8591036

Source:http://linkedlifedata.com/resource/pubmed/id/8591036

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0006837, umls-concept:C0205164, umls-concept:C0243077, umls-concept:C0444626, umls-concept:C1327616, umls-concept:C1704241, umls-concept:C2717969
pubmed:issue	11
pubmed:dateCreated	1996-4-3
pubmed:abstractText	Infections caused by Candida albicans, a common fungal pathogen of humans, are increasing in incidence, necessitating development of new therapeutic drugs. Secreted aspartic proteinase (SAP) activity is considered an important virulence factor in these infections and might offer a suitable target for drug design. Amongst the various SAP isozymes, the SAP2 gene product is the major form expressed in a number of C. albicans strains.
pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/101087697
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/A 70450, http://linkedlifedata.com/resource/pubmed/chemical/Antifungal Agents, http://linkedlifedata.com/resource/pubmed/chemical/Aspartic Acid Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances, http://linkedlifedata.com/resource/pubmed/chemical/Pepstatins, http://linkedlifedata.com/resource/pubmed/chemical/Piperazines, http://linkedlifedata.com/resource/pubmed/chemical/SAP2 protein, Candida, http://linkedlifedata.com/resource/pubmed/chemical/Streptomyces pepsin inhibitor, http://linkedlifedata.com/resource/pubmed/chemical/pepstatin
pubmed:status	MEDLINE
pubmed:month	Nov
pubmed:issn	0969-2126
pubmed:author	pubmed-author:AndersonB FBF, pubmed-author:CutfieldJ FJF, pubmed-author:CutfieldS MSM, pubmed-author:DodsonE JEJ, pubmed-author:MarshallC JCJ, pubmed-author:MoodyP CPC, pubmed-author:SullivanP APA
pubmed:issnType	Print
pubmed:day	15
pubmed:volume	3
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	1261-71
pubmed:dateRevised	2009-11-19
pubmed:meshHeading	pubmed-meshheading:8591036-Amino Acid Sequence, pubmed-meshheading:8591036-Antifungal Agents, pubmed-meshheading:8591036-Aspartic Acid Endopeptidases, pubmed-meshheading:8591036-Binding Sites, pubmed-meshheading:8591036-Candida albicans, pubmed-meshheading:8591036-Crystallography, X-Ray, pubmed-meshheading:8591036-Drug Design, pubmed-meshheading:8591036-Enzyme Inhibitors, pubmed-meshheading:8591036-Fungal Proteins, pubmed-meshheading:8591036-Isoenzymes, pubmed-meshheading:8591036-Macromolecular Substances, pubmed-meshheading:8591036-Models, Molecular, pubmed-meshheading:8591036-Molecular Sequence Data, pubmed-meshheading:8591036-Pepstatins, pubmed-meshheading:8591036-Piperazines, pubmed-meshheading:8591036-Protein Binding, pubmed-meshheading:8591036-Protein Conformation, pubmed-meshheading:8591036-Sequence Alignment, pubmed-meshheading:8591036-Sequence Homology, Amino Acid
pubmed:year	1995
pubmed:articleTitle	The crystal structure of a major secreted aspartic proteinase from Candida albicans in complexes with two inhibitors.
pubmed:affiliation	Biochemistry Department, University of Otago, Dunedin, New Zealand.
pubmed:publicationType	Journal Article, Comparative Study, Research Support, Non-U.S. Gov't