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- Publications
- Influence
Calpains: an elaborate proteolytic system.
- Y. Ono, H. Sorimachi
- Medicine, Biology
- Biochimica et biophysica acta
- 2012
Calpain is an intracellular Ca(2+)-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02). Recent expansion of sequence data across the species definitively shows that calpain has been… Expand
TAL1 and LIM-Only Proteins Synergistically Induce Retinaldehyde Dehydrogenase 2 Expression in T-Cell Acute Lymphoblastic Leukemia by Acting as Cofactors for GATA3
- Y. Ono, N. Fukuhara, O. Yoshie
- Biology, Medicine
- Molecular and Cellular Biology
- 1 December 1998
ABSTRACT Previously, we have shown that TAL1 and the LIM-only protein gene (LMO) are regularly coactivated in T-cell acute lymphoblastic leukemia (T-ALL). This observation is likely to relate to the… Expand
Calpain research for drug discovery: challenges and potential
- Y. Ono, T. Saido, H. Sorimachi
- Biology, Medicine
- Nature Reviews Drug Discovery
- 1 December 2016
Calpains are a family of proteases that were scientifically recognized earlier than proteasomes and caspases, but remain enigmatic. However, they are known to participate in a multitude of… Expand
Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis.
- Suguru Koyama, S. Hata, +14 authors H. Sorimachi
- Biology, Medicine
- Journal of molecular biology
- 7 March 2008
During pathophysiological muscle wasting, a family of ubiquitin ligases, including muscle RING-finger protein-1 (MuRF1), has been proposed to trigger muscle protein degradation via ubiquitination.… Expand
Impact of genetic insights into calpain biology.
- H. Sorimachi, S. Hata, Y. Ono
- Biology, Medicine
- Journal of biochemistry
- 1 July 2011
Calpain has long been an enigmatic enzyme, although it is involved in a variety of biological phenomena. Recent progress in calpain genetics has highlighted numerous physiological contexts in which… Expand
Phosphorylation of protein kinase N by phosphoinositide-dependent protein kinase-1 mediates insulin signals to the actin cytoskeleton.
- L. Dong, L. Landa, +4 authors F. Liu
- Biology, Medicine
- Proceedings of the National Academy of Sciences…
- 9 May 2000
Growth factors such as insulin regulate phosphatidylinositol 3-kinase-dependent actin cytoskeleton rearrangement in many types of cells. However, the mechanism by which the insulin signal is… Expand
Calpain chronicle—an enzyme family under multidisciplinary characterization
- H. Sorimachi, Shoji Hata, Y. Ono
- Biology, Medicine
- Proceedings of the Japan Academy. Series B…
- 10 June 2011
Calpain is an intracellular Ca2+-dependent cysteine protease (EC 3.4.22.17; Clan CA, family C02) discovered in 1964. It was also called CANP (Ca2+-activated neutral protease) as well as CASF, CDP,… Expand
Specific interaction of the potassium channel beta-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system.
- T. Furukawa, Y. Ono, +6 authors C. Gregorio
- Biology, Medicine
- Journal of molecular biology
- 2 November 2001
Ion-channel beta-subunits are ancillary proteins that co-assemble with alpha-subunits to modulate gating kinetics and enhance stability of multimeric channel complexes. They provide binding sites for… Expand
Possible Regulation of the Conventional Calpain System by Skeletal Muscle-specific Calpain, p94/Calpain 3*
- Y. Ono, K. Kakinuma, +6 authors H. Sorimachi
- Biology, Medicine
- Journal of Biological Chemistry
- 23 January 2004
p94 (also called calpain 3) is the skeletal muscle-specific calpain and is considered to be a “modulator protease” in various cellular processes. Analysis of p94 at the protein level is an urgent… Expand
Expanding members and roles of the calpain superfamily and their genetically modified animals.
- H. Sorimachi, S. Hata, Y. Ono
- Biology, Medicine
- Experimental animals
- 2010
Calpains are intracellular Ca²(+)-dependent cysteine proteases (Clan CA, family C02, EC 3.4.22.17) found in almost all eukaryotes and some bacteria. Calpains display limited proteolytic activity at… Expand