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Projects / Programmes source: ARIS

Proteolysis

Periods
Research activity

Code Science Field Subfield
1.05.00  Natural sciences and mathematics  Biochemistry and molecular biology   
4.06.00  Biotechnical sciences  Biotechnology   

Code Science Field
P310  Natural sciences and mathematics  Proteins, enzymology 
B470  Biomedical sciences  Physiology 
B200  Biomedical sciences  Cytology, oncology, cancerology 
T490  Technological sciences  Biotechnology 
B725  Biomedical sciences  Diagnostics 
Evaluation (rules)
source: COBISS
Researchers (36)
no. Code Name and surname Research area Role Period No. of publicationsNo. of publications
1.  12047  PhD Tadeja Bevec  Pharmacy  Researcher  2001 - 2002  36 
2.  23572  PhD Lea Bojič  Pharmacy  Researcher  2003  35 
3.  23573  PhD Dejan Caglič  Biochemistry and molecular biology  Researcher  2003  53 
4.  19331  PhD Tina Cirman  Microbiology and immunology  Researcher  2001 - 2003  52 
5.  00449  PhD Iztok Dolenc  Biochemistry and molecular biology  Researcher  2001 - 2003  110 
6.  06416  PhD Marko Dolinar  Biochemistry and molecular biology  Researcher  2001 - 2003  344 
7.  18801  PhD Marko Fonović  Biochemistry and molecular biology  Researcher  2001 - 2003  189 
8.  18284  PhD Katja Galeša  Biochemistry and molecular biology  Researcher  2001 - 2002  39 
9.  20211  PhD Uroš Gregorc  Biotechnology  Researcher  2001 - 2003  31 
10.  18285  MSc Mirjana Grujić  Biochemistry and molecular biology  Researcher  2001 - 2003  12 
11.  19332  PhD Manca Kenig  Biochemistry and molecular biology  Researcher  2001 - 2003  36 
12.  10502  PhD Nataša Kopitar Jerala  Biochemistry and molecular biology  Researcher  2001 - 2003  239 
13.  04648  PhD Janko Kos  Biotechnical sciences  Researcher  2001 - 2003  1,166 
14.  22312  PhD Gregor Kosec  Biotechnology  Researcher  2002 - 2003  129 
15.  17110  Louisa Johanna Kroon Žitko    Researcher  2001 - 2003  22 
16.  23574  PhD Tomaž Langerholc  Biotechnology  Researcher  2003  289 
17.  03422  PhD Brigita Lenarčič  Biochemistry and molecular biology  Researcher  2001 - 2003  338 
18.  22318  PhD Primož Meh  Pharmacy  Researcher  2002 - 2003  14 
19.  23575  PhD Miha Pavšič  Biochemistry and molecular biology  Researcher  2003  204 
20.  19366  PhD Aleš Premzl  Pharmacy  Researcher  2001 - 2003  81 
21.  09091  PhD Vida Puizdar  Biochemistry and molecular biology  Researcher  2001 - 2003  55 
22.  15286  PhD Galina Pungerčič  Biochemistry and molecular biology  Researcher  2001 - 2002  37 
23.  22321  PhD Sabina Rabzelj  Biochemistry and molecular biology  Researcher  2002 - 2003  43 
24.  06056  PhD Metka Renko  Biochemistry and molecular biology  Researcher  2001 - 2003  99 
25.  05266  PhD Ana Marija Ritonja  Biochemistry and molecular biology  Researcher  2001 - 2003  108 
26.  16411  PhD Jerica Rozman Pungerčar  Biochemistry and molecular biology  Researcher  2001 - 2003  61 
27.  14315  PhD Ana Schweiger  Biochemistry and molecular biology  Researcher  2002 - 2003  62 
28.  17096  Andreja Sekirnik  Biochemistry and molecular biology  Researcher  2001 - 2003  31 
29.  14829  PhD Veronika Stoka  Biochemistry and molecular biology  Researcher  2001 - 2003  237 
30.  15969  Ivica Štefe  Biochemistry and molecular biology  Researcher  2001 - 2003  36 
31.  05234  Mojca Trstenjak Prebanda  Biochemistry and molecular biology  Researcher  2001 - 2003  64 
32.  07561  PhD Boris Turk  Biochemistry and molecular biology  Researcher  2001 - 2003  1,038 
33.  01085  PhD Vito Turk  Biochemistry and molecular biology  Head  2001 - 2003  1,492 
34.  21557  PhD Tjaša Urbič  Chemistry  Researcher  2001 - 2003 
35.  18286  PhD Tina Zavašnik Bergant  Biochemistry and molecular biology  Researcher  2001 - 2003  138 
36.  03368  PhD Eva Žerovnik  Biochemistry and molecular biology  Researcher  2001 - 2003  391 
Organisations (1)
no. Code Research organisation City Registration number No. of publicationsNo. of publications
1.  0106  Jožef Stefan Institute  Ljubljana  5051606000  91,961 
Abstract
Protein degradation or proteolysis occurs in living organisms under normal and pathological conditions. This process is highly controlled by proteolytic enzymes. Cysteine peptidases as one of the four mechanistic classes of proteolytic enzymes are widely distributed in animals, plants and microorganisms. Among many families of cysteine peptidases the largest and best-known being the papain family, which is the object of the proposed programme. Until recently, information about these enzymes of mammalian origin, mostly human, has been limited only to lysosomal cathepsins B, H, L and S. Using a new molecular biology approach, currently more than 15 human cathepsins are known at the sequence level. Some of them are expressed in a variety of cells (cathepsins B, C, F, H, L, O and X), whereas others are tissue-specific (cathepsins S, K, V and W) and are involved in more specialized processes like antigen processing and presentation, in bone remodeling, and processing in various hormones and other proteins. They differ in their specificities, acting as endopeptidases, aminopeptidases and carboxypeptidases. The activities of cathepsins, are regulated mainly by zymogen activation and proteinase-inhibitor interactions. The determined crystal structures provide the basis for the understanding of the activation of cysteine peptidases. Propeptides are potent inhibitors of their corresponding enzymes. However, the main regulation of mature enzymes remains to be the inhibition by their endogenous protein inhibitors, the cystatins, and newly discovered thyroglobulin type-1 domain inhibitors, also called thyropins.
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