Rosenstiel Award lectures on Mar 22 to honor Susan Lindquist

James Haber, Director of the Rosenstiel Center, writes:

The 46th annual Rosenstiel Award for Distinguished Work in Basic Medical Research was awarded last October to Susan Lindquist (MIT), one of the most inventive and influential life scientists of our generation.  Sue tragically passed away a few weeks thereafter; in her honor we have arranged a symposium to celebrate her lab’s great legacy.  The Award talks will be held in next Wednesday, March 22, in Gerstenzang 123 from 3:30 PM to 5:30 PM, followed by a reception open to all in the Shapiro Science Center atrium.  We hope you will all come to honor Sue Lindquist and to be edified by the excellent work carried out by her former colleagues.

Angelika Amon  (Massachusetts Institute of Technology)
“The Remarkable Scientific Life of Susan Lindquist”

Leah Cowen (University of Toronto)
“Harnessing Evolution to Thwart Microbial Drug Resistance and Treat Infectious Disease”

Daniel Jarosz (Stanford University)
“Remembering the Past: A New Form of Protein-Based Inheritance”

Sandro Santagata (Brigham and Women’s Hospital)
“Heat Shock Factor (HSF1): A Powerful Driver of Malignancy”

Susan Lindquist

 

Timothy Street to join Biochemistry faculty

The Biochemistry Department is delighted to announce that Timothy Street has accepted a position as Assistant Professor of Biochemistry. He will arrive at Brandeis in early September.

Timo received his undergraduate degree in Physics from UC  Berkeley and his PhD in Biophysics from Johns Hopkins. For the past few years he has been carrying out postdoctoral research at UCSF in the lab of David Agard.  He works at the nexus of structural biology and the physical chemistry of protein folding, focusing on a perplexing, challenging class of “molecular chaperones,” proteins that help other proteins fold properly into their native conformations.  One of the great puzzles in this biologically crucial field is how these chaperones recognize and engage with the proteins emerging from the ribosome that are improperly folded and need their energy-dependent attention.  Moreover, this process is intimately related to the unfolded protein response, a kind of cellular panic-button.  To attack these kinds of questions, Timo applies a wide range of structural and kinetics methods and in his postdoctoral work has shown how these may be cleverly integrated to picture the mechanisms of highly dynamic chaperone proteins. He is beginning new projects to develop sensors that will allow him to dissect the actions of chaperones in live cells, to complement the mechanistic pictures emerging from his in vitro studies in purified, defined systems.

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