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Patana Teng-umnuay
Researcher at University of Florida
Publications - 8
Citations - 1248
Patana Teng-umnuay is an academic researcher from University of Florida. The author has contributed to research in topics: Gel electrophoresis & Glycosylation. The author has an hindex of 7, co-authored 8 publications receiving 1165 citations.
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Journal ArticleDOI
Recruitment of human muscleblind proteins to (CUG)(n) expansions associated with myotonic dystrophy.
Jill Miller,Carl R. Urbinati,Patana Teng-umnuay,Myrna G. Stenberg,Barry J. Byrne,Charles A. Thornton,Maurice S. Swanson +6 more
TL;DR: This work proposes that DM1 disease is caused by aberrant recruitment of the EXP proteins to the DMPK transcript (CUG)n expansion, and identifies the triplet repeat expansion (EXP) RNA‐binding proteins as candidate sequestered factors.
Journal ArticleDOI
Ribonuclear inclusions in skeletal muscle in myotonic dystrophy types 1 and 2
Ami Mankodi,Patana Teng-umnuay,Matt Krym,Don Henderson,Maurice S. Swanson,Charles A. Thornton +5 more
TL;DR: It is concluded that ribonuclear inclusions are a key feature of the muscle pathology in DM and that sequestration of muscleblind proteins may have a direct role in the disease process.
Journal ArticleDOI
The Cytoplasmic F-box Binding Protein SKP1 Contains a Novel Pentasaccharide Linked to Hydroxyproline inDictyostelium
Patana Teng-umnuay,Howard R. Morris,Anne Dell,Maria Panico,Thanai Paxton,Christopher M. West +5 more
TL;DR: SKP1 is variably modified by an unusual linear pentasaccharide, suggesting the localization of a novel glycosylation pathway in the cytoplasm.
Journal ArticleDOI
Analysis of Skp1 glycosylation and nuclear enrichment in dictyostelium
TL;DR: Evidence is uncovered that the glycosylation pathway is developmentally regulated and can function posttranslationally, and that core glycosYLation is required for Skp1's nuclear concentration.
Journal ArticleDOI
Identification of a UDP-GlcNAc:Skp1-hydroxyproline GlcNAc-transferase in the cytoplasm of Dictyostelium.
TL;DR: The presence of the enzyme in the cytosolic fraction, its dependence on a reducing environment, and its high affinity for UDP-Glc NAc strongly suggest that Skp1 is glycosylated by a HyPro GlcNAc-transferase that resides in the cytoplasm.