Results 71 to 80 of about 623 (108)

Exploring the relationship between cathepsin and age-related macular degeneration using Mendelian randomization

Frontiers in Medicine
PurposeAge-related macular degeneration (AMD) is the leading cause of low vision and even blindness in the elderly population worldwide. However, no studies have been conducted to analyze the causal relationship between the cathepsin family and AMD.
Qiuyuan Wang, Qiuyuan Wang, Shanjun Cai
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Unveiling the Roles of Cysteine Proteinases F and W: From Structure to Pathological Implications and Therapeutic Targets

Cells
Cysteine cathepsins F and W are members of the papain-like cysteine protease family, which have distinct structural features and functional roles in various physiological and pathological processes.
Kristina Zdravkova, Olja Mijanovic, Ana Brankovic, Polina M. Ilicheva, Aleksandra Jakovleva, Jelena Karanovic, Milena Pualic, Dusan Pualic, Aleksandr A. Rubel, Lyudmila V. Savvateeva, Alessandro Parodi, Andrey A. Zamyatnin   +11 more
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Genetic Insights Into the Role of Cathepsins in Alzheimer's Disease, Parkinson's Disease, and Amyotrophic Lateral Sclerosis: Evidence From Mendelian Randomization Study

Brain and Behavior
Background Previous studies have confirmed the significant role of cathepsins in the development of neurodegenerative diseases. We aimed to determine whether genetically predicted 10 cathepsins may have a causal effect on Alzheimer's disease (AD ...
Yanhong Jiang, Wenhui Fan, Yaxin Li, Hua Xue   +3 more
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SPECIFICITY OF CATHEPSIN C

Journal of Biological Chemistry, 1956
Nobuo Izumiya, Joseph S. Fruton
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Cathepsins in the osteoclast

Journal of Electron Microscopy, 2003
The mechanism by which bone collagen and other organic components are degraded by the osteoclast during osteoclastic bone resorption was unclear until the 1980s. Studies conducted since the early 1990s have identified lysosomal proteases, mainly cathepsins that are active at low pH, involved in osteoclastic bone resorption.
Teruo Tanaka, Takayoshi Yamaza, Tetsuya Goto   +2 more
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Cathepsin L, But Not Cathepsin B, Is a Potential Kininogenase

Biological Chemistry, 2001
Although papain-like enzymes are strongly inhibited by their natural tight-binding inhibitors of the cystatin superfamily, cathepsins B and L may still retain some residual proteolytic activity toward Z-Phe-Arg-AMC in the presence of an excess of kininogen. This activity is abolished by adding E-64 or chicken cystatin.
Francis Gauthier, Gilles Lalmanach, Claire Desmazes   +2 more
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Improved purification of cathepsin B1 and cathepsin B2

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
An improved purification of the cathepsins B1 and B2 from bovine spleen is described. In addition to the formerly used procedure, chromatography with DEAE-Sephadex or -cellulose and mercurated agarose is used. Both enzymes are obtained in an electrophoretically pure form but consist of two or more isoenzymes.
Klaus Otto, Horst Riesenkönig
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Cathepsin B

The International Journal of Biochemistry & Cell Biology, 1997
Cathepsin B is a lysosomal cysteine protease of the papain family. It functions in intracellular protein catabolism and in certain situations may also be involved in other physiological processes, such as processing of antigens in the immune response, hormone activation and bone turnover.
J S, Mort, D J, Buttle
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[41] Cathepsin B, cathepsin H, and cathepsin L

1981
Publisher Summary This chapter describes two types of purification methods for Cathepsin B, Cathepsin H, and Cathepsin L. Method I is applicable to large amounts of frozen tissues, whereas method II is used with flesh tissue and takes advantage of a 50-fold purification factor attainable by isolation of lysosomes: it has the further advantage of ...
Heidrun Kirschke, Alan J. Barrett
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Cathepsin K and the Design of Inhibitors of Cathepsin K

Current Pharmaceutical Design, 2000
Cathepsin K, a cysteine protease of the papain family, was identified by sequencing complementary DNA libraries derived from osteoclasts. Cathepsin K can cleave bone proteins such as Type I collagen, osteopontin, and osteonectin. The localization and maturation of cathepsin K in activated osteoclasts have been characterized.
Robert Dodds, Dennis Yamashita
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