Evidence map›Paper›PMID 27991569›Full record

ArticleScientific reports2016

Identification and Characterization of Roseltide, a Knottin-type Neutrophil Elastase Inhibitor Derived from Hibiscus sabdariffa.

Shining Loo, Antony Kam, Tianshu Xiao, Giang K T Nguyen, Chuan Fa Liu, James P Tam

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 46 citations in OpenAlex.

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  6. Peptide hormones in plants.Molecular horticulture · 2025
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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

6 authors at 1 institution in 1 country.

Shining LooSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
Antony KamSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
Tianshu XiaoSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
Giang K T NguyenSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
Chuan Fa LiuSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
James P TamSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore.
Nanyang Technological University · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Plant knottins are of therapeutic interest due to their high metabolic stability and inhibitory activity against proteinases involved in human diseases. The only knottin-type proteinase inhibitor against porcine pancreatic elastase was first identified from the squash family in 1989. Here, we report the identification and characterization of a knottin-type human neutrophil elastase inhibitor from Hibiscus sabdariffa of the Malvaceae family. Combining proteomic and transcriptomic methods, we identified a panel of novel cysteine-rich peptides, roseltides (rT1-rT8), which range from 27 to 39 residues with six conserved cysteine residues. The 27-residue roseltide rT1 contains a cysteine spacing and amino acid sequence that is different from the squash knottin-type elastase inhibitor. NMR analysis demonstrated that roseltide rT1 adopts a cystine-knot fold. Transcriptome analyses suggested that roseltides are bioprocessed by asparagine endopeptidases from a three-domain precursor. The cystine-knot structure of roseltide rT1 confers its high resistance against degradation by endopeptidases, 0.2 N HCl, and human serum. Roseltide rT1 was shown to inhibit human neutrophil elastase using enzymatic and pull-down assays. Additionally, roseltide rT1 ameliorates neutrophil elastase-stimulated cAMP accumulation in vitro. Taken together, our findings demonstrate that roseltide rT1 is a novel knottin-type neutrophil elastase inhibitor with therapeutic potential for neutrophil elastase associated diseases.

Indexed as

A549 CellsAmino Acid SequenceAnimalsAsparaginyl EndopeptidaseCell LineCell Line, TumorCHO CellsCricetulusCyclic AMPCysteineCysteine EndopeptidasesCystine-Knot MiniproteinsHibiscusHumansLeukocyte ElastaseNeutrophilsAsparaginyl EndopeptidaseCyclic AMPCysteineCysteine EndopeptidasesCystine-Knot MiniproteinsLeukocyte ElastasePeptide HydrolasesProteinase Inhibitory Proteins, SecretorySerine Proteinase Inhibitors

Identifiers

PMID27991569
PMCPMC5171801
OpenAlexW2562396479

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.