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1

Cystatins of human placenta

100%
Warwas M., Sawicki G.
Acta Biochimica Polonica
|
1989
|
tom 36
|
nr 1
2

Evaluation of the antibacterial activity of cystatin against selected strains of Escherichia coli

75%
Szpak M., Trziszka T., Polanowski A., Grubek J., Golab K., Juszczynska K., Janik P., Malicki A., Szyplik K.
Folia Biologica
|
2014
|
tom 62
|
nr 3
3

Susceptibility of yeasts isolated from dairy products to cystatin

75%
Chrzanowska J., Krajewska E., Saleh J., Szoltysik M., Trziszka T.
Polish Journal of Natural Sciences. Supplement
|
2004
|
tom 02
23-29
4

Cathepsin H from human placenta

75%
Sawicki G., Warwas M.
Acta Biochimica Polonica
|
1989
|
tom 36
|
nr 3-4
5

Ovocystatin affects actin cytoskeleton organization and induces proapoptotic activity

75%
Malicka-Blaszkiewicz M., Filipczak N., Golab K., Juszczynska K., Sebzda T., Gburek J.
Acta Biochimica Polonica
|
2014
|
tom 61
|
nr 4
6

Structural studies of cysteine proteases and their inhibitors

75%
Grzonka Z., Jankowska E., Kasprzykowski F., Kasprzykowska R., Lankiewicz L., Wiczk W., Wieczerzak E., Ciarkowski J., Drabik P., Janowski R., Kozak M., Jaskolski M., Grubb A.
Acta Biochimica Polonica
|
2001
|
tom 48
|
nr 1
Cysteine proteases (CPs) are responsible for many biochemical processes occurring in living organisms and they have been implicated in the development and progression of several diseases that involve abnormal protein turnover. The activity of CPs is regulated among others by their specific inhibitors: cystatins. The main aim of this review is to dis­cuss the structure-activity relationships of cysteine proteases and cystatins, as well as of some synthetic inhibitors of cysteine proteases structurally based on the binding frag­ments of cystatins.
7

The activities and subcellular localization of cathepsin B and cysteine proteinase inhibitors in human ovarian carcinoma

75%
Haczynska H., Gerber J., Osada J., Warwas M.
Acta Biochimica Polonica
|
1997
|
tom 44
|
nr 1
Ovarian carcinomas exhibited a higher cathepsin B activity than did normal ovaries. The plasma membrane fractions of ovarian cancers were enriched in the activities of both cathepsin and cysteine proteinase inhibitors. The ratio of cathepsin to the inhibitors in these fractions was higher at stage IV than at stage III of the disease, classified according to the Federation of International Gynecology and Obstetrics.
8

Purification and characterization of cystatin from duck egg white

75%
Warwas M., Gburek J., Osada J., Golab K.
Acta Biochimica Polonica
|
1995
|
tom 42
|
nr 3
It is the second peptidase inhibitor, after ovostatin, which showing the same antipapain activity in egg white in different avian species implies differences in amino -acid sequences. Cystatin from duck egg white was purified by carboxymethylpapain affinity chromatography and size-exclusion HPLC. The purified inhibitor which showed partial identity in the immunodiffusion test with chicken egg white cystatin, had an apparent molecular mass of 9.3 kDa as determined by SDS/PAGE. IEF analysis revealed five molecular forms of pi in the range 7.8-S.4. The obtained cystatin was neither glycosylated nor phosphorylated as it is in the case of chicken cystatin. The determined Ki (0.005 ± 0.001 nM) was similar to that reported for human and chicken cystatin C.
9

Modes of inhibition of cysteine proteases

75%
Rzychon M., Chmiel D., Stec-Niemczyk J.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 4
Cysteine proteases are involved in many physiological processes and their hyperac­tivity may lead to severe diseases. Nature has developed various strategies to protect cells and whole organisms against undesired proteolysis. One of them is the control of proteolytic activity by inhibition. This paper presents the mechanisms underlying the action of proteinaceous inhibitors of cysteine proteinases and covers propeptides binding backwards relative to the substrate or distorting the protease catalytic cen­tre similarly to serpins, the p35 protein binding covalently to the enzyme, and cystatins that are exosite binding inhibitors. The paper also discusses tyropins and chagasins that, although unrelated to cystatins, inhibit cysteine proteinases by a sim­ilar mechanism, as well as inhibitors of the apoptosis protein family that bind in a di­rection opposite to that of the substrate, similarly to profragments. Special attention is given to staphostatins, a novel family of inhibitors acting in an unusual manner.
10

Surface plasmon resonance imaging biosensor for cystatin determination based on the application of bromelain, ficin and chymopapain

63%
Gorodkiewicz E., Breczko J., Sankiewicz A.
Folia Histochemica et Cytobiologica
|
2012
|
tom 50
|
nr 1
11
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

Contribution of phytocystatins to the processes of seed development and germination

