Projects / Programmes
Human cathepsin F: An unusual cysteine protease involved in neurodegeneration
Code |
Science |
Field |
Subfield |
1.05.00 |
Natural sciences and mathematics |
Biochemistry and molecular biology |
|
Code |
Science |
Field |
1.06 |
Natural Sciences |
Biological sciences |
Cathepsin F, cysteine cathepsins, inhihitors, neuronal ceroid lipofuscinosis, Kufs disease, neurodegeneration, structure, substrate specificity
Data for the last 5 years (citations for the last 10 years) on
April 22, 2024;
A3 for period
2018-2022
Data for ARIS tenders (
04.04.2019 – Programme tender,
archive
)
Database |
Linked records |
Citations |
Pure citations |
Average pure citations |
WoS |
377 |
35,156 |
32,026 |
84.95 |
Scopus |
357 |
37,376 |
34,220 |
95.85 |
Researchers (8)
no. |
Code |
Name and surname |
Research area |
Role |
Period |
No. of publicationsNo. of publications |
1. |
00449 |
PhD Iztok Dolenc |
Biochemistry and molecular biology |
Researcher |
2020 - 2024 |
110 |
2. |
32503 |
PhD Katarina Karničar |
Biotechnology |
Researcher |
2020 - 2024 |
24 |
3. |
55799 |
Tea Sinožić |
Biochemistry and molecular biology |
Junior researcher |
2022 - 2024 |
5 |
4. |
14829 |
PhD Veronika Stoka |
Biochemistry and molecular biology |
Head |
2020 - 2024 |
237 |
5. |
15969 |
Ivica Štefe |
Biochemistry and molecular biology |
Technical associate |
2020 - 2024 |
36 |
6. |
07561 |
PhD Boris Turk |
Biochemistry and molecular biology |
Researcher |
2020 - 2024 |
1,037 |
7. |
04988 |
PhD Dušan Turk |
Biochemistry and molecular biology |
Researcher |
2020 - 2024 |
621 |
8. |
33762 |
PhD Robert Vidmar |
Biochemistry and molecular biology |
Researcher |
2020 - 2024 |
148 |
Organisations (2)
Abstract
Lysosomal cysteine cathepsins play key roles in various physiological and pathological processes, including aging, neurodegeneration and genetic diseases. Their disregulated activities result in numerous human diseases and consequently are promising drug targets. Among eleven human cysteine cathepsins, cathepsin F is one of the less studied and characterized proteases. The recent discovery of several mutations within the human cathepsin F gene was a significant breakthrough that has provided strong evidence that this enzyme is associated with Type B Kufs disease, an adult onset neuronal ceroid lipofuscinosis (CLN13), and other neurodegenerative disorders. The major focus of this research will be to study the effects of cathepsin F mutations on enzyme activity, processing of cathepsin F proenzyme and the biological role of its proregion containing a cystatin-like domain. In addition we will determine the structures of procathepsin F and mature cathepsin F in complex with its inhibitor(s) and specific substrates. The results will provide insight into the cathepsin F functional network at the molecular level, which serves as a general model system for NCLs and other neurodegenerative diseases. Our integrative approach will map out the topological and dynamic properties of the underlying biological networks. The project combines various fields of expertise such as biochemistry including proteomics, molecular and cell biology, X-ray crystallography and bioinformatics. The results of these studies will not only impact basic science but also provide important information contributing to the development of treatment strategies for Type B Kufs disease and other neurodegenerative diseases.