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David S. Reiner

Researcher at University of California, San Diego

Publications -  41
Citations -  3852

David S. Reiner is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Giardia lamblia & Endoplasmic reticulum. The author has an hindex of 30, co-authored 41 publications receiving 3679 citations. Previous affiliations of David S. Reiner include Oklahoma Medical Research Foundation & Sanford-Burnham Institute for Medical Research.

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Encystation and expression of cyst antigens by Giardia lamblia in vitro

TL;DR: In these studies, encystation of Giardia lamblia in vitro was demonstrated by morphologic, immunologic, and biochemical criteria and will aid in understanding the differentiation of an important protozoan pathogen.
Journal Article

Sorting of cyst wall proteins to a regulated secretory pathway during differentiation of the primitive eukaryote, Giardia lamblia.

TL;DR: In this paper, the encystation-specific vesicles (ESV) of G. lamblia were found to have a regulated pathway of transport and secretion of cyst wall antigens via a novel class of osmiophilic secretory vesicle.
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The minimal kinome of Giardia lamblia illuminates early kinase evolution and unique parasite biology

TL;DR: The reduced kinome of Giardia sheds new light on early kinase evolution, and its highly divergent sequences add to the definition of individual kinase families as well as offering specific drug targets.
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Giardia lamblia: the roles of bile, lactic acid, and pH in the completion of the life cycle in vitro.

TL;DR: Large numbers (10(4) to greater than 10(5)/ml) of Type I water-resistant Giardia lamblia cysts were produced in vitro under conditions that are characteristic of the human intestinal lumen, the first quantitative in vitro demonstration of the complete life cycle of G. Lamblia from humans.
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Isolation and expression of the gene for a major surface protein of Giardia lamblia.

TL;DR: The abundance of cysteine residues suggests that the native proteins on the parasite surface may contain numerous disulfide bonds, which would promote resistance to intestinal fluid proteases and to the detergent activity of bile salts and would help to explain the survival of Giardia in the human small intestine.