A general method for affinity-based proteomic profiling of exo-α-glycosidases

MN Gandy, AW Debowski, KA Stubbs - Chemical Communications, 2011 - pubs.rsc.org
A general method for affinity-based proteomic profiling of exo -α-glycosidases - Chemical
Communications (RSC Publishing) DOI:10.1039/C1CC10308C Royal Society of Chemistry View …

Carbohydrate Bis-acetal-Based Substrates as Tunable Fluorescence-Quenched Probes for Monitoring exo-Glycosidase Activity

S Cecioni, DJ Vocadlo - Journal of the American Chemical …, 2017 - ACS Publications
Tunable Förster resonance energy transfer (FRET)-quenched substrates are useful for
monitoring the activity of various enzymes within their relevant physiological environments …

Assigning N-glycosylation sites of glycoproteins using LC/MSMS in conjunction with endo-M/exoglycosidase mixture

ZM Segu, A Hussein, MV Novotny… - Journal of proteome …, 2010 - ACS Publications
The assignment of protein glycosylation sites and their microheterogeneities are of
biological importance, yet such characterization is still considered to be analytically very …

A High‐Throughput Mass‐Spectrometry‐Based Assay for Identifying the Biochemical Functions of Putative Glycosidases

T Peng, G Nagy, JC Trinidad, JM Jackson… - …, 2017 - Wiley Online Library
The most commonly employed glycosidase assays rely on bulky ultraviolet or fluorescent
tags at the anomeric position in potential carbohydrate substrates, thereby limiting the utility …

Simplifying the exoglycosidase digestion/MALDI-MS procedures for sequencing N-linked carbohydrate side chains

Y Yang, R Orlando - Analytical chemistry, 1996 - ACS Publications
Exoglycosidase digestion coupled with matrix-assisted laser desorption/ionization mass
spectrometry (MALDI-MS) is an effective technique for sequencing the N-linked …

Synthesis and testing of mechanism‐based protein‐profiling probes for retaining endo‐glycosidases

SJ Williams, O Hekmat, SG Withers - ChemBioChem, 2006 - Wiley Online Library
New functional proteomics methods are required for targeting and identification of subsets of
a proteome in an activity‐based fashion. Glycosidases play critical roles in biology, yet a …

A Broad-Specificity O-Glycoprotease That Enables Improved Analysis of Glycoproteins and Glycopeptides Containing Intact Complex O-Glycans

S Vainauskas, H Guntz, E McLeod, C McClung… - Analytical …, 2021 - ACS Publications
Characterization of mucin-type O-glycans linked to serine/threonine of glycoproteins is
technically challenging, in part, due to a lack of effective enzymatic tools that enable their …

Aglycon specificity profiling of α-glucosidases using synthetic probes

W Hakamata, M Muroi, K Kadokura, T Nishio… - Bioorganic & medicinal …, 2005 - Elsevier
We designed and synthesized hydrogen bond based probes 1–8 with the exception of
known glycosidase inhibition mechanisms, and aglycon specificity of 11 different sources of …

Glycoprotein identification and localization of O-glycosylation sites by mass spectrometric analysis of deglycosylated/alkylaminylated peptide fragments

FG Hanisch, M Jovanovic, J Peter-Katalinic - Analytical biochemistry, 2001 - Elsevier
In-gel digestion of densely O-glycosylated proteins, an essential step in proteome analysis,
is often hampered by steric hindrance of the proteases. To overcome this technical problem …

Deciphering Protein O-Glycosylation: Solid-Phase Chemoenzymatic Cleavage and Enrichment

S Yang, P Onigman, WW Wu, J Sjogren… - Analytical …, 2018 - ACS Publications
Glycosylation plays a critical role in the biosynthetic-secretory pathway in the endoplasmic
reticulum (ER) and Golgi apparatus. Over 50% of mammalian cellular proteins are typically …