2010
Two Independent Histidines, One in Human Prolactin and One in Its Receptor, Are Critical for pH-dependent Receptor Recognition and Activation*
Kulkarni MV, Tettamanzi MC, Murphy JW, Keeler C, Myszka DG, Chayen NE, Lolis EJ, Hodsdon ME. Two Independent Histidines, One in Human Prolactin and One in Its Receptor, Are Critical for pH-dependent Receptor Recognition and Activation*. Journal Of Biological Chemistry 2010, 285: 38524-38533. PMID: 20889499, PMCID: PMC2992285, DOI: 10.1074/jbc.m110.172072.Peer-Reviewed Original Research
2007
The Kinetics of Binding Human Prolactin, but Not Growth Hormone, to the Prolactin Receptor Vary over a Physiologic pH Range †
Keeler C, Jablonski EM, Albert YB, Taylor BD, Myszka DG, Clevenger CV, Hodsdon ME. The Kinetics of Binding Human Prolactin, but Not Growth Hormone, to the Prolactin Receptor Vary over a Physiologic pH Range †. Biochemistry 2007, 46: 2398-2410. PMID: 17279774, DOI: 10.1021/bi061958v.Peer-Reviewed Original Research
2004
Consequences of Binding an S-Adenosylmethionine Analogue on the Structure and Dynamics of the Thiopurine Methyltransferase Protein Backbone †
Scheuermann TH, Keeler C, Hodsdon ME. Consequences of Binding an S-Adenosylmethionine Analogue on the Structure and Dynamics of the Thiopurine Methyltransferase Protein Backbone †. Biochemistry 2004, 43: 12198-12209. PMID: 15379558, DOI: 10.1021/bi0492556.Peer-Reviewed Original ResearchConceptsNMR chemical shift mapping experimentsChemical shift mapping experimentsNative structureS-adenosylmethionineProteasomal-dependent pathwayCatalytic mechanismProtein backboneIntracellular degradationIndirect conformational changesS-adenosylmethionine analogPresence of sinefunginBacterial orthologuesChemical shift changesProtein backbone dynamicsPseudomonas syringaeSubstrate recognitionProtein sequencesSAM analoguesConformational changesNMR spectroscopyBackbone dynamicsMapping experimentsBackbone mobilitySinefunginNMR relaxation