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N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity.
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N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity.
N-Glycosylation of Asparagine 130 in the Extracellular Domain of the Human Calcitonin Receptor Significantly Increases Peptide Hormone Affinity. Biochemistry. 2017 07 05; 56(26):3380-3393.
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subject areas
Acetylglucosamine
Acetylglucosamine
Amino Acid Substitution
Amino Acid Substitution
Asparagine
Asparagine
Binding Sites
Binding Sites
Calcitonin
Calcitonin
Glycosylation
Glycosylation
HEK293 Cells
HEK293 Cells
Humans
Humans
Islet Amyloid Polypeptide
Islet Amyloid Polypeptide
Kinetics
Kinetics
Ligands
Ligands
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Models, Molecular
Models, Molecular
Molecular Conformation
Molecular Conformation
Mutation
Mutation
Peptide Fragments
Peptide Fragments
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Protein Interaction Domains and Motifs
Protein Interaction Domains and Motifs
Protein Processing, Post-Translational
Protein Processing, Post-Translational
Receptor Activity-Modifying Protein 2
Receptor Activity-Modifying Protein 2
Receptors, Calcitonin
Receptors, Calcitonin
Recombinant Fusion Proteins
Recombinant Fusion Proteins
authors with profiles
Augen A Pioszak