.
Guro Kruge NærdalSINTEF Industry, Department of Biotechnology and Nanomedicine, NO-7465 Trondheim, Norway.
Håvard SlettaSINTEF Industry, Department of Biotechnology and Nanomedicine, NO-7465 Trondheim, Norway.
Zarah ForsbergFaculty of Chemistry, Biotechnology and Food Science, NMBU-Norwegian University of Life Sciences, NO-1432 Ås, Norway zarah.forsberg@nmbu.no.
Vincent G H EijsinkFaculty of Chemistry, Biotechnology and Food Science, NMBU-Norwegian University of Life Sciences, NO-1432 Ås, Norway vincent.eijsink@nmbu.no.ORCID 0000-0002-9220-8743
Norwegian University of Life Sciences · NOSINTEF · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lytic polysaccharide monooxygenases (LPMOs) catalyze oxidative cleavage of recalcitrant polysaccharides such as cellulose and chitin and play an important role in the enzymatic degradation of biomass. Although it is clear that these monocopper enzymes have extended substrate-binding surfaces for interacting with their fibrous substrates, the structural determinants of LPMO substrate specificity remain largely unknown. To gain additional insight into substrate specificity in LPMOs, here we generated a mutant library of a cellulose-active family AA10 LPMO from

Indexed as

Protein EngineeringCelluloseChitinMixed Function OxygenasesModels, MolecularPolysaccharidesStreptomyces coelicolorSubstrate SpecificityCelluloseChitinMixed Function OxygenasesPolysaccharidesauxiliary activity family 10 (AA10)carbohydrate-active enzymecellulosechitinglycosidic bond cleavagehigh-throughput screeninglytic polysaccharide monooxygenase (LPMO)protein stabilityrenewable energysubstrate specificity

Identifiers

PMID31656228
PMCPMC6916511
OpenAlexW2982477590

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.