Discerning Dynamic Signatures of Membrane-Bound α-Synuclein Using Site-Specific Fluorescence Depolarization Kinetics

2020 ◽  
Vol 124 (5) ◽  
pp. 708-717 ◽  
Author(s):  
Karishma Bhasne ◽  
Neha Jain ◽  
Rishabh Karnawat ◽  
Shruti Arya ◽  
Anupa Majumdar ◽  
...  
Keyword(s):  
Fluorescence Depolarization ◽  
Site Specific ◽  
Specific Fluorescence ◽  
Membrane Bound

scholarly journals Neutrophil azurophilic granule glycoproteins are distinctively decorated by atypical pauci- and phosphomannose glycans

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Karli R. Reiding ◽  
Yu-Hsien Lin ◽  
Floris P. J. van Alphen ◽  
Alexander B. Meijer ◽  
Albert J. R. Heck
Keyword(s):  
Immune System ◽  
Autoimmune Disease ◽  
Secreted Proteins ◽  
Receptor Interaction ◽  
Post Translational Modification ◽  
Site Specific ◽  
Healthy Donors ◽  
Asymmetric Hybrid ◽  
Membrane Bound ◽  
High Mannose

AbstractWhile neutrophils are critical first-responders of the immune system, they also cause tissue damage and act in a variety of autoimmune diseases. Many neutrophil proteins are N-glycosylated, a post-translational modification that may affect, among others, enzymatic activity, receptor interaction, and protein backbone accessibility. So far, a handful neutrophil proteins were reported to be decorated with atypical small glycans (paucimannose and smaller) and phosphomannosylated glycans. To elucidate the occurrence of these atypical glycoforms across the neutrophil proteome, we performed LC-MS/MS-based (glyco)proteomics of pooled neutrophils from healthy donors, obtaining site-specific N-glycan characterisation of >200 glycoproteins. We found that glycoproteins that are typically membrane-bound to be mostly decorated with high-mannose/complex N-glycans, while secreted proteins mainly harboured complex N-glycans. In contrast, proteins inferred to originate from azurophilic granules carried distinct and abundant paucimannosylation, asymmetric/hybrid glycans, and glycan phosphomannosylation. As these same proteins are often autoantigenic, uncovering their atypical glycosylation characteristics is an important step towards understanding autoimmune disease and improving treatment.

Mapping Calcium-Sensitive Regions in the Neuronal Calcium Sensor GCAP2 by Site-Specific Fluorescence Labeling

Biochemistry ◽  
2016 ◽  
Vol 55 (18) ◽  
pp. 2567-2577 ◽  
Author(s):  
Stefan Sulmann ◽  
Melanie Wallisch ◽  
Alexander Scholten ◽  
Jens Christoffers ◽  
Karl-Wilhelm Koch
Keyword(s):  
Fluorescence Labeling ◽  
Calcium Sensor ◽  
Site Specific ◽  
Specific Fluorescence ◽  
Neuronal Calcium Sensor

Site-specific .epsilon.-amino monoacylation of pancreatic phospholipase A2. 2. Transformation of soluble phospholipase A2 into a highly penetrating "membrane-bound" form

Biochemistry ◽  
1988 ◽  
Vol 27 (5) ◽  
pp. 1688-1694 ◽  
Author(s):  
Frans C. Van der Wiele ◽  
Wim Atsma ◽  
Ben Roelofsen ◽  
Margreet Van Linde ◽  
Jan Van Binsbergen ◽  
...  
Keyword(s):  
Phospholipase A2 ◽  
Site Specific ◽  
Pancreatic Phospholipase ◽  
Pancreatic Phospholipase A2 ◽  
Membrane Bound

scholarly journals G-quadruplex ligands exhibit differential G-tetrad selectivity

2015 ◽  
Vol 51 (38) ◽  
pp. 8048-8050 ◽  
Author(s):  
D. D. Le ◽  
M. Di Antonio ◽  
L. K. M. Chan ◽  
S. Balasubramanian
Keyword(s):  
Site Specific ◽  
Specific Fluorescence ◽  
Equilibrium Binding ◽  
Fluorescence Quench ◽  
G Quadruplex ◽  
Selective Ligands

Site-specific fluorescence quench assay allows for targeted G-quadruplex equilibrium binding measurements to investigate G-tetrad selective ligands.

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