2000
DOI: 10.1006/bbrc.2000.3540
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Isolation of a Novel Ubiquitin-like Protein from Pleurotus ostreatus Mushroom with Anti-Human Immunodeficiency Virus, Translation-Inhibitory, and Ribonuclease Activities

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Cited by 88 publications
(36 citation statements)
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“…Clone MV094 coded for a conserved ubiquitin core fused to 58 aminoacids homologous to the S27 ribosomal protein. This protein diVers from that described by Wang and Ng in P. ostreatus (Wang and Ng, 2000), but its structure has been also found in other fungi such as Ustilago maydis and N. crassa, animals and plants.…”
Section: Protein Metabolismcontrasting
confidence: 53%
“…Clone MV094 coded for a conserved ubiquitin core fused to 58 aminoacids homologous to the S27 ribosomal protein. This protein diVers from that described by Wang and Ng in P. ostreatus (Wang and Ng, 2000), but its structure has been also found in other fungi such as Ustilago maydis and N. crassa, animals and plants.…”
Section: Protein Metabolismcontrasting
confidence: 53%
“…Ubiquitin-like peptides from the fruiting bodies of edible mushrooms, including Pleurotus sajor-caju, Pleurotus ostreatus, and Cantharellus cibarius, have been characterized so far (29,47,48). These peptides show an N-terminal sequence identical to that of ubiquitin, and all have RNaseand translation-inhibiting activities.…”
Section: Discussionmentioning
confidence: 99%
“…wt. 14.5 kDa) were isolated and characterized from sclerotia of P. tuber-regium, exhibited very stable nuclease activity at 100°C for 30 minutes with a higher ribonucleolytic activity toward poly-G [39,40,41]. Another ribonuclease, pleuturegin, was also isolated from both fresh and dried sclerotia of P. tuber-regium [17].…”
Section: Antihuman Immunodeficiency Virus (Hiv) Activitymentioning
confidence: 99%