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Kaye D. Speicher

Researcher at Wistar Institute

Publications -  21
Citations -  1726

Kaye D. Speicher is an academic researcher from Wistar Institute. The author has contributed to research in topics: Endoplasmic reticulum & Membrane protein. The author has an hindex of 17, co-authored 21 publications receiving 1629 citations.

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A HUPO test sample study reveals common problems in mass spectrometry–based proteomics

Alexander W. Bell, +101 more
- 01 Jun 2009 - 
TL;DR: Central analysis determined missed identifications, environmental contamination, database matching and curation of protein identifications as sources of problems in liquid chromatography–mass spectrometry–based proteomics.
Journal Article

Systematic analysis of peptide recoveries from in-gel digestions for protein identifications in proteome studies

TL;DR: An optimized in-geltrypsin digestion strategy in which proteins in 1.0-mm-thick gels are stained with Coomassie blue or Ruby Red, digested overnight with modified trypsin, and extracted one or two times with small volumes of aqueous buffer is suggested.
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Deciphering the human platelet sheddome.

TL;DR: A subset of membrane proteins are defined as sheddome candidates, forming the basis for further studies examining the impact of ectodomain shedding on platelet function.
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Erythrocyte detergent-resistant membrane proteins: Their characterization and selective uptake during malarial infection

TL;DR: Ten internalized DRM proteins show varied lipid and peptidic anchors indicating that, contrary to the prevailing model of apicomplexan vacuole formation, DRM association, rather than lipid anchors, provides the preferred criteria for protein recruitment to the malarial vacuoles.
Journal ArticleDOI

Landscape of the mitochondrial Hsp90 metabolome in tumours.

TL;DR: It is reported that Heat Shock Protein 90 (Hsp90)-directed protein folding in mitochondria controls central metabolic networks in tumor cells, including the electron transport chain, citric acid cycle, fatty acid oxidation, amino acid synthesis, and cellular redox status.