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YashoNandini Singh
Researcher at Florida Atlantic University
Publications - 6
Citations - 21
YashoNandini Singh is an academic researcher from Florida Atlantic University. The author has contributed to research in topics: Glycosylation & Chemistry. The author has an hindex of 1, co-authored 3 publications receiving 4 citations.
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Journal ArticleDOI
Positional Scanning MUC1 Glycopeptide Library Reveals the Importance of PDTR Epitope Glycosylation for Lectin Binding
YashoNandini Singh,Maria C. Rodriguez Benavente,Mohammed H. Al-Huniti,Donella Beckwith,Ramya Ayyalasomayajula,Eric Patino,William S. Miranda,Alex Wade,Mare Cudic +8 more
TL;DR: This study synthesized for the first time a MUC1-derived positional scanning synthetic glycopeptide combinatorial library (PS-SGCL) that vary in number and location of cancer-associated Tn antigen using the “tea bag” approach and revealed a carbohydrate density-dependent affinity trend and site-specific glycosylation requirements for high affinity binding to these lectins.
Journal ArticleDOI
TF-containing MUC1 glycopeptides fail to entice Galectin-1 recognition of tumor-associated Thomsen-Freidenreich (TF) antigen (CD176) in solution
Forrest G. FitzGerald,Forrest G. FitzGerald,Maria C. Rodriguez Benavente,Maria C. Rodriguez Benavente,Camelia Garcia,Yaima Rivero,YashoNandini Singh,Hongjie Wang,Gregg B. Fields,Gregg B. Fields,Mare Cudic +10 more
TL;DR: A method for large-scale expression of Gal-1 and its histidine-tagged analog for use in binding studies by isothermal titration calorimetry (ITC) and development of an analytical method based on AlphaScreen technology to screen forGal-1 inhibitors are developed.
Journal ArticleDOI
Tyrosine O -GalNAc Alters the Conformation and Proteolytic Susceptibility of APP Model Glycopeptides.
TL;DR: In this paper, the authors showed that O-glycosylation of Tyr681 can induce a conformational change in APP and affect its proteolytic processing fate toward the amyloidogenic pathway.
Journal ArticleDOI
Mucin-Type O-Glycosylation Proximal to β-Secretase Cleavage Site Affects APP Processing and Aggregation Fate
YashoNandini Singh,Deepika Regmi,David Ormaza,Ramya Ayyalasomayajula,Nancy Vela,Gustavo Mundim,Deguo Du,Dmitriy Minond,Mare Cudic +8 more
TL;DR: The results confirm that the Swedish mutation and/or O-glycosylation can render APP model glycopeptides more susceptible to cleavage by β-secretase and sheds new light on the possible role of glycosolation and/ or glycan density on the rate of Aβ40 aggregation.
OtherDOI
Exploring Glycan Binding Specificity of Odorranalectin by Alanine Scanning Library.
TL;DR: Alanine scan analogues of odorranalectin, a cyclic peptide that exhibits lectin like properties, were screened for binding BSA-conjugated monosaccharides using an enzyme-linked lectin assay (ELLA), and results revealed that Lys5, Phe7, Tyr9, Gly12, Leu14, and Thr17 were crucial for bindingBSA-L-fucose, BSA