Establishment of a new short, protease-resistant, affinity labeling reagent for the cholecystokinin receptor
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference16 articles.
1. Affinity labeling of a novel cholecystokinin-binding protein in rat pancreatic plasmalemma using new short probes for the receptor.
2. Use of the heterobifunctional cross-linker m-maleimidobenzoyl N-hydroxysuccinimide ester to affinity label cholecystokinin binding proteins on rat pancreatic plasma membranes.
3. Specific photoaffinity crosslinking of [125I]cholecystokinin to pancreatic plasma membranes. Evidence for a disulfide-linked Mr 76000 peptide in cholecystokinin receptors
4. Characterization of cholecystokinin receptor subunits on pancreatic plasma membranes.
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1. Use of N,O-bis-Fmoc-d-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides;International Journal of Peptide and Protein Research;2009-01-12
2. A unidirectional crosslinking strategy for HIV-1 protease dimerization inhibitors;Bioorganic & Medicinal Chemistry Letters;2004-08
3. Key Differences in Molecular Complexes of the Cholecystokinin Receptor with Structurally Related Peptide Agonist, Partial Agonist, and Antagonist;Molecular Pharmacology;2004-06-02
4. Environment and Mobility of a Series of Fluorescent Reporters at the Amino Terminus of Structurally Related Peptide Agonists and Antagonists Bound to the Cholecystokinin Receptor;Journal of Biological Chemistry;2002-05
5. Characterization of the type A cholecystokinin receptor hormone-binding domain: use of contrasting and complementary methodologies;Peptides;2001-08
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