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Cathepsin B Is Dispensable for Cellular Processing of Cathepsin B-Cleavable Antibody–Drug Conjugates [PDF]
Cancer Research, 2017 Abstract Antibody–drug conjugates (ADC) are designed to selectively bind to tumor antigens via the antibody and release their cytotoxic payload upon internalization. Controllable payload release through judicious design of the linker has been an early technological milestone.
Thomas H. Pillow +14 more
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[41] Cathepsin B, cathepsin H, and cathepsin L
1981Publisher 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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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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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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Biochimica et Biophysica Acta (BBA) - General Subjects, 2003
Active cathepsin B has been found in cell extract and medium of human osteoblast-like cells and MG-63 cells. The released form is stable at neutral and alkaline pH and, in both cell types, intracellular and extracellular cathepsin B activities are increased by interleukin-1 beta (IL-1beta) and parathyroid hormone (PTH).
Aisa M. C. +3 more
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Active cathepsin B has been found in cell extract and medium of human osteoblast-like cells and MG-63 cells. The released form is stable at neutral and alkaline pH and, in both cell types, intracellular and extracellular cathepsin B activities are increased by interleukin-1 beta (IL-1beta) and parathyroid hormone (PTH).
Aisa M. C. +3 more
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Current Medicinal Chemistry, 2006
Cathepsin B is an abundant and ubiquitously expressed cysteine peptidase of the papain family. It is involved in many physiological processes, such as remodeling of the extracellular matrix (wound healing), apoptosis, and activation of thyroxine and renin.
Stanislav Gobec, Rok Frlan
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Cathepsin B is an abundant and ubiquitously expressed cysteine peptidase of the papain family. It is involved in many physiological processes, such as remodeling of the extracellular matrix (wound healing), apoptosis, and activation of thyroxine and renin.
Stanislav Gobec, Rok Frlan
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Cathepsin L, But Not Cathepsin B, Is a Potential Kininogenase
Biological Chemistry, 2001Although 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 +2 more
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Cathepsin B in Human Leukocytes
cclm, 1998Abstract We have applied a method using the fluorigenic substrate benzoloxycarbonyl-Arg-Arg-amido-4-methylcoumarin to measure cathepsin B, a thiol proteinase, in homogenates of human leukocytes. Data like pH optimum, stability, influence of thiol groups and effects of thiol proteinase inhibitors, lack of binding to Concanavalin A and ...
den Tandt, Wilfried, Scharpe, Simon
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Cathepsin-B activity in otosclerosis
Archives of Oto-Rhino-Laryngology, 1983Cathepsin-B activity was determined fluorimetrically in the otosclerotic stapes footplate, the stapes superstructure, normal temporal cortical bone, and os frontale osteoma. Measurements with a synthetic substrate made determinations in individual samples possible. The cathepsin-B activity in the otosclerotic stapes footplate was one order of magnitude
Ottó Ribári +3 more
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Angewandte Chemie, 2017
Until recently, chemiluminescence cell images could only be obtained using luciferase-activated probes. Moreover, chemiluminescence microscopy cell-imaging has not been demonstrated for natively expressed enzymes like cathepsin B. Herein, we describe the
Michal E Roth-Konforti +2 more
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Until recently, chemiluminescence cell images could only be obtained using luciferase-activated probes. Moreover, chemiluminescence microscopy cell-imaging has not been demonstrated for natively expressed enzymes like cathepsin B. Herein, we describe the
Michal E Roth-Konforti +2 more
semanticscholar +1 more source