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Molecular mechanisms of cell death: recommendations of the Nomenclature Committee on Cell Death 2018
An updated classification of cell death subroutines focusing on mechanistic and essential aspects of the process is proposed, and the utility of neologisms that refer to highly specialized instances of these processes are discussed.
Cysteine cathepsins: From structure, function and regulation to new frontiers☆
  • V. Turk, V. Stoka, +4 authors D. Turk
  • Biology, Medicine
    Biochimica et Biophysica Acta (BBA) - Proteins…
  • 12 October 2011
The view of cysteine cathepsins as lysosomal proteases is changing as there is now clear evidence of their localization in other cellular compartments, and some of the remarkable advances that have taken place in the past decade are presented.
Selective Disruption of Lysosomes in HeLa Cells Triggers Apoptosis Mediated by Cleavage of Bid by Multiple Papain-like Lysosomal Cathepsins*
It is shown that selective lysosome disruption with l-leucyl-l-leucine methyl ester results in apoptosis, characterized by translocation of lysOSomal proteases into the cytosol and by the cleavage of a proapoptotic Bcl-2-family member Bid.
Targeting proteases: successes, failures and future prospects
  • B. Turk
  • Biology, Medicine
    Nature Reviews Drug Discovery
  • 1 September 2006
The status of human protease research and prospects for future protease-targeted drugs are reviewed, with reference to some key examples where protease drugs have succeeded or failed.
Lysosomal cysteine proteases: more than scavengers.
The various physiological roles of mammalian lysosomal papain-like cysteine proteases as well as their mechanisms of action and the regulation of their activity are reviewed and discussed.
Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)
There continues to be confusion regarding acceptable methods to measure autophagy, especially in multicellular eukaryotes, so it is important to update guidelines for monitoring autophagic activity in different organisms.
Lysosomal Protease Pathways to Apoptosis
Data suggest that Bid represents a sensor that allows cells to initiate apoptosis in response to widespread adventitious proteolysis, supported by the finding that cytosolic extracts from mice ablated in the bid gene are impaired in the ability to release cytochrome c in Response to lysosome extracts.
Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors.
Among the lysosomal cysteine proteinases, cathepsin L was found to be the most active in degradation of protein substrates, such as collagen, elastin and azocasein, and the most abundant (Kirschke and Barrett, 1981).
Lysosomal cysteine proteases: facts and opportunities
From their discovery in the first half of the 20th century, lysosomal cysteine proteases have come a long way: from being the enzymes non‐selectively degrading proteins in lysosomes to being those
Structure of human dipeptidyl peptidase I (cathepsin C): exclusion domain added to an endopeptidase framework creates the machine for activation of granular serine proteases
It is suggested that the exclusion domain originates from a metallo‐protease inhibitor, characterized in people suffering from Haim–Munk and Papillon–Lefevre syndromes, suggests how they disrupt the fold and function of the enzyme.