His scientific interests lie mostly in Myosin, Myosin light-chain kinase, Phosphorylation, Biochemistry and Phosphatase. His studies deal with areas such as Smooth muscle contraction, Protein subunit and Actin as well as Myosin. In general Myosin light-chain kinase, his work in Telokin is often linked to Antiparallel linking many areas of study.
David J. Hartshorne interconnects Molecular biology, Kinase and RHOA in the investigation of issues within Phosphorylation. Meromyosin and Protein phosphorylation are subfields of Biochemistry in which his conducts study. His Phosphatase research is classified as research in Enzyme.
His primary areas of investigation include Myosin, Myosin light-chain kinase, Biochemistry, Phosphorylation and Phosphatase. His biological study spans a wide range of topics, including Dephosphorylation, Rho-associated protein kinase and Actin. Myosin light-chain kinase is the subject of his research, which falls under Cell biology.
His research on Biochemistry often connects related areas such as Muscle contraction. David J. Hartshorne combines subjects such as Immunoglobulin light chain, ATPase, Kinase and RHOA with his study of Phosphorylation. His Phosphatase study combines topics in areas such as Molecular biology, Protein subunit, Protein phosphorylation and MYH7.
David J. Hartshorne mainly focuses on Myosin, Myosin light-chain kinase, Phosphatase, Phosphorylation and Biochemistry. Specifically, his work in Myosin is concerned with the study of Myosin-light-chain phosphatase. To a larger extent, he studies Cell biology with the aim of understanding Myosin light-chain kinase.
His Phosphatase research incorporates themes from Retinoblastoma protein, Protein subunit and MYH7. As part of the same scientific family, David J. Hartshorne usually focuses on Phosphorylation, concentrating on RHOA and intersecting with Protein kinase C. In his study, cGMP-dependent protein kinase, Smooth muscle contraction and Myosin phosphatase activity is strongly linked to Vascular smooth muscle, which falls under the umbrella field of Biochemistry.
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Calyculin A and okadaic acid: inhibitors of protein phosphatase activity
H. Ishihara;B.L. Martin;D.L. Brautigan;H. Karaki.
Biochemical and Biophysical Research Communications (1989)
Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts.
Go Totsukawa;Yoshihiko Yamakita;Shigeko Yamashiro;David J. Hartshorne.
Journal of Cell Biology (2000)
Inhibitory Phosphorylation Site for Rho-associated Kinase on Smooth Muscle Myosin Phosphatase
Jianhua Feng;Masaaki Ito;Kazuhito Ichikawa;Naoki Isaka.
Journal of Biological Chemistry (1999)
Modulator protein as a component of the myosin light chain kinase from chicken gizzard.
Renata Dabrowska;James M. F. Sherry;Debra K. Aromatorio;David J. Hartshorne.
Biochemistry (1978)
Myosin phosphatase: structure, regulation and function.
Masaaki Ito;Takeshi Nakano;Ferenc Erdodi;David J. Hartshorne.
Molecular and Cellular Biochemistry (2004)
Myosin light chain phosphatase: subunit composition, interactions and regulation.
David J. Hartshorne;Masaaki Ito;Ferenc Erdödi.
Journal of Muscle Research and Cell Motility (1998)
Distinct roles of MLCK and ROCK in the regulation of membrane protrusions and focal adhesion dynamics during cell migration of fibroblasts
Go Totsukawa;Yue Wu;Yasuharu Sasaki;David J. Hartshorne.
Journal of Cell Biology (2004)
Activation of RhoA and Inhibition of Myosin Phosphatase as Important Components in Hypertension in Vascular Smooth Muscle
Tetsuya Seko;Masaaki Ito;Yasuko Kureishi;Ryuji Okamoto.
Circulation Research (2003)
Hepatocyte deformation induced by cyanobacterial toxins reflects inhibition of protein phosphatases.
J. E. Eriksson;D. Toivola;J. A. O. Meriluoto;H. Karaki.
Biochemical and Biophysical Research Communications (1990)
Rho-associated Kinase of Chicken Gizzard Smooth Muscle
Jianhua Feng;Masaaki Ito;Yasuko Kureishi;Kazuhito Ichikawa.
Journal of Biological Chemistry (1999)
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