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A relationship between protein stability and protein function.
Enzymes are thought to use their ordered structures to facilitate catalysis. A corollary of this theory suggests that enzyme residues involved in function are not optimized for stability. We testedExpand
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Low-barrier hydrogen bond in photoactive yellow protein
Low-barrier hydrogen bonds (LBHBs) have been proposed to play roles in protein functions, including enzymatic catalysis and proton transfer. Transient formation of LBHBs is expected to stabilizeExpand
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Anti‐FGF23 Neutralizing Antibodies Show the Physiological Role and Structural Features of FGF23
Fibroblast growth factor (FGF)23 is proposed to play a physiological role in the regulation of phosphate and vitamin D metabolism; deranged circulatory levels of FGF23 cause several diseases withExpand
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Characterization of the Interaction between Interleukin-13 and Interleukin-13 Receptors*
Interleukin-13 (IL-13) possesses two types of receptor: the heterodimer, composed of the IL-13Rα1 chain (IL-13Rα1) and the IL-4Rα chain (IL-4Rα), transducing the IL-13 signals; and the IL-13Rα2 chainExpand
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A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozyme.
The glycosyl-enzyme intermediate in lysozyme action has long been considered to be an oxocarbonium ion, although precedent from other glycosidases and theoretical considerations suggest it should beExpand
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Homodimeric cross-over structure of the human granulocyte colony-stimulating factor (GCSF) receptor signaling complex.
A crystal structure of the signaling complex between human granulocyte colony-stimulating factor (GCSF) and a ligand binding region of GCSF receptor (GCSF-R), has been determined to 2.8 A resolution.Expand
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Structure and function of ∆1-tetrahydrocannabinolic acid (THCA) synthase, the enzyme controlling the psychoactivity of Cannabis sativa.
∆1-Tetrahydrocannabinolic acid (THCA) synthase catalyzes the oxidative cyclization of cannabigerolic acid (CBGA) into THCA, the precursor of the primary psychoactive agent ∆1-tetrahydrocannabinol inExpand
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Structure-based design of a lysozyme with altered catalytic activity
Here we show that the substitution Thr 26→His in the active site of T4 lysozyme causes the product to change from the α- to the β-anomer. This implies an alteration in the catalytic mechanism of theExpand
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Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site.
In contrast to hen egg-white lysozyme, which retains the beta-configuration of the substrate in the product, T4 lysozyme (T4L) is an inverting glycosidase. The substitution Thr-26 --> His, however,Expand
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Crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus.
The crystal structure of glycosyltrehalose trehalohydrolase from the hyperthermophilic archaeum Sulfolobus solfataricus KM1 has been solved by multiple isomorphous replacement. The enzyme is anExpand
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