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Vito Turk

Researcher at Jožef Stefan Institute

Publications -  272
Citations -  25567

Vito Turk is an academic researcher from Jožef Stefan Institute. The author has contributed to research in topics: Cathepsin & Cathepsin B. The author has an hindex of 74, co-authored 271 publications receiving 23205 citations. Previous affiliations of Vito Turk include Siberian State Medical University.

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Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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Cysteine cathepsins: From structure, function and regulation to new frontiers

TL;DR: 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.
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Lysosomal cysteine proteases: more than scavengers.

TL;DR: 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.
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The cystatins: protein inhibitors of cysteine proteinases.

TL;DR: Recently determined crystal structures of chicken cystatin and human stefin B established a new mechanism of interaction between cysteine proteinases and their inhibitors which is fundamentally different from the standard mechanism for serine proteinase inhibitors and their inhibitor.