Development and validation of ligand-binding assays to support the bioanalysis of therapeutic antibodies

2013 ◽  
pp. 76-90 ◽  
Author(s):  
Joseph C Marini ◽  
Tong-Yuan Yang ◽  
Jeffrey P Kuhl ◽  
Mark A Ware
Keyword(s):  
Ligand Binding ◽  
Therapeutic Antibodies ◽  
Binding Assays ◽  
Development And Validation

Development and Validation of Ligand-Binding Assays for Biomarkers

2009 ◽  
pp. 129-161 ◽  
Author(s):  
Jean W. Lee ◽  
Yang Pan ◽  
Peter J. O'Brien ◽  
Ren Xu
Keyword(s):  
Ligand Binding ◽  
Binding Assays ◽  
Development And Validation

scholarly journals The structure of SeviL, a GM1b/asialo-GM1 binding R-type lectin from the mussel Mytilisepta virgata

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Kenichi Kamata ◽  
Kenji Mizutani ◽  
Katsuya Takahashi ◽  
Roberta Marchetti ◽  
Alba Silipo ◽  
...  
Keyword(s):  
Immune System ◽  
Sialic Acid ◽  
Ligand Binding ◽  
Steric Hindrance ◽  
Sequence Similarity ◽  
Binding Assays ◽  
Subunit Interface ◽  
Nmr Techniques ◽  
And Control ◽  
Asialo Gm1

AbstractSeviL is a recently isolated lectin found to bind to the linear saccharides of the ganglioside GM1b (Neu5Ac$$\alpha$$ α (2-3)Gal$$\beta$$ β (1-3)GalNAc$$\beta$$ β (1-4)Gal$$\beta$$ β (1-4)Glc) and its precursor, asialo-GM1 (Gal$$\beta$$ β (1-3)GalNAc$$\beta$$ β (1-4)Gal$$\beta$$ β (1-4)Glc). The crystal structures of recombinant SeviL have been determined in the presence and absence of ligand. The protein belongs to the $$\beta$$ β -trefoil family, but shows only weak sequence similarity to known structures. SeviL forms a dimer in solution, with one binding site per subunit, close to the subunit interface. Molecular details of glycan recognition by SeviL in solution were analysed by ligand- and protein-based NMR techniques as well as ligand binding assays. SeviL shows no interaction with GM1 due to steric hindrance with the sialic acid branch that is absent from GM1b. This unusual specificity makes SeviL of great interest for the detection and control of certain cancer cells, and cells of the immune system, that display asialo-GM1.

Characterization of labeled reagents in ligand-binding assays by a surface plasmon resonance biosensor

Bioanalysis ◽  
2017 ◽  
Vol 9 (2) ◽  
pp. 193-207 ◽  
Author(s):  
Jia Duo ◽  
JoAnne Bruno ◽  
Steven Piccoli ◽  
Binodh DeSilva ◽  
Yan J Zhang
Keyword(s):  
Surface Plasmon Resonance ◽  
Ligand Binding ◽  
Surface Plasmon ◽  
Plasmon Resonance ◽  
Binding Assays ◽  
Surface Plasmon Resonance Biosensor

Study of Cardiac Autonomic Receptors by Radiolabeled Ligand Binding Assays

1984 ◽  
pp. 77-94
Author(s):  
Allan S. Manalan ◽  
Larry R. Jones ◽  
Henry R. Besch ◽  
August M. Watanabe
Keyword(s):  
Ligand Binding ◽  
Binding Assays ◽  
Autonomic Receptors

Cell-Free Ligand Binding Assays for Nuclear Receptors

2003 ◽  
pp. 53-71 ◽  
Author(s):  
Stacey A Jones ◽  
Derek J Parks ◽  
Steven A Kliewer
Keyword(s):  
Ligand Binding ◽  
Nuclear Receptors ◽  
Free Ligand ◽  
Binding Assays

Considerations and rationale for the selection of LC-MS/MS or ligand binding assays for bioanalysis of therapeutic proteins

2016 ◽  
pp. 154-166
Author(s):  
Charles Scott Hottenstein ◽  
Eric Dobrzynski ◽  
Joshua Albert ◽  
Jonathan Kehler ◽  
Matthew Szapacs
Keyword(s):  
Ligand Binding ◽  
Therapeutic Proteins ◽  
Binding Assays ◽  
Selection Of

Ligand-binding assays with OBPs and CSPs

2020 ◽  
pp. 229-258 ◽  
Author(s):  
Chiara D'Onofrio ◽  
Valeriia Zaremska ◽  
Jiao Zhu ◽  
Wolfgang Knoll ◽  
Paolo Pelosi
Keyword(s):  
Ligand Binding ◽  
Binding Assays
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