Evidence map›Paper›PMID 22024571›Full record

ReviewBiochimica et biophysica acta2012

Cysteine cathepsins: from structure, function and regulation to new frontiers.

Vito Turk, Veronika Stoka, Olga Vasiljeva, Miha Renko, Tao Sun, Boris Turk, Dušan Turk

Open access · hybridAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 636 papers.

0numbers the graph read from it
0cells of the map it votes in
636citing papers in PubMed
15.7field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

636 citing papers in PubMed, 1,333 citations in OpenAlex.

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  12. Monoterpene-Rich Nanoemulsion fromMolecules (Basel, Switzerland) · 2026
    Article
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576 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Vito TurkDepartment of Biochemistry and Molecular and Structural Biology, J. Stefan Institute, Ljubljana, Slovenia. dusan.turk@ijs.si
Veronika Stoka
Olga Vasiljeva
Miha Renko
Tao Sun
Boris Turk
Dušan Turk
Jožef Stefan Institute · SICentre of Excellence for Integrated Approaches in Chemistry and Biology of Proteins · SI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

It is more than 50 years since the lysosome was discovered. Since then its hydrolytic machinery, including proteases and other hydrolases, has been fairly well identified and characterized. Among these are the cysteine cathepsins, members of the family of papain-like cysteine proteases. They have unique reactive-site properties and an uneven tissue-specific expression pattern. In living organisms their activity is a delicate balance of expression, targeting, zymogen activation, inhibition by protein inhibitors and degradation. The specificity of their substrate binding sites, small-molecule inhibitor repertoire and crystal structures are providing new tools for research and development. Their unique reactive-site properties have made it possible to confine the targets simply by the use of appropriate reactive groups. The epoxysuccinyls still dominate the field, but now nitriles seem to be the most appropriate "warhead". The view of cysteine cathepsins as lysosomal proteases is changing as there is now clear evidence of their localization in other cellular compartments. Besides being involved in protein turnover, they build an important part of the endosomal antigen presentation. Together with the growing number of non-endosomal roles of cysteine cathepsins is growing also the knowledge of their involvement in diseases such as cancer and rheumatoid arthritis, among others. Finally, cysteine cathepsins are important regulators and signaling molecules of an unimaginable number of biological processes. The current challenge is to identify their endogenous substrates, in order to gain an insight into the mechanisms of substrate degradation and processing. In this review, some of the remarkable advances that have taken place in the past decade are presented. This article is part of a Special Issue entitled: Proteolysis 50 years after the discovery of lysosome.

Indexed as

Amino Acid SequenceAnimalsCathepsinsCell BiologyCysteine ProteasesGene Expression Regulation, EnzymologicHumansModels, BiologicalModels, MolecularMolecular Sequence DataProtein ConformationSequence Homology, Amino AcidStructure-Activity RelationshipCathepsinsCysteine Proteases

Identifiers

PMID22024571
PMCPMC7105208
OpenAlexW2075729810

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.