{"doi":"10.1073/pnas.68.5.909","title":"The Reaction of Glucagon with Its Receptor: Evidence for Discrete Regions of Activity and Binding in the Glucagon Molecule","abstract":"<jats:p>\n                    Des-histidine-glucagon (DH-glucagon, glucagon\n                    <jats:sub>2-29</jats:sub>\n                    ) does not activate the glucagon-sensitive adenylate cyclase system present in either liver plasma membranes or in fat-cell “ghosts”, but inhibits the response of these systems to submaximal concentrations of glucagon. DH-glucagon also inhibits, competitively, the binding of [\n                    <jats:sup>125</jats:sup>\n                    I]glucagon to its receptor in liver plasma membranes. Amino-terminal fragments of glucagon (glucagon\n                    <jats:sub>1-21</jats:sub>\n                    , glucagon\n                    <jats:sub>1-23</jats:sub>\n                    ) and carboxy-terminal fragments (glucagon\n                    <jats:sub>20-29</jats:sub>\n                    , glucagon\n                    <jats:sub>22-29</jats:sub>\n                    ) failed to activate adenylate cyclase, to inhibit the response of the enzyme to glucagon, or to compete with labeled glucagon at its receptor.\n                  </jats:p>\n                  <jats:p>It is concluded that the amino-terminal histidine residue of glucagon is essential for biological activity and that a hydrophobic near-carboxy-terminal region (residues 22-27) is essential for binding of glucagon to its receptor. Amino-terminal histidine may also contribute to the binding of glucagon, since the apparent affinity of DH-glucagon for the receptor is only about one-sixth that of glucagon. Thus, essentially the entire molecule of glucagon must be considered to be the biologically active species.</jats:p>\n                  <jats:p>Because, as shown elsewhere, the binding of glucagon to its receptor shows characteristics of hydrophobic bonding, and because certain detergents induce conformational changes in the carboxy-terminal binding region of glucagon, the binding is probably of a lipophilic type.</jats:p>","journal":"Proceedings of the National Academy of Sciences","year":1971,"id":617776,"datarank":9.119194982436222,"base_score":4.890349128221754,"endowment":4.890349128221754,"self_citation_contribution":0.7335523692332632,"citation_network_contribution":8.385642613202958,"self_endowment_contribution":0.7335523692332632,"citer_contribution":8.385642613202958,"corpus_percentile":null,"corpus_rank":null,"citation_count":132,"citer_count":117,"citers_with_citation_signal":103,"citers_with_endowment":103,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":110422,"name":"Lutz Birnbaumer","orcid":"0000-0002-0775-8661","position":1,"is_corresponding":false},{"id":1544649,"name":"Stephen L. Pohl","orcid":null,"position":2,"is_corresponding":false},{"id":1593326,"name":"F. Sundby","orcid":null,"position":3,"is_corresponding":false},{"id":1593321,"name":"Martin Rodbell","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"citation_network_status":"fetched"},"created_at":"2026-08-03T02:35:34.148073Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}