[HTML][HTML] Cysteine cathepsins: from structure, function and regulation to new frontiers

V Turk, V Stoka, O Vasiljeva, M Renko, T Sun… - … et Biophysica Acta (BBA …, 2012 - Elsevier
It is more than 50years since the lysosome was discovered. Since then its hydrolytic
machinery, including proteases and other hydrolases, has been fairly well identified and …

[HTML][HTML] Cysteine proteases: modes of activation and future prospects as pharmacological targets

S Verma, R Dixit, KC Pandey - Frontiers in pharmacology, 2016 - frontiersin.org
Proteolytic enzymes are crucial for a variety of biological processes in organisms ranging
from lower (virus, bacteria, and parasite) to the higher organisms (mammals). Proteases …

Proteolytic networks in cancer

SD Mason, JA Joyce - Trends in cell biology, 2011 - cell.com
Proteases are important for multiple processes during malignant progression, including
tumor angiogenesis, invasion and metastasis. Recent evidence reveals that tumor …

[HTML][HTML] Specialized roles for cysteine cathepsins in health and disease

J Reiser, B Adair, T Reinheckel - The Journal of clinical …, 2010 - Am Soc Clin Investig
Cathepsins were originally identified as proteases that act in the lysosome. Recent work has
uncovered nontraditional roles for cathepsins in the extracellular space as well as in the …

The role of lysosomal cysteine cathepsins in NLRP3 inflammasome activation

RI Campden, Y Zhang - Archives of Biochemistry and Biophysics, 2019 - Elsevier
Lysosomal cysteine cathepsins are a family of proteases that are involved in a myriad of
cellular processes from proteolytic degradation in the lysosome to bone resorption. These …

Proteolytic Cleavage Mechanisms, Function, and “Omic” Approaches for a Near-Ubiquitous Posttranslational Modification

T Klein, U Eckhard, A Dufour, N Solis… - Chemical …, 2018 - ACS Publications
Proteases enzymatically hydrolyze peptide bonds in substrate proteins, resulting in a
widespread, irreversible posttranslational modification of the protein's structure and …

[PDF][PDF] Cystatins: biochemical and structural properties, and medical relevance

V Turk, V Stoka, D Turk - Front Biosci, 2008 - article.imrpress.com
Introduction 3. Discovery of the cystatin superfamily 4. Evolution and classification of the
cystatin superfamily 5. General properties of the cystatin superfamily 5.1. Type 1 cystatins …

Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators

B Turk, D Turk, GS Salvesen - Current pharmaceutical design, 2002 - ingentaconnect.com
Cysteine proteases are widespread in nature. Their implication in numerous vital processes
and pathologies make them highly attractive targets for drug design. The proper functioning …

Cathepsin V: Molecular characteristics and significance in health and disease

F Lecaille, T Chazeirat, A Saidi, G Lalmanach - Molecular Aspects of …, 2022 - Elsevier
Human cysteine cathepsins form a family of eleven proteases (B, C, F, H, K, L, O, S, V, W,
X/Z) that play important roles in a considerable number of biological and pathophysiological …

Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease

DP Dickinson - Critical Reviews in Oral Biology & Medicine, 2002 - journals.sagepub.com
Cysteine peptidases (CPs) are phylogenetically ubiquitous enzymes that can be classified
into clans of evolutionarily independent proteins based on the structural organization of the …