Evidence map›Paper›PMID 28900033›Full record

ArticleThe Journal of biological chemistry2017

High-resolution structure of a lytic polysaccharide monooxygenase from

Henrik Hansson, Saeid Karkehabadi, Nils Mikkelsen, Nicholai R Douglas, Steve Kim, Anna Lam, Thijs Kaper, Brad Kelemen, Katlyn K Meier, Stephen M Jones and 2 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 76 citations in OpenAlex.

  1. Article
  2. Article
  3. Carbohydrate-binding modules enhance HThe Journal of biological chemistry · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Lytic Polysaccharide Monooxygenase fromInternational journal of molecular sciences · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Kinetic analysis of amino acid radicals formed in HProceedings of the National Academy of Sciences of the United States of America · 2020
    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

12 authors at 3 institutions in 2 countries.

Henrik HanssonFrom the Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, P.O. Box 7015, SE-750 07 Uppsala, Sweden.
Saeid KarkehabadiFrom the Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, P.O. Box 7015, SE-750 07 Uppsala, Sweden.
Nils MikkelsenFrom the Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, P.O. Box 7015, SE-750 07 Uppsala, Sweden.
Nicholai R DouglasDuPont Industrial Biosciences, Palo Alto, California 94304, and.
Steve KimDuPont Industrial Biosciences, Palo Alto, California 94304, and.
Anna LamDuPont Industrial Biosciences, Palo Alto, California 94304, and.
Thijs KaperDuPont Industrial Biosciences, Palo Alto, California 94304, and.
Brad KelemenDuPont Industrial Biosciences, Palo Alto, California 94304, and.
Katlyn K Meierthe Department of Chemistry, Stanford University, Stanford, California 94305.
Stephen M Jonesthe Department of Chemistry, Stanford University, Stanford, California 94305.
Edward I Solomonthe Department of Chemistry, Stanford University, Stanford, California 94305 edward.solomon@stanford.edu.
Mats SandgrenFrom the Department of Chemistry and Biotechnology, Swedish University of Agricultural Sciences, P.O. Box 7015, SE-750 07 Uppsala, Sweden, mats.sandgren@slu.se.
DuPont (United States) · USSwedish University of Agricultural Sciences · SEStanford University · US

Funding

Structure/Function Correlations Over Copper EnzymesR01DK031450 · NIDDK · STANFORD UNIVERSITY · PI EDWARD I SOLOMON · 1986 to 2026
$8.7M
Spectroscopic and computational characterization of Cu/O2 species in Cu enzymesF32GM116240 · NIGMS · STANFORD UNIVERSITY · PI MEIER, KATLYN KELLI · 2015 to 2017
$162k
NIDDK NIH HHS R01 DK031450NIGMS NIH HHS F32 GM116240
6 · The paper itself

Abstract

For decades, the enzymes of the fungus

Indexed as

Amino Acid SequenceBinding SitesCatalytic DomainCelluloseCrystallography, X-RayHypocreaMixed Function OxygenasesModels, MolecularPolysaccharidesProtein ConformationSequence AlignmentCelluloseMixed Function OxygenasesPolysaccharidesauxiliary activity family 9 (AA9)electron paramagnetic resonance (EPR)enzyme mechanismenzyme structureHypocrea jecorinalytic polysaccharide monooxygenase (LPMO)X-ray crystallography

Identifiers

PMID28900033
PMCPMC5704490
OpenAlexW2755701752

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.