Combination of receptor-binding assays and designed mutant receptors for discerning agonists and antagonists

2007 ◽  
Vol 43 (3) ◽  
pp. 822-828 ◽  
Author(s):  
Kazuhiro Matsui
Keyword(s):  
Receptor Binding ◽  
Binding Assays ◽  
Mutant Receptors

scholarly journals Estrogenicity of styrene oligomers and assessment of estrogen receptor binding assays.

2002 ◽  
Vol 110 (7) ◽  
Author(s):  
Katsutoshi Ohno ◽  
Yukimasa Azuma ◽  
Katsuhiro Date ◽  
Shigeru Nakano ◽  
Toru Kobayashi ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Receptor Binding ◽  
Binding Assays ◽  
Estrogen Receptor Binding

Impact of IgG2 high molecular weight species on neonatal Fc receptor binding assays

2015 ◽  
Vol 489 ◽  
pp. 25-31 ◽  
Author(s):  
Yuling Zhang ◽  
Abhishek Mathur ◽  
Gwen Maher ◽  
Thomas Arroll ◽  
Robert Bailey
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Receptor Binding ◽  
Fc Receptor ◽  
Binding Assays ◽  
Neonatal Fc Receptor ◽  
High Molecular Weight Species

scholarly journals Structural and Biochemical Characterization of Botulinum Neurotoxin Subtype B2 Binding to Its Receptors

Toxins ◽  
2020 ◽  
Vol 12 (9) ◽  
pp. 603
Author(s):  
Jonathan R. Davies ◽  
Geoffrey Masuyer ◽  
Pål Stenmark
Keyword(s):  
Receptor Binding ◽  
Molecular Mechanisms ◽  
Biochemical Characterization ◽  
Hydrophobic Interactions ◽  
Binding Assays ◽  
Protein Receptor ◽  
Wide Range ◽  
Protein Receptors ◽  
Therapeutic Molecules ◽  
Botulinum Neurotoxins

Botulinum neurotoxins (BoNTs) can be used therapeutically to treat a wide range of neuromuscular and neurological conditions. A collection of natural BoNT variants exists which can be classified into serologically distinct serotypes (BoNT/B), and further divided into subtypes (BoNT/B1, B2, …). BoNT subtypes share a high degree of sequence identity within the same serotype yet can display large variation in toxicity. One such example is BoNT/B2, which was isolated from Clostridium botulinum strain 111 in a clinical case of botulism, and presents a 10-fold lower toxicity than BoNT/B1. In an effort to understand the molecular mechanisms behind this difference in potency, we here present the crystal structures of BoNT/B2 in complex with the ganglioside receptor GD1a, and with the human synaptotagmin I protein receptor. We show, using receptor-binding assays, that BoNT/B2 has a slightly higher affinity for GD1a than BoNT/B1, and confirm its considerably weaker affinity for its protein receptors. Although the overall receptor-binding mechanism is conserved for both receptors, structural analysis suggests the lower affinity of BoNT/B2 is the result of key substitutions, where hydrophobic interactions important for synaptotagmin-binding are replaced by polar residues. This study provides a template to drive the development of future BoNT therapeutic molecules centered on assessing the natural subtype variations in receptor-binding that appears to be one of the principal stages driving toxicity.

An improved swinging-bucket ultracentrifugal filter for receptor-binding assays

1981 ◽  
Vol 114 (1) ◽  
pp. 103-104 ◽  
Author(s):  
Robert Freundlich ◽  
Dermot B. Taylor
Keyword(s):  
Receptor Binding ◽  
Binding Assays

Detection of antibiotics in sheep milk by receptor-binding assays

2014 ◽  
Vol 34 (2) ◽  
pp. 184-189 ◽  
Author(s):  
M.C. Beltrán ◽  
R.L. Althaus ◽  
M.I. Berruga ◽  
A. Molina ◽  
M.P. Molina
Keyword(s):  
Receptor Binding ◽  
Binding Assays ◽  
Sheep Milk

Expression and Functional Characterization of the β-Isoform of the Folate Receptor on CD34+ Cells

Blood ◽  
1999 ◽  
Vol 93 (11) ◽  
pp. 3940-3948 ◽  
Author(s):  
Joseph A. Reddy ◽  
Laura S. Haneline ◽  
Edward F. Srour ◽  
Asok C. Antony ◽  
D. Wade Clapp ◽  
...  
Keyword(s):  
Folic Acid ◽  
Receptor Binding ◽  
Folate Receptor ◽  
Functional Characterization ◽  
Hematopoietic Cells ◽  
Chemotherapeutic Agents ◽  
Malignant Cells ◽  
Binding Assays ◽  
Kb Cells ◽  
Cd34 Cells

We have investigated the expression and functional competence of folate receptor (FR) isoforms on human hematopoietic cells. Using immunofluorescence and reverse transcriptase-polymerase chain reaction (RT-PCR) methodology, we find that a substantial fraction of low-density mononuclear and CD34+ cells express both the β and γ isoforms of FR. The  isoform of FR (the form most commonly found on cancer cells) was surprisingly absent from all hematopoietic cells examined. Compared with KB cells (a human cell line known for its elevated expression of FR-), the abundance of FR-β on CD34+ cell surfaces was relatively low (≈8% of KB cell levels). Because many antifolates and folic acid-linked chemotherapeutic agents enter malignant cells at least partially via FR endocytosis, it was important to evaluate the ability of FR on CD34+ cells to bind folic acid (FA). Based on three FR binding assays, freshly isolated CD34+ cells were found to display no affinity for FA. Thus, regardless of whether steps were taken to remove endogenous folates before receptor binding assays, FR on primitive hematopoietic cells failed to bind 3H-FA, fluorescein isothiocyanate (FITC)-linked FA, or FA-derivatized liposomes. In contrast, analogous studies on KB cells showed high levels of receptor binding for all three FR probes. These studies show that although multipotent hematopoietic progenitor cells express FR, the receptor does not transport significant amounts of FA. Consequently, antifolates and FA-linked chemotherapeutic agents that can be engineered to enter malignant cells exclusively through the FR should not harm progenitor/stem cell function.

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