From USC News
2011-10-17
Massry Prize Winners Discuss Chaperone-assisted protein folding
2011 Massry Prize winners F. Ulrich Hartl and Arthur Horwich delivered their laureate lectures in Artesy Auditorium on Oct. 13.
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From USC’s HSC Weekly
2011-10-13
2011 Massry Prize Winners to Speak on Oct 13
F. Ulrich Hartl, M.D. and Arthur Horwich, M.D. have been named recipients of the 2011 Massry Prize.
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From USC’s HSC Weekly
2010-10-29
Massry Prize Winners Discuss Discovery of Cellular Membrane Trafficking
Leaders in the field of membrane fusion, 2010 Massry Prize winners James E. Rothman and Randy Schekman delivered their laureate lectures in Mayer Auditorium on Oct. 21.
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From USC News
2010-10-21
2010 Massry Prize winners to speak on Oct. 21
James E. Rothman, the Fergus F. Wallace Professor of Biomedical Sciences at Yale University, and Randy Schekman, an investigator of the Howard Hughes Medical Institute, have been named the recipients of the 2010 Massry Prize.
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From USC News
2009-11-17
Ambros, Ruvkun Receive Massry Prize
Gary Ruvkun and fellow molecular biologist Victor Ambros recently received the prestigious Meira and Shaul G. Massry Prize for their revolutionary research in micro RNA (miRNA).
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From USC’s HSC Weekly
2009-10-16
Massry Prize Laureate wins the 2009 Nobel Prize in Chemistry
Professor Ada Yonath of the Weizmann Institute in Israel, who won the 2004 Massry Prize, has received the 2009 Nobel Prize in Chemistry.
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From USC’s HSC Weekly
2009-09-25
Pioneers in small RNA research receive Massry Prize
Molecular biologists Victor Ambros and Gary Ruvkun have been named recipients of the 2009 Massry Prize for their discovery of microRNAs.
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News Archives
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2011 Massry Prize Laureates’ Lectures
KECK School of Medicine of USC
Thursday, October 21st
12:00 - 1:30 PM
Aresty Auditorium
Harlyne J. Norris Research Tower, Lower Level
Reception in the Aresty Auditorium Foyer at 11:30 AM
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F. Ulrich Hartl, M.D.
Max Planck Institute of Biochemistry
"Chaperone-assisted protein folding in health and disease"
The past two decades have witnessed a paradigm shift in our understanding of cellular protein folding. While the three-dimensional structures of functional proteins are determined by their amino acid sequences, we now know that in the crowded cellular environment many proteins depend on molecular chaperones to fold efficiently and at a biologically relevant rate. This role in folding was first demonstrated for the class of chaperones called chaperonins, which provide nano-compartments for single protein molecules to fold in isolation, unimpaired by aggregation. Failure of the chaperone machinery to maintain the conformational integrity of the cellular proteome (proteostasis), may facilitate the manifestation of diseases associated with protein aggregation, such as Parkinson’s and Huntington’s disease. Motivated by the desire to find a cure for these ailments, researchers are now searching for drugs that can activate the chaperone system, thereby delaying disease onset and prolonging the healthy human lifespan. |
Arthur Horwich, M.D.
Yale University
“Chaperonin-mediated protein folding”
A mutant of yeast was originally identified and studied with Ulrich Hartl in which proteins could enter mitochondria but were unable to properly fold. The mutation turned out to affect a large ring assembly, the chaperonin Hsp60. Using the homologous GroEL/GroES system of bacteria we, Ulrich, and others have dissected a mechanism by which this machine provides kinetic assistance through the consumption of ATP to the protein folding process. During the time of our work on mechanism a community of neurobiologists has identified that protein misfolding is associated with a number of neurodegenerative diseases, and we have begun to study a misfolding-induced model of ALS. |
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