Cystatins: biochemical and structural properties, and medical relevance.
@article{Turk2008CystatinsBA, title={Cystatins: biochemical and structural properties, and medical relevance.}, author={Vito Turk and Veronika Stoka and Du{\vs}an Turk}, journal={Frontiers in bioscience : a journal and virtual library}, year={2008}, volume={13}, pages={ 5406-20 } }
The cystatin superfamily comprises a large group of the cystatin domain containing proteins, present in a wide variety of organisms, including humans. Cystatin inhibitory activity is vital for the delicate regulation of normal physiological processes by limiting the potentially highly destructive activity of their target proteases such as the papain (C1) family, including cysteine cathepsins. Some of the cystatins also inhibit the legumain (C13) family of enzymes. Failures in biological…
300 Citations
Modelling family 2 cystatins and their interaction with papain
- Biology, ChemistryJournal of biomolecular structure & dynamics
- 2013
Using interaction energy, HB and solvent accessible surface area analyses, a series of key residues that may be involved in papain–cystatin interaction are identified and will improve the understanding of fundamental inhibitory mechanisms of cystatin.
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The role of cystatins in neurological diseases is considered to be highly significant as it pave the way for commanding tool in the drug design.
Journey of cystatins from being mere thiol protease inhibitors to at heart of many pathological conditions
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- 2017
A Brief Account of Structure-Function Relationship of the Traditional Cysteine Protease Inhibitor - Cystatin with a Special Focus on Human Family 1 and 2 Cystatins
- Biology, Chemistry
- 2017
Crystallographic and mutagenesis studies identify three conserved regions mainly involved in the interaction with papain (C1) family of CPs, namely, N-terminal region, L1 loop, and (c) L2 loop, which determined the wide-ranging affinity of cystatins toward papain family ofCPs.
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- Biology
- 2017
This chapter presents an overview of the structure, synthesis, mode of action, regulation of expression and activity, and physiological as well as pathological role of lysosomal cysteine cathepsins.
Molecular Cloning and Characterization of Cystatin, a Cysteine Protease Inhibitor, from Bufo melanostictus
- Biology, ChemistryBioscience, biotechnology, and biochemistry
- 2013
The novel cystatin cloned from a cDNA library of the skin of Bufo melanostictus can play an important role in host immunity and in the medical effect of B. melanstictus.
Functional characterization of single-domain cystatin-like cysteine proteinase inhibitors expressed by the trematode Fasciola hepatica
- BiologyParasitology
- 2017
The aim of this work is to characterize the cystatin repertoire of F. hepatica, and to suggest that it is secreted by non-classical secretory pathway and that it may interact with host lysosomal cysteine proteinases.
Cysteine cathepsins and cystatins: from ancillary tasks to prominent status in lung diseases
- Medicine, BiologyBiological chemistry
- 2015
A growing body of evidence supports the theory that cathepsins play specific functions in lung homeostasis and pathophysiological events such as asthma, lung fibrosis, chronic obstructive pulmonary disease, silicosis, bronchopulmonary dysplasia or tumor invasion.
Cystatins as regulators of cancer
- Biology, Chemistry
- 2017
Overexpression of cystatins has been found to inhibit metastasis and angiogenesis in certain cancers and may introduce future therapeutic advances in the control of cancer.
Cysteine cathepsins: From structure, function and regulation to new frontiers☆
- Biology, ChemistryBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 2012
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