Bioxanthracenes from the insect pathogenic fungus Cordyceps pseudomilitaris BCC 1620: I. Taxonomy, fermentation, isolation and antimalarial activity

Journal of Antibiotics

Volumn 54, Issue 1, 2001, Pages 29-35

  Jaturapat, A ^a   Isaka, M ^a   Hywel Jones, N L ^a   Lertwerawat, Y ^a   Kamchonwongpaisan, S ^a   Kirtikara, K ^a   Tanticharoen, M ^a   Thebtaranonth, Y ^a  

^a NATIONAL SCIENCE AND TECHNOLOGY DEVELOPMENT AGENCY   (Thailand)

Author keywords

[No Author keywords available]

Indexed keywords

ACID ANHYDRIDE; ANTHRACENE DERIVATIVE; BIOXANTHRACENE DERIVATIVE; CHLOROQUINE; CORDYANHYDRIDE A; CORDYANHYDRIDE B; MONOMER; UNCLASSIFIED DRUG;

ANIMAL CELL; ANTIMALARIAL ACTIVITY; ARTICLE; BREAST CANCER; CANCER CELL CULTURE; CONTROLLED STUDY; CORDYCEPS PSEUDOMILITARIS; CYTOTOXICITY; DRUG ISOLATION; DRUG SCREENING; DRUG STRUCTURE; DRUG SYNTHESIS; FERMENTATION; FUNGUS; FUNGUS GROWTH; HUMAN; HUMAN CELL; INSECT; NONHUMAN; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; SQUAMOUS CELL CARCINOMA; TAXONOMY; VERO CELL;

CORDYCEPS PSEUDOMILITARIS;

EID: 0035126005     PISSN: 00218820     EISSN: None     Source Type: Journal    
DOI: 10.7164/antibiotics.54.29     Document Type: Article

References (9)

1. Cordyceps khaoyaiensis and C. pseudomilitaris, two new pathogens of lepidopteran larvae from Thailand
2. Cordyanhydrides A and B. Two unique anhydrides from the insect pathogenic fungus Cordyceps pseudomilitaris BCC 1620
3. Bioxanthracenes from the insect pathogenic fungus Cordyceps pseudomilitaris BCC 1620. II. Structure elucidation
4. Human malaria parasites in continuous culture
5. Quantitative assessment of antimalarial activity in vitro by a semiautomated microdilution technique
6. New colorimetic cytotoxicity assay for anticancer-drug screening
7. ES-242-1, a novel compound from Verticillium sp., binds to a site on N-methyl-D-aspartate receptor that is coupled to the channel domain
8. ES-242-2, -3, -4, -5, -6, -7, and -8, novel bioxanthracenes produced by Verticillium sp., which act on the N-methyl-D-aspartate receptor
9. The ES-242s, novel N-methyl-D-aspartate antagonists of microbial origin, interact with both the neurotransmitter recognition site and the ion channel domain