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Projects / Programmes
Structural studies of lysosomal cysteine proteases and their inhibitors
Research activity
| Code | Science | Field | Subfield |
|---|---|---|---|
| 1.05.00 | Natural sciences and mathematics | Biochemistry and molecular biology |
| Code | Science | Field |
|---|---|---|
| P310 | Natural sciences and mathematics | Proteins, enzymology |
| B120 | Biomedical sciences | Molecular biophysics |
Keywords
proteases, inhibitors, cysteine, kathepsin, x-ray structures
Evaluation
(metodology)
Citations
Citations for bibliographic records in COBIB.SI that are linked to records in citation databases
Organisations (1) , Researchers (5)
0106 Jožef Stefan Institute
| no. | Code | Name and surname | Research area | Role | Period | No. of publicationsNo. of publications |
|---|---|---|---|---|---|---|
| 1. | 15970 | Biochemistry and molecular biology | Researcher | 1999 - 2001 | 25 | |
| 2. | 12048 | Biochemistry and molecular biology | Researcher | 1998 - 2001 | 351 | |
| 3. | 01092 | Biochemistry and molecular biology | Researcher | 1998 - 2001 | 46 | |
| 4. | 07561 | Biochemistry and molecular biology | Researcher | 1999 - 2001 | 1,067 | |
| 5. | 04988 | Biochemistry and molecular biology | Head | 1999 - 2001 | 648 |
Abstract
Intracellular protein degradation is part of cell methabolism. Lysosomal cysteine proteases degrade proteins to peptides and amino acids. Their activity is regulated by expression, processing, inhibitors and degradation. Determination of their 3-dimensional structures in the forms of proenzyme, mature enzye and in complexes with inhibitors allows us to understand the molecular events in atomic detail and therby support biochemical, medicinal and pharaceutical research and product development in the field.