Výsledky vyhledávání

A Peptide Agonist Acts by Occupation of a Monomeric G Protein-Coupled Receptor: Dual Sites of Covalent Attachment to Domains Near TM1 and TM7 of the Same Molecule Make Biologically Significant Domain-Swapped Dimerization Unlikely

Autor: Zongshi Ji, Elizabeth M. Hadac, Laurence J. Miller, Delia I. Pinon, Randal M. Henne, Terry P. Lybrand

Publikováno v: Journal of Medicinal Chemistry. 42:2105-2111

Membrane receptor dimerization is a well-established event for initiation of signaling at growth factor receptors and has been postulated to exist for G protein-coupled receptors, based on correction of nonfunctional truncated, mutant, or chimeric co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac6aa8ed831b4d6d39b30a2052015e47
https://doi.org/10.1021/jm980732q

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Direct Identification of a Distinct Site of Interaction between the Carboxyl-terminal Residue of Cholecystokinin and the Type A Cholecystokinin Receptor Using Photoaffinity Labeling

Autor: Randel M. Henne, Zongshi Ji, Terry P. Lybrand, Laurence J. Miller, Elizabeth M. Hadac, Sunil A. Patel

Publikováno v: Journal of Biological Chemistry. 272:24393-24401

Mechanisms of ligand binding and activation of G protein-coupled receptors are particularly important, due to their ubiquitous expression and potential as drug targets. Molecular interactions between ligands and these receptors are best defined for s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67dbc8713afa6af4f2903582a5b4fafa
https://doi.org/10.1074/jbc.272.39.24393

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Direct identification of a second distinct site of contact between cholecystokinin and its receptor

Autor: Terry P. Lybrand, Eileen L. Holicky, Elizabeth M. Hadac, Randal M. Henne, Laurence J. Miller, Zongshi Ji, Delia I. Pinon

Publikováno v: The Journal of biological chemistry. 273(21)

We have developed a biologically active analogue of cholecystokinin (CCK) that incorporates a photolabile benzoylphenylalanine (Bpa) moiety in the middle of its pharmacophoric domain, which efficiently establishes a covalent bond with an interacting

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::511afe05d4ae8bc5794152490c857d57
https://pubmed.ncbi.nlm.nih.gov/9582333

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Development of magnetic beads for rapid and efficient metal-chelate affinity purifications

Autor: Zongshi Ji, Laurence J. Miller, Delia I. Pinon

Publikováno v: Analytical biochemistry. 240(2)

Metal-chelate affinity chromatography offers multiple advantages for protein purification, yet existing resins make its applications to sparse, hydrophobic, or particularly labile proteins and peptides quite difficult. In this work, we have developed

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6df058a139fc4daaec5d6dcf6ba0bbd
https://pubmed.ncbi.nlm.nih.gov/8811907

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