Results 31 to 40 of about 29,724,597 (193)

Identification of calpain cleavage sites in the G1 cyclin-dependent kinase inhibitor p19(INK4d) [PDF]

, 2006
Calpains are a large family of Ca2+-dependent cysteine proteases that are ubiquitously distributed across most cell types and vertebrate species. Calpains play a role in cell differentiation, apoptosis, cytoskeletal remodeling, signal transduction and ...
Popp, Oliver, Nalabothula, Narasimharao, Gil-Parrado, S., Jochum, M., Ghosh, M., Machleidt, W., Machleidt, Werner, Ghosh, Madhumita, Gil-Parrado, Shirley, Holak, Tad A., Joy, J., Joy, Joma, Holak, T. A., Jochum, Marianne, Popp, O., Nalabothula, N.   +15 more
core   +1 more source

Inhibition of human mu-calpain by conformationally constrained calpastatin peptides [PDF]

, 2008
Pfizer J, Assfalg-Machleidt I, Machleidt W, Schaschke N. Inhibition of human mu-calpain by conformationally constrained calpastatin peptides. BIOLOGICAL CHEMISTRY.
Machleidt, Werner, Schaschke, Norbert, Assfalg-Machleidt, Irmgard, Pfizer, Jose   +3 more
core   +1 more source

Proteolysis of insulin-like growth factor binding proteins (IGFBPs) by calpain [PDF]

, 2005
Calpains are non-lysosomal, Ca2+-dependent cysteine proteases, which are ubiquitously distributed across cell types and vertebrate species. The rules that govern calpain specificity have not yet been determined.
Mann, Karlheinz, Mann, K., Ghosh, M., Machleidt, W., Machleidt, Werner, Siwanowicz, I., Ghosh, Madhumita, Holak, Tad A., Holak, T. A., Holak, T., Siwanowicz, Igor, Shanker, Sreejesh, Shanker, S.   +12 more
core   +1 more source

μ-calpain binds to lipid bilayers via the exposed hydrophobic surface of its Ca2+-activated conformation [PDF]

, 2006
μ- and m-calpain are cysteine proteases requiring micro- and millimolar Ca2+ concentrations for their activation in vitro. Among other mechanisms, interaction of calpains with membrane phospholipids has been proposed to facilitate their activation by ...
Machleidt, Werner, Assfalg-Machleidt, Irmgard, Fernández-Montalván, Amaury, Pfeiler, Dietmar, Jochum, Marianne, Fritz, Hans   +5 more
core   +1 more source

Calpastatin exon 1B-derived peptide, a selective inhibitor of calpain: Enhancing cell permeability by conjugation with penetratin [PDF]

, 2003
Gil-Parrado S, Assfalg-Machleidt I, Fiorino F, et al. Calpastatin exon 1B-derived peptide, a selective inhibitor of calpain: Enhancing cell permeability by conjugation with penetratin. BIOLOGICAL CHEMISTRY.
Dominga Deluca, Schaschke, N., Gil-Parrado, S, Werner M.a.c.h.l.e.i.d.t., Luis Moroder, Dietmar Pfeiler, Irmgard Assfalg Machleidt, Machleidt, Werner, Fiorino, F, Pfeiler, D., Pfeiler, D, Machleidt, W, Schaschke, Norbert, Assfalg-Machleidt, Irmgard, Moroder, L, Deluca, D, Gil-Parrado, S., Moroder, L., Machleidt, W., Fiorino, F., Assfalg-Machleidt, I, Norbert Schaschke, Deluca, D., Assfalg-Machleidt, I., FIORINO, FERDINANDO, Shirley Gil Parrado   +25 more
core   +1 more source

Calpain system protein expression and activity in ovarian cancer [PDF]

