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Cysteine proteases of parasitic organisms

Molecular and Biochemical Parasitology, 2002
Cysteine proteases play numerous indispensable roles in the biology of parasitic organisms. Aside from previously known general catabolic functions and protein processing, cysteine proteases may be key to parasite immunoevasion, excystment/encystment, exsheathing and cell and tissue invasion.
M, Sajid, J H, McKerrow
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Papain‐like Cysteine Proteases

Current Protocols in Protein Science, 2000
AbstractThe name “cysteine protease“ refers to the protease's nucleophilic cysteine residue that forms a covalent bond with the carbonyl group of the scissile peptide bond in substrates. The papain‐like cysteine proteases, classified as the “C1 family” are the most predominant cysteine proteases.
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Microbial inhibitors of cysteine proteases

Medical Microbiology and Immunology, 2016
Cysteine proteases are one of the major classes of proteolytic enzymes involved in a number of physiological and pathological processes in plants, animals and microorganisms. When their synthesis, activity and localization in mammalian cells are altered, they may contribute to the development of many diseases, including rheumatoid arthritis ...
Mateusz, Kędzior   +2 more
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Michael Acceptors as Cysteine Protease Inhibitors

Mini-Reviews in Medicinal Chemistry, 2007
Cysteine proteases selectively catalyze the hydrolysis of peptide bonds. Uncontrolled, unregulated, or undesired proteolysis can lead to many disease states including emphysema, stroke, viral infections, cancer, Alzheimer's disease, inflammation, and arthritis.
Santos, Maria M. M., Moreira, Rui
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Lysosomal cysteine proteases: more than scavengers

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 2000
Lysosomal cysteine proteases were believed to be mainly involved in intracellular protein degradation. Under special conditions they have been found outside lysosomes resulting in pathological conditions. With the discovery of a series of new cathepsins with restricted tissue distributions, it has become evident that these enzymes must be involved in a
B, Turk, D, Turk, V, Turk
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Cysteine Protease Inhibitors Containing Small Rings

Mini-Reviews in Medicinal Chemistry, 2003
Since the discovery of E-64 in 1978 as potent cysteine protease inhibitor a variety of inhibitors containing small rings as electrophilic building blocks responsible for enzyme inhibition have been developed. In this review we summarize new aspects concerning epoxysuccinyl peptides derived from E-64 and discuss inhibition potency, selectivity and ...
T, Schirmeister, A, Klockow
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The apoptotic cysteine protease CPP32

The International Journal of Biochemistry & Cell Biology, 1997
CPP32 (also called Yama and apopain) is a member of a growing family of cysteine proteases which includes the interleukin-1 beta-converting enzyme (ICE) and the product of the Caenorhabditis elegans cell death gene ced-3. CPP32 has been consistently implicated as a key protease of the ICE/CED-3 family that is activated in response to a variety of death
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Organic Azide Inhibitors of Cysteine Proteases

Journal of the American Chemical Society, 2006
Cysteine proteases are crucial regulatory enzymes in human physiology and disease. Inhibitors are usually designed with reactive electrophiles to covalently bond to the catalytic cysteinyl sulfur, and consequently they also indiscriminately interact with biological thiolates and other nucleophiles, leading to toxic side effects in vivo.
Le, G. T.   +4 more
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Non-Peptidic Inhibitors of Cysteine Proteases

Mini-Reviews in Medicinal Chemistry, 2003
In comparison to the huge number of peptidic and peptidomimetic inhibitors of cysteine proteases which have been developed during the last twenty years the number of non-peptidic compounds with cysteine protease inhibiting properties is restricted to a few substance classes.
T, Schirmeister, U, Kaeppler
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Cysteine proteases of malaria parasites

International Journal for Parasitology, 2004
A number of cysteine proteases of malaria parasites have been described, and many more putative cysteine proteases are suggested by analysis of the Plasmodium falciparum genome sequence. Studies with protease inhibitors have suggested roles for cysteine proteases in hemoglobin hydrolysis, erythrocyte rupture, and erythrocyte invasion by erythrocytic ...
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