Results 21 to 30 of about 37,520 (214)

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

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

The calpastatin-derived calpain inhibitor CP1B reduces mRNA expression of matrix metalloproteinase-2 and-9 and invasion by leukemic THP-1 cells [PDF]

, 2003
The ubiquitous proteases μ- and m-calpain are Ca2+-dependent cysteine endopeptidases. Besides involvement in a variety of physio(patho)logical processes, recent studies suggest a pivotal role of calpains in differentiation of hematopoietic cells and ...
Ries, C., Gil-Parrado, S., Jochum, M., Heidinger, M., Ruiz-Heinrich, L., Popp, O.   +5 more
core   +1 more source

Characterization of mitochondrial calpain-5 [PDF]

, 2022
Calpain, a Ca2+-dependent cysteine protease, plays a significant role in gene expression, signal transduction, and apoptosis. Mutations in human calpain-5 cause autosomal dominant neovascular inflammatory vitreoretinopathy and the inhibition of calpain-5
CHUKAI, Yusaku, ITOH, Ken, TOMITA, Hiroshi, OZAKI, Taku, IWAMOTO, Takeshi   +4 more
core   +2 more sources

Calpain activity is negatively regulated by a KCTD7–Cullin-3 complex via non-degradative ubiquitination

Cell Discovery, 2023
Calpains are a class of non-lysosomal cysteine proteases that exert their regulatory functions via limited proteolysis of their substrates. Similar to the lysosomal and proteasomal systems, calpain dysregulation is implicated in the pathogenesis of ...
Jaiprakash Sharma, Shalaka Mulherkar, Uan-I Chen, Yan Xiong, Lakshya Bajaj, Byoung-Kyu Cho, Young Ah Goo, Hon-Chiu Eastwood Leung, Kimberley F. Tolias, Marco Sardiello   +9 more
doaj   +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

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

Activation of calpain-1 in human carotid artery atherosclerotic lesions

BMC Cardiovascular Disorders, 2009
Background In a previous study, we observed that oxidized low-density lipoprotein-induced death of endothelial cells was calpain-1-dependent. The purpose of the present paper was to study the possible activation of calpain in human carotid plaques, and ...
Pedro Luis M, Dias Nuno, Saido Takaomi C, Nitulescu Mihaela, Gonçalves Isabel, e Fernandes José, Ares Mikko PS, Pörn-Ares Isabella   +7 more
doaj   +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

Calpain Activity Is Generally Elevated during Transformation but Has Oncogene-Specific Biological Functions

Neoplasia: An International Journal for Oncology Research, 2004
Several oncogene and tumor-suppressor gene products are known substrates for the calpain family of cysteine proteases, and calpain is required for transformation by v-src and tumor invasion.
N.O. Carragher, B.D. Fonseca, M.C. Frame
doaj   +1 more source