scholarly journals Imidazolium-tagged glycan probes for non-covalent labeling of live cells

2016 ◽  
Vol 52 (27) ◽  
pp. 4906-4909 ◽  
Author(s):  
David Benito-Alifonso ◽  
Shirley Tremell ◽  
Joanna C. Sadler ◽  
Monica Berry ◽  
M. Carmen Galan
Keyword(s):  
Sialic Acid ◽  
Live Cells ◽  
Covalent Labeling ◽  
Site Specific

The use imidazolium tagged-mannosamine derivative for the non-covalent, rapid and site-specific labeling of sialic acid containing glycoproteins using commercial N-nitrilotriacetate fluorescent reagents in a range of live cells is reported.

Site-specific covalent labeling of proteins inside live cells using small molecule probes

2009 ◽  
Vol 17 (3) ◽  
pp. 981-989 ◽  
Author(s):  
Souvik Chattopadhaya ◽  
Rajavel Srinivasan ◽  
Dawn S.Y. Yeo ◽  
Grace Y.J. Chen ◽  
Shao Q. Yao
Keyword(s):  
Small Molecule ◽  
Live Cells ◽  
Covalent Labeling ◽  
Site Specific ◽  
Small Molecule Probes

scholarly journals An Efficient Site-Specific Method for Irreversible Covalent Labeling of Proteins with a Fluorophore

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Jiaquan Liu ◽  
Jeungphill Hanne ◽  
Brooke M. Britton ◽  
Matthew Shoffner ◽  
Aaron E. Albers ◽  
...  
Keyword(s):  
Specific Method ◽  
Covalent Labeling ◽  
Site Specific

Site-Specific Introduction of Sialic Acid into Insulin

2004 ◽  
Vol 116 (12) ◽  
pp. 1542-1546 ◽  
Author(s):  
Masaaki Sato ◽  
Reiko Sadamoto ◽  
Kenichi Niikura ◽  
Kenji Monde ◽  
Hirosato Kondo ◽  
...  
Keyword(s):  
Sialic Acid ◽  
Site Specific

scholarly journals Cross-species comparison of site-specific evolutionary-rate variation in influenza haemagglutinin

2013 ◽  
Vol 368 (1614) ◽  
pp. 20120334 ◽  
Author(s):  
Austin G. Meyer ◽  
Eric T. Dawson ◽  
Claus O. Wilke
Keyword(s):  
Protein Structure ◽  
Sialic Acid ◽  
Avian Influenza ◽  
Evolutionary Rate ◽  
Solvent Accessibility ◽  
Rate Variation ◽  
Structural Constraints ◽  
Binding Region ◽  
Site Specific ◽  
Sialic Acid Binding

We investigate the causes of site-specific evolutionary-rate variation in influenza haemagglutinin (HA) between human and avian influenza, for subtypes H1, H3, and H5. By calculating the evolutionary-rate ratio, ω = d N /d S as a function of a residue's solvent accessibility in the three-dimensional protein structure, we show that solvent accessibility has a significant but relatively modest effect on site-specific rate variation. By comparing rates within HA subtypes among host species, we derive an upper limit to the amount of variation that can be explained by structural constraints of any kind. Protein structure explains only 20–40% of the variation in ω . Finally, by comparing ω at sites near the sialic-acid-binding region to ω at other sites, we show that ω near the sialic-acid-binding region is significantly elevated in both human and avian influenza, with the exception of avian H5. We conclude that protein structure, HA subtype, and host biology all impose distinct selection pressures on sites in influenza HA.

scholarly journals Advanced Fluorescent Polymer Probes for the Site-Specific Labeling of Proteins in Live Cells Using the HaloTag Technology

ACS Omega ◽  
2019 ◽  
Vol 4 (7) ◽  
pp. 12841-12847
Author(s):  
Thomas Berki ◽  
Anush Bakunts ◽  
Damien Duret ◽  
Laura Fabre ◽  
Catherine Ladavière ◽  
...  
Keyword(s):  
Live Cells ◽  
Site Specific ◽  
Fluorescent Polymer

scholarly journals Site-specific covalent labeling of His-tag fused proteins with N-acyl-N-alkyl sulfonamide reagent

2021 ◽  
Vol 30 ◽  
pp. 115947
Author(s):  
Vikram Thimaradka ◽  
Jae Hoon Oh ◽  
Christina Heroven ◽  
A. Radu Aricescu ◽  
Michisuke Yuzaki ◽  
...  
Keyword(s):  
Covalent Labeling ◽  
Site Specific ◽  
His Tag
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