Search Results - "Dolenc, Iztok"
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1
Glucosamine prevents polarization of cytotoxic granules in NK-92 cells by disturbing FOXO1/ERK/paxillin phosphorylation
Published in PloS one (17-07-2018)“…Glucosamine (GlcN) is a naturally occurring derivative of glucose and an over-the-counter food additive. However, the mechanism underlying GlcN action on cells…”
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2
Feedback Regulation of Cathepsin C by the Propeptide Dipeptides of Granzymes A and B
Published in Acta chimica Slovenica (01-06-2019)“…Granzymes A and B are activated by proteolytic removal of their N-terminal dipeptides by cathepsin C (dipeptidyl-peptidase I). However, the possible…”
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3
Expression, purification and auto-activation of cathepsin E from insect cells
Published in Protein and peptide letters (01-01-2015)“…Cathepsin E is an aspartic protease that belongs to the pepsin family. This protease is similar to cathepsin D but differs in its tissue distribution and cell…”
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4
Soft roll linings - better conduits: First press of the PS 2, paper machine, Belišće, Croatia
Published in Hemijska industrija (01-01-2005)“…Paper with demanding technical properties is formed in the press of the paper machine when the paper pulp is passed between the rolls. In order to form paper…”
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5
Oligomeric Structure and Substrate Induced Inhibition of Human Cathepsin C (∗)
Published in The Journal of biological chemistry (15-09-1995)“…Cathepsin C has been purified from human kidney by a modified procedure. Human cathepsin C was isolated as pure protein with a pI close to 6.0. The enzyme was…”
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6
Molecular cloning and sequence analysis of human preprocathepsin C
Published in FEBS letters (07-08-1995)“…A cDNA clone (C1) coding for human preprocathepsin C was isolated from a human ileum cDNA library using a rat kidney-derived RT-PCR probe and its complete…”
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7
Human cathepsin X/Z is a biologically active homodimer
Published in Biochimica et biophysica acta. Proteins and proteomics (01-02-2021)“…Human cathepsin X belongs to the cathepsin family of 11 lysosomal cysteine proteases. We expressed recombinant procathepsin X in Pichia pastoris in vitro and…”
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8
Tumor Necrosis Factor‐α Induced Apoptosis in U937 Cells Promotes Cathepsin D‐Independent Stefin B Degradation
Published in Journal of cellular biochemistry (01-12-2017)“…ABSTRACT Lysosomal cathepsins were previously found to be involved in tumor necrosis factor‐α (TNFα)‐induced apoptosis. However, there are opposing views…”
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9
Characteristics, Structure, and Biological Role of Stefins (type-1 cystatins) of Human, Mammal, and Parasite Origin
Published in Acta chimica Slovenica (01-02-2019)“…The majority of lysosomal cysteine cathepsins are ubiquitously expressed enzymes. However, some of them differ in their specific cell or tissue distribution…”
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10
Aspartic cathepsin D degrades the cytosolic cysteine cathepsin inhibitor stefin B in the cells
Published in Biochemical and biophysical research communications (18-09-2015)“…Stefin B is the major general cytosolic protein inhibitor of cysteine cathepsins. Its main function is to protect the organism against the activity of…”
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11
Menadione‐induced apoptosis in U937 cells involves Bid cleavage and stefin B degradation
Published in Journal of cellular biochemistry (01-06-2019)“…Earlier studies showed that the oxidant menadione (MD) induces apoptosis in certain cells and also has anticancer effects. Most of these studies emphasized the…”
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12
Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases
Published in FEBS letters (27-02-1995)“…For the first time, three different stefins, A, B and C, have been isolated from a single species. The complete amino acid sequence of bovine stefin A was…”
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13
Acidic pH as a physiological regulator of human cathepsin L activity
Published in European journal of biochemistry (01-02-1999)“…Human cysteine protease cathepsin L was inactivated at acid pH by a first‐order process. The inactivation rate decreased with increasing concentrations of a…”
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14
Characteristics, Structure, and Biological Role of Stefins (Type-1 Cystatins) of Human
Published in Acta chimica Slovenica (01-02-2019)“…The majority of lysosomal cysteine cathepsins are ubiquitously expressed enzymes. However, some of them differ in their specific cell or tissue distribution…”
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15
Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins
Published in Biological chemistry Hoppe-Seyler (01-04-1995)“…The kinetics of pH-induced inactivation of human cathepsins B and L was studied by conventional and stopped-flow methods. The inactivation of both enzymes was…”
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16
Cathepsin C and plasma glutamate carboxypeptidase secreted from Fischer rat thyroid cells liberate thyroxin from the N-terminus of thyroglobulin
Published in Biochimie (01-03-2012)“…The release of a thyroid hormone from thyroglobulin is controlled by a complex regulatory system. We focused on the extracellular action of two lysosomal…”
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17
Baculoviral expression and characterization of human recombinant PGCP in the form of an active mature dimer and an inactive precursor protein
Published in Protein expression and purification (01-02-2011)“…The human-blood plasma glutamate carboxypeptidase (PGCP) is a proteinase that acts on the unsubstituted N- and C-termini of dipeptides. It has been suggested…”
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18
N-terminally truncated forms of human cathepsin F accumulate in aggresome-like inclusions
Published in Biochimica et biophysica acta (01-10-2013)“…The contribution of individual cysteine cathepsins as positive mediators of programmed cell death is dependent on several factors, such as the type of stimuli,…”
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19
Presence of the propeptide on recombinant lysosomal dipeptidase controls both activation and dimerization
Published in Biological chemistry (01-01-2007)“…Lysosomal dipeptidase catalyzes the hydrolysis of dipeptides with unsubstituted terminals. It is a homodimer and binds zinc. Dimerization is an important issue…”
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20
Crystal Structure of Stefin A in Complex with Cathepsin H: N-terminal Residues of Inhibitors can Adapt to the Active Sites of Endo- and Exopeptidases
Published in Journal of molecular biology (21-02-2003)“…Binding of cystatin-type inhibitors to papain-like exopeptidases cannot be explained by the stefin B–papain complex. The crystal structure of human stefin A…”
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