ArticleCurrent microbiology2016
Application of Differential Proteomic Analysis to Authenticate Ophiocordyceps sinensis.
Article in Current microbiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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.
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Who cites it
6 citing papers in PubMed.
- Chemometric-Guided Approaches for Profiling and Authenticating Botanical Materials.Frontiers in nutrition · 2021Review
- Proteome sequencing and analysis of Ophiocordyceps sinensis at different culture periods.BMC genomics · 2020Article
- Differential proteomics for studying action mechanisms of traditional Chinese medicines.Chinese medicine · 2019Review
- Evaluation of the Use of TRIzol-Based Protein Extraction Approach for Gel-Based Proteomic Analysis of Dried Seafood Products and Chinese Tonic Foods.International journal of molecular sciences · 2018Article
- Article
- Identification of Ophiocordyceps sinensis and Its Artificially Cultured Ophiocordyceps Mycelia by Ultra-Performance Liquid Chromatography/Orbitrap Fusion Mass Spectrometry and Chemometrics.Molecules (Basel, Switzerland) · 2018Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ophiocordyceps sinensis (Berk.) Sacc. is one of the most well-known fungi in traditional Chinese medicine and is attracting attention because of its nutritious and medicinal properties. The present study aimed to produce a proteomic map to identify common O. sinensis proteins. The caterpillar body and stroma of O. sinensis collected from five locations and four fungal specimens of similar appearance were examined by two-dimensional electrophoresis (2-DE). Five proteins were identified using MALDI-TOF--TOF/MS, and the 2-DE identification pattern was provided. OCS_04585 and β-lactamase domain-containing protein, the two abundant and characteristic proteins, were separated and purified using liquid-phase isoelectric focusing. The products were high-quality materials that can be used for future protein-function studies and immunoassay development.
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