Dynamics of actomyosin interactions in relation to the cross-bridge cycle.
Philos Trans R Soc Lond B Biol Sci 359, 1843-55.
Low concentrations of sodium dodecyl sulfate induce the extension of beta 2-microglobulin-related amyloid fibrils at a neutral pH.
Biochemistry 43, 11075-82.
Increase in the conformational flexibility of beta 2-microglobulin upon copper binding: a possible role for copper in dialysis-related amyloidosis.
Protein Sci 13, 797-809.
Same fold with different mobility: backbone dynamics of small protease inhibitors from the desert locust, Schistocerca gregaria.
Biochemistry 43, 3376-84.
Combinatorial control of gene expression.
Nat Struct Mol Biol 11, 812-5.
Revealing the molecular principles of eukaryotic transcription factor assembly on specific DNA sites is pivotal to understanding how genes are differentially expressed. By analyzing structures of transcription factor complexes bound to specific DNA elements we demonstrate how protein and DNA regulators manage gene expression in a combinatorial fashion.
Mutant rat trypsin selectively cleaves tyrosyl peptide bonds.
Anal Biochem 326, 190-9.
Thermal stability of chemically denatured green fluorescent protein (GFP). A preliminary study.
Thermochim Acta 410, 161.
Differential actin binding along the PEVK domain of skeletal muscle titin.
J Cell Sci 117, 5781-9.
Comparison of proteolytic activities produced by entomopathogenic Photorhabdus bacteria: strain- and phase-dependent heterogeneity in composition and activity of four enzymes.
Appl Environ Microbiol 70, 7311-20.
Two-headed binding of the unphosphorylated nonmuscle heavy meromyosin.ADP complex to actin.
Biochemistry 43, 4219-26.
Engineering lysine reactivity as a conformational sensor in the Dictyostelium myosin II motor domain.
J Muscle Res Cell Motil 25, 95-102.
Mechanism of blebbistatin inhibition of myosin II.
J Biol Chem 279, 35557-63.
Ala226 to Gly and Ser189 to Asp mutations convert rat chymotrypsin B to a trypsin-like protease.
Protein Eng Des Sel 17, 127-31.
The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions.
J Mol Biol 342, 1533-46.
Handbook of Proteolytic Enzym-es 2nd Edn (Barrett, A. J., Woessner, F., Rawlings, N., ed.), pp. 1495-1501. Elsevier Ltd, Amsterdam.
The effect of F-actin on the relay helix position of myosin II, as revealed by tryptophan fluorescence, and its implications for mechanochemical coupling.
Biochemistry 43, 15404-17.
Characterization of f-actin tryptophan phosphorescence in the presence and absence of tryptophan-free myosin motor domain.
Biophys J 87, 1146-54.