Noncompetitive Inhibition of the Acetylcholine Receptor
{'Code': '08090200', 'Directorate': {'Abbreviation': 'BIO', 'LongName': 'Direct For Biological Sciences'}, 'Division': {'Abbreviation': 'IOS', 'LongName': 'Division Of Integrative Organismal Systems'}}
{'SignBlockName': 'Stacy Springer', 'PO_EMAI': None, 'PO_PHON': None}
The control of skeletal muscles by the brain requires the                       transmission of electrical signals down nerve fibers to the                     muscles.  When the electrical signals reach the end of the nerve                fibers, a chemical, acetylcholine, is released and diffuses                     across the space between the nerves and muscles.  The                           acetylcholine that reaches the muscles binds to a molecule in the               muscle membrane, the acetylcholine receptor, and opens an ion                   channel in the receptor molecule which starts a series of events                leading to the contraction of the muscle.  In addition to                       acetylcholine, many drugs bind to the acetylcholine receptor.                   Some of these drugs, i.e. noncompetitive inhibitors, bind at                    sites different from where acetylcholine binds.  These                          noncompetitive inhibitors block the effects of acetylcholine.                   The purpose of this research is to understand at a molecular                    level how these noncompetitive inhibitors block the effects of                  acetylcholine.  Because the acetylcholine receptor from Torpedo                 electric organ is very similar to human acetylcholine receptor                  and is the richest source of receptors, the Torpedo will be used                as a model.                                                                                                                                                     Fluorescence techniques will be utilized to determine whether                   different types of noncompetitive inhibitors perturb 1) the                     distance between drug binding sites, 2) the orientation of bound                drugs, 3) the distance from drug binding sites to the membrane                  surface, 4) the rotational constraints of lipids proximal and                   distal to the receptor.  The ability of a variety of                            noncompetitive inhibitors to perturb the above parameters will be               correlated with their capacity to inhibit receptor functional                   activity.                                                                                                                                                       Because the acetylcholine receptor is structurally similar to                   other ligand-regulated ion channel molecules, the research should               advance the basic understanding of how drugs, especially general                anesthetics, modulate the functional activity of ligand-regulated               ion channel molecules.
{'FirstName': 'David', 'LastName': 'Johnson', 'PI_MID_INIT': 'A', 'PI_SUFX_NAME': None, 'PI_FULL_NAME': 'David A Johnson', 'EmailAddress': 'david.johnson@ucr.edu', 'NSF_ID': '000109272', 'StartDate': '08/01/1989', 'EndDate': None, 'RoleCode': 'Principal Investigator'}
{'Name': 'University of California-Riverside', 'CityName': 'RIVERSIDE', 'ZipCode': '925210001', 'PhoneNumber': '9518275535', 'StreetAddress': '200 UNIVERSTY OFC BUILDING', 'StreetAddress2': None, 'CountryName': 'United States', 'StateName': 'California', 'StateCode': 'CA', 'CONGRESSDISTRICT': '39', 'CONGRESS_DISTRICT_ORG': 'CA39', 'ORG_UEI_NUM': 'MR5QC5FCAVH5', 'ORG_LGL_BUS_NAME': 'REGENTS OF THE UNIVERSITY OF CALIFORNIA AT RIVERSIDE', 'ORG_PRNT_UEI_NUM': None}
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[{'Code': '118800', 'Text': 'SYNAPTIC MECHANISMS'}, {'Code': '119200', 'Text': 'NEURONAL AND GLIAL MECHANISMS'}]
{'url': 'https://www.nsf.gov/awardsearch/download?DownloadFileName=1988&All=true', 'xml': '8821357.xml'}