ArticleThe Journal of biological chemistry2019
Insights into an unusual Auxiliary Activity 9 family member lacking the histidine brace motif of lytic polysaccharide monooxygenases.
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 11 papers.
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.
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.
Who cites it
11 citing papers in PubMed, 39 citations in OpenAlex.
- A Molecular Mechanism for the Reduction of the Cu Site in Lytic Polysaccharide Monooxygenases by Phenol Reductants.JACS Au · 2025Article
- Anions and citrate inhibit LsAA9A, a lytic polysaccharide monooxygenase (LPMO).The FEBS journal · 2025Article
- Functional characterization of fungal lytic polysaccharide monooxygenases for cellulose surface oxidation.Biotechnology for biofuels and bioproducts · 2023Article
- Insights into peculiar fungal LPMO family members holding a short C-terminal sequence reminiscent of phosphate binding motifs.Scientific reports · 2023Article
- Orchestrating copper binding: structure and variations on the cupredoxin fold.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- C-H Bond Cleavage by Bioinspired Nonheme Metal Complexes.Inorganic chemistry · 2021Review
- Four cellulose-active lytic polysaccharide monooxygenases from Cellulomonas species.Biotechnology for biofuels · 2021Article
- LPMOInternational journal of molecular sciences · 2020Article
- Functional characterization of cellulose-degrading AA9 lytic polysaccharide monooxygenases and their potential exploitation.Applied microbiology and biotechnology · 2020Review
- Profile Comparer Extended: phylogeny of lytic polysaccharide monooxygenase families using profile hidden Markov model alignments.F1000Research · 2019Article
- Identification of the molecular determinants driving the substrate specificity of fungal lytic polysaccharide monooxygenases (LPMOs).The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
18 authors at 10 institutions in 5 countries.
Funding
Abstract
Lytic polysaccharide monooxygenases (LPMOs) are redox-enzymes involved in biomass degradation. All characterized LPMOs possess an active site of two highly conserved histidine residues coordinating a copper ion (the histidine brace), which are essential for LPMO activity. However, some protein sequences that belong to the AA9 LPMO family display a natural N-terminal His to Arg substitution (Arg-AA9). These are found almost entirely in the phylogenetic fungal class
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.