{"125661":{"#nid":"125661","#data":{"type":"event","title":"Prof. P. John Hart, Univ of Texas Health Science Ctr","body":[{"value":"\u003Cp\u003EProf. P. John Hart, Univ of Texas Health Science Ctr\u003C\/p\u003E\u003Cp\u003E\u003Cem\u003E\u003Cstrong\u003EImmature Superoxide Dismutase, its Copper Chaperone, and Motor Neuron Disease\u003C\/strong\u003E\u003C\/em\u003E\u003C\/p\u003E\u003Cp\u003EBiochemistry Division Seminar Series\u003C\/p\u003E\u003Cp\u003EMutations in human copper-zinc superoxide dismutase (SOD1) cause an inherited form of amyotrophic lateral sclerosis (ALS, Lou Gehrig\u2019s disease, motor neuron disease). Insoluble forms of mutant SOD1 accumulate in neural tissues of human ALS patients and in spinal cords of transgenic mice expressing these polypeptides, suggesting that SOD1-linked ALS is a protein misfolding disorder. Understanding the molecular basis for how the pathogenic mutations give rise to SOD1 folding intermediates, which may themselves be toxic, is therefore of keen interest. A critical step on the SOD1 folding pathway occurs when the copper chaperone for SOD1 (CCS) modifies the nascent SOD1 polypeptide by inserting the catalytic copper cofactor and oxidizing its intrasubunit disulfide bond. Recent studies reveal that pathogenic SOD1 proteins coming from cultured cells and from the spinal cords of transgenic mice tend to be metal-deficient and\/or lacking the disulfide bond, raising the possibility that the disease-causing mutations may enhance levels of SOD1-folding intermediates by preventing or hindering CCS-mediated SOD1 maturation. Recently determined structures of SOD1\/CCS complexes suggest molecular motions accompanying CCS-mediated SOD1 posttranslational modification.\u003C\/p\u003E\u003Cp\u003EFor more information contact \u003Ca href=\u0022http:\/\/mailto:raquel.lieberman@chemistry.gatech.edu\u0022\u003EProf. Raquel Lieberman\u003C\/a\u003E (404-385-3663).\u003C\/p\u003E","summary":null,"format":"limited_html"}],"field_subtitle":"","field_summary":[{"value":"\u003Cp\u003EProf. P. John Hart, Univ of Texas Health Science Ctr\u003C\/p\u003E\u003Cp\u003E\u003Cem\u003E\u003Cstrong\u003EImmature Superoxide Dismutase, its Copper Chaperone, and Motor Neuron Disease\u003C\/strong\u003E\u003C\/em\u003E\u003C\/p\u003E\u003Cp\u003EBiochemistry Division Seminar Series\u003Cem\u003E\u003Cstrong\u003E\u003Cbr \/\u003E\u003C\/strong\u003E\u003C\/em\u003E\u003C\/p\u003E","format":"limited_html"}],"field_summary_sentence":"","uid":"27275","created_gmt":"2012-04-23 10:41:53","changed_gmt":"2016-10-08 01:58:45","author":"Shirley Tomes","boilerplate_text":"","field_publication":"","field_article_url":"","field_event_time":{"event_time_start":"2012-05-03T21:00:00-04:00","event_time_end":"2012-05-03T22:00:00-04:00","event_time_end_last":"2012-05-03T22:00:00-04:00","gmt_time_start":"2012-05-04 01:00:00","gmt_time_end":"2012-05-04 02:00:00","gmt_time_end_last":"2012-05-04 02:00:00","rrule":null,"timezone":"America\/New_York"},"extras":[],"related_links":[{"url":"http:\/\/hartlab.uthscsa.edu\/","title":"Prof. P. John Hart, University of Texas Health Science Center"}],"groups":[{"id":"85951","name":"School of Chemistry and Biochemistry"}],"categories":[],"keywords":[],"core_research_areas":[],"news_room_topics":[],"event_categories":[],"invited_audience":[],"affiliations":[],"classification":[],"areas_of_expertise":[],"news_and_recent_appearances":[],"phone":[],"contact":[{"value":"\u003Cp\u003EShirley Tomes (404-894-0591) \u003Ca href=\u0022mailto:shirley.tomes@chemistry.gatech.edu\u0022\u003Eshirley.tomes@chemistry.gatech.edu\u003C\/a\u003E\u003C\/p\u003E","format":"limited_html"}],"email":[],"slides":[],"orientation":[],"userdata":""}}}