, 2019
Purpose: Expression of members of the calpain system are associated with clinical outcome of patients with, amongst others, breast and ovarian cancer, with calpain-2 expression in ovarian cancer being implicated in chemo-resistance and survival.
Nicholls, Holly, Zhang, Siwei, Chondrou, Panagiota S., Rungsakaolert, Ployphailin, Martin, Stewart G., Yao, Anqi, Storr, Sarah J., Deen, Suha   +7 more
core   +1 more source

Human μ-calpain: Simple isolation from erythrocytes and characterization of autolysis fragments [PDF]

, 2001
Heterodimeric μ-calpain, consisting of the large (80 kDa) and the small (30 kDa) subunit, was isolated and purified from human erythrocytes by a highly reproducible four-step purification procedure.
Mentele, Reinhard, Hinz, Heide, Machleidt, Werner, Assfalg-Machleidt, Irmgard, Gabrijelcic-Geiger, Dusica, Auerswald, Ennes A., Möller, Achim, Meisel, Barbara   +7 more
core   +1 more source

Reduction of myocardial infarction by calpain inhibitors A-705239 and A-705253 in isolated perfused rabbit hearts [PDF]

, 2004
Two novel calpain inhibitors (A-705239 and A-705253) were studied in isolated perfused rabbit hearts subjected to 60-min occlusion of the ramus interventricularis of the left coronary artery (below the origin of the first diagonal branch), followed by ...
Speth, Maria, Deibele, Karin, Neuhof, Heinz, Lubisch, Wilfried, Möller, Achim, Neuhof, Christiane, Fabiunke, Verena, Fritz, Hans, Tillmanns, Harald, Maria Speth, Heinz Neuhof, Hans Fritz, Christiane Neuhof, Verena Fabiunke, Harald Tillmanns   +14 more
core   +1 more source

Characterisation and expression of calpain family members in relation to nutritional status, diet composition and flesh texture in gilthead sea bream (Sparus aurata). [PDF]

, 2013
Calpains are non-lysosomal calcium-activated neutral proteases involved in a wide range of cellular processes including muscle proteolysis linked to post-mortem flesh softening.
Encarnación Capilla (462852), Fontanillas, Ramon, Navarro Álvarez, Isabel, Salmerón Salvador, Cristina, Salmeron, Cristina, Navarro Isabel, Gutierrez, Joaquim, Isabel Navarro (462849), Daniel García de la serrana (5656525), Ramón Fontanillas (462847), García de la serrana Daniel, Jiménez-Amilburu Vanesa, García de la Serrana Castillo, Daniel, Vanesa Jiménez-Amilburu, Fontanillas Ramón, Jimenez-Amilburu, Vanesa, Ian A. Johnston, Gutiérrez Joaquim, Joaquim Gutiérrez, Capilla, Encarnacion, Ramón Fontanillas, Cristina Salmerón (462843), Gutiérrez Fruitós, Joaquín, Navarro, Isabel, Encarnación Capilla, Salmerón Cristina, Capilla Campos, Encarnación, Ian A. Johnston (39412), Johnston, Ian A., Isabel Navarro, Vanesa Jiménez-Amilburu (462845), Cristina Salmerón, Capilla Encarnación, Johnston Ian A., Jiménez-Amilburu, V., Daniel García de la serrana, Joaquim Gutiérrez (368250), Ian A Johnston, Cristina Salmerón   +38 more
core   +2 more sources

Reduction of myocardial infarction by postischemic administration of the calpain inhibitor A-705253 in comparison to the Na(+)/H(+) exchange inhibitor Cariporide (R) in isolated perfused rabbit hearts [PDF]

, 2008
The calpain inhibitor A-705253 and the Na(+)/H(+) exchange inhibitor Cariporide (R) were studied in isolated perfused rabbit hearts subjected to 60 min occlusion of the ramus interventricularis of the left coronary artery (below the origin of the first ...
Speth, Maria, Erdogan, Ali, Neuhof, Heinz, Neuhof, Christiane, Fabiunke, Verena, Fritz, Hans, Moeller, Achim, Tillmanns, Harald   +7 more
core   +1 more source