Evidence map›Paper›PMID 27353064›Full record

ArticleProteins2016

Novel proteases from the genome of the carnivorous plant Drosera capensis: Structural prediction and comparative analysis.

Carter T Butts, Jan C Bierma, Rachel W Martin

Open access · greenAbstract readComparative Study
In one paragraph

Article in Proteins, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
11.7field-weighted citation impact, top 2% 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

24 citing papers in PubMed, 43 citations in OpenAlex.

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  20. Long-read sequencing uncovers the adaptive topography of a carnivorous plant genome.Proceedings of the National Academy of Sciences of the United States of America · 2017
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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

3 authors at 2 institutions in 1 country.

Carter T ButtsDepartment of Electrical Engineering and Computer Science, UC Irvine, Irvine, California, 92697. rwmartin@uci.edu.
Jan C BiermaDepartment of Molecular Biology and Biochemistry, UC Irvine, Irvine, California, 92697.
Rachel W MartinDepartment of Molecular Biology and Biochemistry, UC Irvine, Irvine, California, 92697. buttsc@uci.edu.
UC Irvine Health · USUniversity of California, Irvine · US

Funding

Univ.of Calif., Irvine Cancer Center Support GrantP30CA062203 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI Melanie Funes · 1994 to 2026
$57.9M
PacBio RS Single Molecule, Real-Time (SMRT) DNA SequencerS10OD010794 · OD · UNIVERSITY OF CALIFORNIA-IRVINE · PI SANDMEYER, SUZANNE · 2012 to 2012
$600k
High-Throughput DNA SequencerS10OD021718 · OD · UNIVERSITY OF CALIFORNIA-IRVINE · PI SANDMEYER, SUZANNE · 2016 to 2016
$600k
High Throughput DNA SequencerS10RR025496 · NCRR · UNIVERSITY OF CALIFORNIA-IRVINE · PI SANDMEYER, SUZANNE · 2009 to 2009
$500k
NCI NIH HHS P30 CA062203NCRR NIH HHS S10 RR025496NIH HHS S10 OD010794NIH HHS S10 OD021718
6 · The paper itself

Abstract

In his 1875 monograph on insectivorous plants, Darwin described the feeding reactions of Drosera flypaper traps and predicted that their secretions contained a "ferment" similar to mammalian pepsin, an aspartic protease. Here we report a high-quality draft genome sequence for the cape sundew, Drosera capensis, the first genome of a carnivorous plant from order Caryophyllales, which also includes the Venus flytrap (Dionaea) and the tropical pitcher plants (Nepenthes). This species was selected in part for its hardiness and ease of cultivation, making it an excellent model organism for further investigations of plant carnivory. Analysis of predicted protein sequences yields genes encoding proteases homologous to those found in other plants, some of which display sequence and structural features that suggest novel functionalities. Because the sequence similarity to proteins of known structure is in most cases too low for traditional homology modeling, 3D structures of representative proteases are predicted using comparative modeling with all-atom refinement. Although the overall folds and active residues for these proteins are conserved, we find structural and sequence differences consistent with a diversity of substrate recognition patterns. Finally, we predict differences in substrate specificities using in silico experiments, providing targets for structure/function studies of novel enzymes with biological and technological significance. Proteins 2016; 84:1517-1533. © 2016 Wiley Periodicals, Inc.

Indexed as

Genome, PlantAmino Acid SequenceCarnivoryCatalytic DomainContig MappingDroseraDroseraceaeHigh-Throughput Nucleotide SequencingMolecular Docking SimulationMolecular Sequence AnnotationPeptide HydrolasesPhylogenyPlant ProteinsProtein DomainsProtein FoldingProtein Structure, SecondaryPeptide HydrolasesPlant Proteinsaspartic proteasecarnivorous plantcysteine proteasedigestive enzymeenzyme substrate specificitygenome sequencemolecular dockingplant-specific insertprotein structure predictionRosetta

Identifiers

PMID27353064
PMCPMC5026580
OpenAlexW2474334848

What OpenQuestion holds

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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.