| pubmed-article:8747464 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8747464 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:8747464 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:8747464 | lifeskim:mentions | umls-concept:C0607430 | lld:lifeskim |
| pubmed-article:8747464 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:8747464 | lifeskim:mentions | umls-concept:C1332765 | lld:lifeskim |
| pubmed-article:8747464 | lifeskim:mentions | umls-concept:C0055271 | lld:lifeskim |
| pubmed-article:8747464 | lifeskim:mentions | umls-concept:C1615557 | lld:lifeskim |
| pubmed-article:8747464 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:8747464 | pubmed:dateCreated | 1996-10-24 | lld:pubmed |
| pubmed-article:8747464 | pubmed:abstractText | The Charcot-Leyden crystal (CLC) protein is a major autocrystallizing constituent of human eosinophils and basophils, comprising approximately 10% of the total cellular protein in these granulocytes. Identification of the distinctive hexagonal bipyramidal crystals of CLC protein in body fluids and secretions has long been considered a hallmark of eosinophil-associated allergic inflammation. Although CLC protein possesses lysophospholipase activity, its role(s) in eosinophil or basophil function or associated inflammatory responses has remained speculative. | lld:pubmed |
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| pubmed-article:8747464 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8747464 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8747464 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8747464 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8747464 | pubmed:issn | 0969-2126 | lld:pubmed |
| pubmed-article:8747464 | pubmed:author | pubmed-author:LefflerHH | lld:pubmed |
| pubmed-article:8747464 | pubmed:author | pubmed-author:ZhouZZ | lld:pubmed |
| pubmed-article:8747464 | pubmed:author | pubmed-author:AcharyaK RKR | lld:pubmed |
| pubmed-article:8747464 | pubmed:author | pubmed-author:LeonidasD DDD | lld:pubmed |
| pubmed-article:8747464 | pubmed:author | pubmed-author:AckermanS JSJ | lld:pubmed |
| pubmed-article:8747464 | pubmed:author | pubmed-author:ElbertB LBL | lld:pubmed |
| pubmed-article:8747464 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8747464 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:8747464 | pubmed:volume | 3 | lld:pubmed |
| pubmed-article:8747464 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8747464 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8747464 | pubmed:pagination | 1379-93 | lld:pubmed |
| pubmed-article:8747464 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8747464 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8747464 | pubmed:articleTitle | Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. | lld:pubmed |
| pubmed-article:8747464 | pubmed:affiliation | School of Biology and Biochemistry, University of Bath, Claverton Down, UK. | lld:pubmed |
| pubmed-article:8747464 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8747464 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8747464 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8747464 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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