Search Results - "Mitchelhill, Kenneth I."

The T-cell protein tyrosine phosphatase is phosphorylated on Ser-304 by cyclin-dependent protein kinases in mitosis by Bukczynska, Patricia, Klingler-Hoffmann, Manuela, Mitchelhill, Kenneth I, Lam, Mark H C, Ciccomancini, Melissa, Tonks, Nicholas K, Sarcevic, Boris, Kemp, Bruce E, Tiganis, Tony

“…Two alternatively spliced forms of the human protein tyrosine phosphatase TCPTP (T-cell protein tyrosine phosphatase) exist: a 48 kDa form that is targeted to…”
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Plasma amino-terminal pro-brain natriuretic peptide: A novel approach to the diagnosis of cardiac dysfunction by Campbell, Duncan J., Mitchelhill, Kenneth I., Schlicht, Stephen M., Booth, Russell J.

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Plasma amino-terminal pro-brain natriuretic peptide: A novel approach to the diagnosis of cardiac dysfunction by Campbell, Duncan J., Mitchelhill, Kenneth I., Schlicht, Stephen M., Booth, Russell J.

“…Background: Heart failure is a common cause of hospitalization and death across the industrialized world. Improving the diagnosis and care of patients with…”
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FHA domain boundaries of the Dun1p and Rad53p cell cycle checkpoint kinases by Hammet, Andrew, Pike, Brietta L., Mitchelhill, Kenneth I., Teh, Trazel, Kobe, Bostjan, House, Colin M., Kemp, Bruce E., Heierhorst, Jörg

“…Dun1p and Rad53p of the budding yeast Saccharomyces cerevisiae are members of a conserved family of cell cycle checkpoint protein kinases that contain…”
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Role of the pseudosubstrate sequence in smooth muscle myosin light chain kinase thermal stability by FAUX, M. C, PEARSON, R. B, MITCHELHILL, K. I, KEMP, B. E

“…Smooth muscle myosin light chain kinase (MLCK) is stable in the presence of Ca2+/calmodulin and does not undergo inactivation as reported for skeletal muscle…”
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Chicken smooth muscle myosin light chain kinase is acetylated on its NH2-terminal methionine by Faux, M C, Mitchelhill, K I, Katsis, F, Wettenhall, R E, Kemp, B E

“…The reported cDNA structure of chicken smooth muscle myosin light chain kinase (smMLCK) encodes a protein of 972 residues (Olson et al. Proc. Natl. Acad. Sci…”
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