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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
1999-10-19
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pubmed:databankReference |
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pubmed:abstractText |
Mammalian purple acid phosphatases are highly conserved binuclear metal-containing enzymes produced by osteoclasts, the cells that resorb bone. The enzyme is a target for drug design because there is strong evidence that it is involved in bone resorption.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
757-67
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10425678-Acid Phosphatase,
pubmed-meshheading:10425678-Amino Acid Sequence,
pubmed-meshheading:10425678-Animals,
pubmed-meshheading:10425678-Binding Sites,
pubmed-meshheading:10425678-Catalytic Domain,
pubmed-meshheading:10425678-Crystallography, X-Ray,
pubmed-meshheading:10425678-Glycoproteins,
pubmed-meshheading:10425678-Humans,
pubmed-meshheading:10425678-Models, Molecular,
pubmed-meshheading:10425678-Molecular Sequence Data,
pubmed-meshheading:10425678-Protein Conformation,
pubmed-meshheading:10425678-Sequence Homology, Amino Acid,
pubmed-meshheading:10425678-Swine
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pubmed:year |
1999
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pubmed:articleTitle |
Crystal structure of mammalian purple acid phosphatase.
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pubmed:affiliation |
Department of Biochemistry, University of Queensland, St Lucia, Australia. guddat@biosci.uq.edu.au
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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