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Projects / Programmes source: ARIS

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 (rules)
source: COBISS
Researchers (5)
no. Code Name and surname Research area Role Period No. of publicationsNo. of publications
1.  15970  Andreja Doberšek  Biochemistry and molecular biology  Researcher  1999 - 2001 
2.  12048  PhD Marjetka Podobnik  Biochemistry and molecular biology  Researcher  1998 - 2001 
3.  01092  PhD Alojzij Suhar  Biochemistry and molecular biology  Researcher  1998 - 2001 
4.  07561  PhD Boris Turk  Biochemistry and molecular biology  Researcher  1999 - 2001 
5.  04988  PhD Dušan Turk  Biochemistry and molecular biology  Head  1999 - 2001 
Organisations (1)
no. Code Research organisation City Registration number No. of publicationsNo. of publications
1.  0106  Jožef Stefan Institute  Ljubljana  5051606000  18 
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.
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