Evidence map›Paper›PMID 30385768›Full record

ArticleScientific reports2018

Ginsentides: Cysteine and Glycine-rich Peptides from the Ginseng Family with Unusual Disulfide Connectivity.

James P Tam, Giang K T Nguyen, Shining Loo, Shujing Wang, Daiwen Yang, Antony Kam

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 39 citations in OpenAlex.

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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 2 institutions in 1 country.

James P TamSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore, Singapore. JPTam@ntu.edu.sg.
Giang K T NguyenSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore, Singapore.
Shining LooSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore, Singapore.
Shujing WangSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore, Singapore.
Daiwen YangDepartment of Biological Sciences, National University of Singapore, 14 Science Drive 4, 117543, Singapore, Singapore.
Antony KamSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551, Singapore, Singapore.
Nanyang Technological University · SGNational University of Singapore · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ginseng, a popular and valuable traditional medicine, has been used for centuries to maintain health and treat disease. Here we report the discovery and characterization of ginsentides, a novel family of cysteine and glycine-rich peptides derived from the three most widely-used ginseng species: Panax ginseng, Panax quinquefolius, and Panax notoginseng. Using proteomic and transcriptomic methods, we identified 14 ginsentides, TP1-TP14 which consist of 31-33 amino acids and whose expression profiles are species- and tissues-dependent. Ginsentides have an eight-cysteine motif typical of the eight-cysteine-hevein-like peptides (8C-HLP) commonly found in medicinal herbs, but lack a chitin-binding domain. Transcriptomic analysis showed that the three-domain biosynthetic precursors of ginsentides differ from known 8C-HLP precursors in architecture and the absence of a C-terminal protein-cargo domain. A database search revealed an additional 50 ginsentide-like precursors from both gymnosperms and angiosperms. Disulfide mapping and structure determination of the ginsentide TP1 revealed a novel disulfide connectivity that differs from the 8C-HLPs. The structure of ginsentide TP1 is highly compact, with the N- and C-termini topologically fixed by disulfide bonds to form a pseudocyclic structure that confers resistance to heat, proteolysis, and acid and serum-mediated degradation. Together, our results expand the chemical space of natural products found in ginseng and highlight the occurrence, distribution, disulfide connectivity, and precursor architectures of cysteine- and glycine-rich ginsentides as a class of novel non-chitin-binding, non-cargo-carrying 8C-HLPs.

Indexed as

Antimicrobial Cationic PeptidesCysteineDisulfidesGene Expression Regulation, PlantGlycineMolecular StructurePanaxPanax notoginsengPeptidesPlant LectinsProteomeTranscriptomeAntimicrobial Cationic PeptidesCysteineDisulfidesGlycineheveinPeptidesPlant LectinsProteome

Identifiers

PMID30385768
PMCPMC6212409
OpenAlexW2898166047

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LicenceCC BY
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Registered trials

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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.