[February 23, 2018}
Wiggle Wiggle Not a Trickle; Structure Specificity and Integrity at Biological Membranes
Presented by Dr. Robert Stroud
March 8, 2018 | 3:30 pm | Byers Auditorium
NEWS FROM THE ACADEMIC SENATE Contact: Kenneth Laslavic, 415/476.8827
UCSF Academic Senate's 61st Annual Faculty Research Lecture – Basic Science Awarded to Robert Stroud, PhD
The Academic Senate is pleased to announce the selection of Robert Stroud, PhD, as recipient of the 61st Annual Faculty Research Lectureship – Basic Science for his prolific research on modern structural biology. The lecture, titled "Wiggle Wiggle Not a Trickle; Structure Specificity and Integrity at Biological Membranes", will take place on Thursday, March 8, 2018, at 3:30 p.m. in Byers Auditorium, Mission Bay Campus. The event will be simulcast and a reception will follow.
A world leader in structural biology, Dr. Stroud's research has addressed a breadth of systems that impact a wide array of biological processes. This work has aimed to understand the molecular level cellular signaling and communication across cell membranes, and the macromolecular encoding of specificity and affinity at protein/protein and protein/ligand interfaces.
Dr. Stroud has more than 340 peer reviewed publications and 300 structures to his credit.
Dr. Stroud's contributions have been recognized by his election to the Royal Society of Medicine, the National Academy of Sciences, and the American Academy of Arts & Sciences
Dr. Stroud is Professor of Biochemistry and Biophysics and Professor of pharmaceutical Chemistry in the Department of Department of Biochemistry and Biophysics. He received his PhD from University of London and completed postdoctoral training at California Institute of Technology. Dr. Stroud joined UCSF in 1976 to start the University's first structural biology program.
The 61st Annual Faculty Research Lecture – Basic Science will be held in Byers Auditorium, Mission Bay Campus, on Thursday, March 8, 2018, at 3:30 p.m., and will be available to stream via simulcast. Refreshments will be provided. The lecture is open to the campus community and the general public.
*** Since 1957, this award has been bestowed on an individual member of the UCSF faculty who has made a distinguished record in basic science. Nominations are made by UCSF faculty, who consider scientific research contributions of their colleagues and submit nominations for this prestigious award to the Academic Senate Committee on Research. Each year, the Committee on Research selects the recipient of this award.
A list of the past recipients of the award can be viewed at http://tiny.ucsf.edu/QzEFLb.
Filoviruses, such as Ebola virus require host-cell receptors, endocytosis, proteolytic cleavage, and fusion with the endolysosomal membrane for release of viral material into the cytoplasm. Two-pore channels (TPCs) comprise a subfamily (TPC1-3) of eukaryotic voltage- and ligand-gated cation channels that contain two non-equivalent tandem pore-forming subunits that then dimerize to form quasi-tetramers and orchestrate the trafficking of Filoviruses, including Ebola, in human cells.
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New research reveals the mechanism behind a cancer-relevant inhibition of human sugar transporting protein. The hope is that this will guide future drug design targeting sugar uptake mechanisms. This will ultimately lead to progress in a number of important common conditions, such as diabetes and cancer.
Our group revealed how different inhibitors of the human sugar transporter GLUT1 (figure) bind to a central cavity in the protein to inhibit its function. The results show a surprisingly promiscuous internal binding pocket with submicromolar affinities for chemically distinct substrates. With these results, the hope is that this will guide future drug design targeting sugar uptake mechanisms.
Tumors and cancer cells are highly dependent on sugar uptake to maintain their rapid growth rate. It has been proposed that a regulation or reduction of cellular sugar uptake might have therapeutic benefits. While not being a panacea, a reduction in cancer growth rate could allow other treatments time to reach full effect, and potentially could allow a much improved efficacy of other chemotherapeutics.
Coordinating the impact of structural genomics on the human α-helical transmembrane proteome: This Commentary by 9 membrane centers received 1,327 visits and 2,233 page views since it was published in February 2013. It was ranked #4 in article requests for the month of February.
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