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Using x-ray vision, he keeps his eye on the bacteria
The New York Times
Dr. C. Erec Stebbins, head of Rockefeller University's Laboratory of Structural Microbiology, spends much
of his time using a nearly 100-year-old investigative tool, X-ray crtystallography, to identify the bacterial
proteins that cause disease. Finding these proteins is a first step in developing drugs to counter the organisms'
harmful effect. Dr. Stebbins is only 34, but has already identified 10 proteins. [pdf]
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M. Lilic, V. E. Galkin, A. Orlova, M. S. Van-Loock, E. H. Egelman, and C. E. Stebbins,
A salmonella invasion protein that acts as a
"molecular staple"
Science, 301,1918-1921 (2003).
Salmonella invasion protein A (SipA) is an important virulence factor injected
into host cells, where it modulates the cytoskeleton by polym-erizing actin.
By combining high resolution X-ray crystallography of SipA, reconstructions of
electron micrographs of actin-SipA filaments, modeling, and structure-based
mutagenesis, we demonstrate that SipA functions as a 'molecular staple,' in
which a central globular domain and two non-globular 'arms' mechanically stabilize
the filament by tethering actin subunits in opposing strands. [pdf]
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Threading a narrow needle
Chemical & Engineering News; 79:45.
A high-resolution crystal structure obtained by
Jorge E. Galán, a microbiologist at Yale School of
Medicine, and former postdoc C. Erec Stebbins,
now at Rockefeller University, sheds some light on
the type III secretion system used by many
pathogenic bacteria to inject effector proteins into
host eukaryotic cells. The structure could help in
identifying or designing compounds to interfere with
the secretion system. [pdf]
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Rockefeller researchers solve structure for deadly
bacterial toxin
Drug Discovery & Development
Researchers at Rockefeller University, New York, have determined the
structure of a potent DNA-damaging protein involved in many bacterial
diseases. Known as cytolethal distending toxin (CDT), the protein
poison is the chemical culprit responsible for leading killer diseases in
the developing world, such as typhoid fever and diarrhea. It is the only
bacterial toxin known to attack its victim's DNA, and therefore is also a
suspected carcinogen. [pdf]
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Battle against terror gains silicon ally
Stebbins helps bring power of "distributed computing" to bear on biowarfare
news & notes
If two brains are better than one, then imagine what a network of
thousands could do. That's the reasoning behind distributed
computing networks, such as the non-profit organization Find-a-
Drug, which has hundreds of people volunteering their idle
personal computers for the mountainous task of screening billions
of chemicals for new disease-fighting drugs.
[pdf]
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Structure of a DNA attack
The Rockefeller University Scientist
After two years and hundreds of gallons of buffering solution,
scientists in C. Erec Stebbins' laboratory have visualized
the molecular structure of a genotoxin used by 10 different
disease-causing bacteria to attack human DNA. [pdf]
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The democratization of supercomputing
The Scientist, 17: 30.
The genome has been read. The proteome has been opened. As a
result, research problems have gotten more difficult. Fortunately,
access to the tools that help investigators rise to those new challenges
is quickly becoming easier.
How much easier? Ask Charles Taylor, a biomechanical engineer at
Stanford University. To model the flow of blood in human arteries,
Taylor needs to solve as many as 10 million nonlinear partial
differential equations at once, "and because the equations are
nonlinear, we need to do a few subiterations of each," Taylor says.
"That definitely requires supercomputing." [pdf]
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