Results 21 to 30 of about 49,188 (286)

Changes in neurodegeneration-related miRNAs in brains from CAPN1−/− mice

BBA Advances, 2021
Calpain-1 knock-out (KO) mice exhibit enhanced susceptibility to neurodegeneration due to the lack of the neuroprotective function of calpain-1. Dicer has been shown to play a fundamental role in the biogenesis of most miRNAs.
Wenyue Su, Xiaoning Bi, Yubin Wang, Michel Baudry   +3 more
doaj   +1 more source

Calpain: the regulatory point of myocardial ischemia-reperfusion injury

Frontiers in Cardiovascular Medicine, 2023
Calpain is a conserved cysteine protease readily expressed in several mammalian tissues, which is usually activated by Ca2+ and with maximum activity at neutral pH.
Guo-Yang Liu, Guo-Yang Liu, Guo-Yang Liu, Wan-Li Xie, Wan-Li Xie, Wan-Li Xie, Yan-Ting Wang, Yan-Ting Wang, Yan-Ting Wang, Lu Chen, Lu Chen, Lu Chen, Zhen-Zhen Xu, Zhen-Zhen Xu, Zhen-Zhen Xu, Yong Lv, Yong Lv, Yong Lv, Qing-Ping Wu, Qing-Ping Wu, Qing-Ping Wu   +20 more
doaj   +1 more source

Calpain cleavage of Junctophilin-2 generates a spectrum of calcium-dependent cleavage products and DNA-rich NT1-fragment domains in cardiomyocytes

Scientific Reports, 2022
Calpains are calcium-activated neutral proteases involved in the regulation of key signaling pathways. Junctophilin-2 (JP2) is a Calpain-specific proteolytic target and essential structural protein inside Ca2+ release units required for excitation ...
Gunnar Weninger, Tatiana Pochechueva, Dana El Chami, Xiaojing Luo, Tobias Kohl, Sören Brandenburg, Henning Urlaub, Kaomei Guan, Christof Lenz, Stephan E. Lehnart   +9 more
doaj   +1 more source

Cystatins as calpain inhibitors: Engineered chicken cystatin- and stefin B-kininogen domain 2 hybrids support a cystatin-like mode of interaction with the catalytic subunit of μ-calpain [PDF]

, 2001
Within the cystatin superfamily, only kininogen domain 2 (KD2) is able to inhibit μ- and m-calpain. In an attempt to elucidate the structural requirements of cystatins for calpain inhibition, we constructed recombinant hybrids of human stefin B (an ...
Gross, Stefan, Machleidt, Werner, Assfalg-Machleidt, Irmgard, Pfeiler, Dietmar, Gabrijelcic-Geiger, Dusica, Gollmitzer, Nicole, García Diaz, Beatriz, Auerswald, Ennes A., Stubbs, Milton T., Fritz, Hans   +9 more
core   +1 more source

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

GPS-CCD: a novel computational program for the prediction of calpain cleavage sites. [PDF]

PLoS ONE, 2011
As one of the most essential post-translational modifications (PTMs) of proteins, proteolysis, especially calpain-mediated cleavage, plays an important role in many biological processes, including cell death/apoptosis, cytoskeletal remodeling, and the ...
Zexian Liu, Jun Cao, Xinjiao Gao, Qian Ma, Jian Ren, Yu Xue   +5 more
doaj   +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

Novel insights into the progression and prognosis of the calpain family members in hepatocellular carcinoma: a comprehensive integrated analysis

Frontiers in Molecular Biosciences, 2023
Objectives: The goal of our bioinformatics study was to comprehensively analyze the association between the whole calpain family members and the progression and prognosis of hepatocellular carcinoma (HCC).Methods: The data were collected from The Cancer ...
Dongjun Dai, Dongjun Dai, Dehao Wu, Runliang Ni, Runliang Ni, Ping Li, Ping Li, Zhifeng Tian, Zhifeng Tian, Yongjie Shui, Hanguang Hu, Hanguang Hu, Qichun Wei, Qichun Wei   +13 more
doaj   +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