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Allostery in the Hsp70 chaperone proteins.
Heat shock 70-kDa (Hsp70) chaperones are essential to in vivo protein folding, protein transport, and protein re-folding. They carry out these activities using repeated cycles of binding and releaseExpand
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Allosteric drugs: the interaction of antitumor compound MKT-077 with human Hsp70 chaperones.
Hsp70 (heat shock protein 70 kDa) chaperones are key to cellular protein homeostasis. However, they also have the ability to inhibit tumor apoptosis and contribute to aberrant accumulation ofExpand
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Chemical Manipulation of Hsp70 ATPase Activity Regulates Tau Stability
Alzheimer's disease and other tauopathies have recently been clustered with a group of nervous system disorders termed protein misfolding diseases. The common element established between theseExpand
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  • Open Access
SAGA: rapid automatic mainchain NMR assignment for large proteins
Here we describe a new algorithm for automatically determining the mainchain sequential assignment of NMR spectra for proteins. Using only the customary triple resonance experiments, assignments canExpand
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Study of the photocycle of the metastable states of SRII and their mutants with the use of light activated NMR spectroscopy
Sensory rhodopsin II (SRII) is a seven helix protein that belongs to the rhodopsin protein family. Light induced conformational changes govern SRII's function. These changes are related to the photoExpand
Gradient-enhanced TROSY described with Cartesian product operators
TROSY, Transverse Relaxation Optimized Spectroscopy, was developed more than a decade ago. Since that time, the 15 N- 1 H HSQC-TROSY experiment has become the standard ''fingerprint'' correlationExpand