63%
Siminska J., Sitnicka D., Bielawski W.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
|
2013
|
tom 94
|
nr 3
12

Inhibition of cysteine peptidase activity in ascitic fluid in pancreatic cancer patients

51%
Agrawal A., Kielan W., Katib A., Grzebieniak Z., Skalski A., Grzebieniak T., Duda-Barcik L., Janocha A., Siewinski M.
Folia Histochemica et Cytobiologica
|
2010
|
tom 48
|
nr 4
13

Izolacja cystatyny z bialka jaja z zastosowaniem filtracji membranowej i chromatografii powinowactwa

51%
Korzeniowska M., Kopec W.
Żywność Nauka Technologia Jakość. Suplement
|
2000
|
tom 07
|
nr 3
88-95
Podobieństwa budowy i właściwości biologicznych cystatyny białka jaja kurzego do ludzkiej cystatyny c stwarzają możliwość jej wykorzystania w prewencji i leczeniu wielu chorób. Dlatego celem badań było opracowanie podstaw procesów izolacji i oczyszczania cystatyny białka jaja przy użyciu techniki filtracji membranowej i chromatografii powinowactwa. W wyniku diaflltracji odzyskiwano z białka jaja lub jego roztworów, po usunięciu z nich lizozymu, 40-65% aktywnego inhibitora. Wykazano, że usunięcie lizozymu z roztworu białka nie wpływa na ilość odzyskanej cystatyny w filtratach. Natomiast w procesach oczyszczania cystatyny metodą chromatografii powinowactwa odzyskiwano do 50% inhibitora zawartego w preparatach uzyskanych po suszeniu rozpyłowym roztworów białek; ilości te były niższe o 3-4% jeśli oczyszczano preparaty białka z którego usunięto lizozym.
14
Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik
Content available

3D domain swapping – implications for conformational disorders and ways of control

51%
Jaskolski M.
BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology
|
2011
|
tom 92
|
nr 1
15

Eggs as a main source of new generation of nutraceuticals

51%
Trziszka T.
Polish Journal of Food and Nutrition Sciences
|
2011
|
tom 61
|
nr Suppl.1
16

Control of active B and L cathepsins in tissues of colorectal cancer using cystatins isolated from chicken egg proteins: in vitro studies

51%
Hap A., Kielan W., Grzebieniak Z., Siewinski M., Rudnicki J., Tarnawa R., Rudno-Rudzinska J., Agrawal A. K.
Folia Histochemica et Cytobiologica
|
2011
|
tom 49
|
nr 4
17

Fluorogenic peptide substrates for carboxydipeptidase activity of cathepsin B

51%
Stachowiak K., Tokmina M., Karpinska A., Sosnowska R., Wiczk W.
Acta Biochimica Polonica
|
2004
|
tom 51
|
nr 1
Cathepsin B is a lysosomal cysteine protease exhibiting mainly dipeptidyl carboxypeptidase activity, which decreases dramatically above pH 5.5, when the en­zyme starts acting as an endopeptidase. Since the common cathepsin B assays are performed at pH 6 and do not distinguish between these activities, we synthesized a series of peptide substrates specifically designed for the carboxydipeptidase activity of cathepsin B. The amino-acid sequences of the P5-P1 part of these substrates were based on the binding fragments of cystatin C and cystatin SA, the natural reversible inhibitors of papain-like cysteine protease. The sequences of the P'1-P'2 dipeptide fragments of the substrates were chosen on the basis of the specificity of the S'1-S'2 sites of the cathepsin B catalytic cleft. The rates of hydrolysis by cathepsin B and papain, the archetypal cysteine protease, were monitored by a continuous fluores­cence assay based on internal resonance energy transfer from an Edans to a Dabcyl group. The fluorescence energy donor and acceptor were attached to the C- and the N-terminal amino-acid residues, respectively. The kinetics of hydrolysis followed the Michaelis-Menten model. Out of all the examined peptides Dabcyl-R-L-V-G-FE(Edans) turned out to be a very good substrate for both papain and cathepsin B at both pH 6 and pH 5. The replacement of Glu by Asp turned this peptide into an exclusive substrate for cathepsin B not hydrolyzed by papain. The substitution of Phe by Nal in the original substrate caused an increase of the specificity constant for cathepsin B at pH 5, and a significant decrease at pH 6. The results of kinetic studies also suggest that Arg in position P4 is not important for the exopeptidase activity of cathepsin B, and that introducing Glu in place of Val in position P2 causes an increase of the substrate preference towards this activity.
18

Cysteine peptidases and their inhibitors in breast and genital cancer

45%
Agrawal A. K., Ekonjo G. B., Teterycz E., Zysko D., Grzebieniak Z., Milan M., Marek G., Siewinski M.
Folia Histochemica et Cytobiologica
|
2010
|
tom 48
|
nr 3
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