Wyniki wyszukiwania

1

Target enzymes for plasma proteinase inhibitors

100%

Travis J.

Folia Histochemica et Cytobiologica

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1986

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tom 24

|

nr 2

2

An attempt to isolate High-molecular proteinase inhibitors from boar seminal plasma

100%

Torska J., Strzezek J.

Applied Biology Communications. Lublin Scientific Center

|

1992

|

tom 02

|

nr 6-7

3

Granulocyte proteinases as mediators of unspecific proteolysis in inflammation: a review

88%

Fritz H., Jochum M., Geiger R., Duswald K. H., Dittmer H., Kortmann S., Neumann S., Lang H.

Folia Histochemica et Cytobiologica

|

1986

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tom 24

|

nr 2

4

Two serine proteinase inhibitors from the larval hemolymph of Heliothis zea

88%

Polanowski A., Wilusz T., Blum M. S., Travis J.

Acta Biochimica Polonica

|

1994

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tom 41

|

nr 2

5

Alteration of hormone secretion by proteinase inhibitors

75%

Rappay G., Makara G. B., Nagy I.

Folia Histochemica et Cytobiologica

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1984

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tom 22

|

nr 3-4

6

Serine proteinase inhibitor family in squash seeds: mutational variability mechanism and correlation

75%

Leluk J.

Cellular and Molecular Biology Letters

|

2000

|

tom 05

|

nr 1

Proteinase inhibitors from squash seeds were analyzed for mutational variability. The non-homologous positions were subjected to an analysis of the interrelation between occurring residues and the mechanism of variability, using the algorithm of genetic semihomology [1]. The study also concerned mutational correlation at particular positions and their contact with each other. It was observed that: the number of residues occupying particular positions varies from 1 to 8 the mechanism of variability is based on single point mutation the variable positions are seldom in contact with each other the mutations in distant positions (not in contact with each other) are correlated with each other the correlated mutations refer to those positions which are far from the reactive site of the inhibitor the mutational variability in primary structure within this family is not consistent with the Markovian model of amino acid replacement.

7

Activity of proteinase inhibitors in seminal plasma of vasectomised boars

75%

Strzezek J., Torska J.

Animal Science Papers and Reports

|

2001

|

tom 19

|

nr 2

8

The intracellular serpin family

75%

Korpula-Mastalerz R., Dubin A.

Acta Biochimica Polonica

|

1996

|

tom 43

|

nr 3

The serpins are widely distributed, structurally related family of proteins with diverse functions. Most of the known serpins are proteinase inhibitors, the majority being found as secreted species, however, there are a few that occur intracellularly and their physiological role remains unknown. Most of the intracellularly occuring serpins have been classified into the ovalbumin subfamily. The possible phytogenetic tree of 14 intracellular serpins is presented.

9

The effect of grain aphid [Sitobion avenae F.] feeding on antitrypsin activity in ears of selected spring triticale cultivars

63%

Sprawka I., Ciepiela A. P., Kmoch E.

Pestycydy

|

2005

|

nr 3

189-193

10

Mechanism of the activation of proteinase inhibitors synthesis by systemic involves beta-sheet structure, a specific DNA binding protein domain

63%

Slosarek G., Kalbitzer H. R., Mucha P., Rekowski P., Kupryszewski G., Giel-Pietraszuk M., Szymanski M., Barciszewski J.

Biological Bulletin of Poznań. Supplement

|

1997

|

tom 34

11

Synthesis, cloning and expression in Escherichia coli of the gene coding for the trypsin inhibitor from Cucurbita pepo

63%

Rempola B., Wilusz T., Markiewicz W., Fikus M.

Acta Biochimica Polonica

|

1995

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tom 42

|

nr 1

A chemically synthesized gene coding for the serine proteinase inhibitor CPTI II was cloned in E. coli and its expression was investigated in cytoplasmic and secretion systems. Under all conditions investigated the biologically active form of the inhibitor was found only in the latter system, although the yield was rather low.

12

Molecular aspects of plant cell responses to wounding

63%

Davies E., Vian A., Vian C., Stankovic B.

Biological Bulletin of Poznań. Supplement

|

1997

|

tom 34

13

Jasmonate-signalling in stress-induced gene expression

63%

Wasternack C., Hause B., Kramell R., Miersch O., Atzorn R., Demus U., Feussner I., Parthier B.

Biological Bulletin of Poznań. Supplement

|

1997

|

tom 34

14

Effect of serine proteinase inhibitors on intracellular free calcium rise in human polymorphonuclear leukocytes after stimulation with receptor agonists

63%

Nowak D., Krol M., Bialasiewicz P.

Archivum Immunologiae et Therapiae Experimentalis

|

1998

|

tom 46

|

nr 2

15

Phage display of proteins

63%

Koscielska K., Kiczak L., Kasztura M., Wesolowska O., Otlewski J.

Acta Biochimica Polonica

|

1998

|

tom 45

|

nr 3

In recent years the phage display approach has become an increasingly popular method in protein research. This method enables the presentation of large peptide and protein libraries on the surface of phage particles from which molecules of desired functional property(ies) can be rapidly selected. The great advantage of this method is a direct linkage between an observed phenotype and encapsulated genotype, which allows fast determination of selected sequences. The phage display approach is a powerful tool in generating highly potent biomolecules, including: search for specific antibodies, determining enzyme specificity, exploring protein-protein and protein-DNA interactions, minimizing proteins, introducing new functions into different protein scaffolds, and searching sequence space of protein folding. In this article many examples are given to illustrate that this technique can be used in different fields of protein science. The phage display has a potential of the natural evolution and its possibilities are far beyond rational prediction. Assuming that we can design the selection agents and conditions we should be able to engineer any desired protein function or feature.

16

Engineered resistance against proteinases

51%

Milner M., Chroboczek J., Zagorski-Ostoja W.

Acta Biochimica Polonica

|

2007

|

tom 54

|

nr 3

Exogenous proteinase inhibitors are valuable and economically interesting protective biotechnological tools. We examined whether small proteinase inhibitors when fused to a selected target protein can protect the target from proteolytic degradation without simultaneously affecting the function and activity of the target domain. Two proteinase inhibitors were studied: a Kazal-type silk proteinase inhibitor (SPI2) from Galleria mellonella, and the Cucurbita maxima trypsin inhibitor I (CMTI I). Both inhibitors target serine proteinases, are small proteins with a compact structure stabilized by a network of disulfide bridges, and are expressed as free polypeptides in their natural surroundings. Four constructs were prepared: the gene for either of the inhibitors was ligated to the 5' end of the DNA encoding one or the other of two selected target proteins, the coat protein (CP) of Potato potyvirus Y or the Escherichia coli β-glucuronidase (GUS). CMTI I fused to the target proteins strongly hampered their functions. Moreover, the inhibitory activity of CMTI I was retained only when it was fused to the CP. In contrast, when fused to SPI2, specific features and functions of both target proteins were retained and the inhibitory activity of SPI2 was fully preserved. Measuring proteolysis in the presence or absence of either inhibitor, we demonstrated that proteinase inhibitors can protect target proteins used either free or as a fusion domain. Interestingly, their inhibitory efficiency was superior to that of a commercial inhibitor of serine proteinases, AEBSF.

17

Molecules released by helminth parasites involved in host colonization

51%

Dzik J. M.

Acta Biochimica Polonica

|

2006

|

tom 53

|

nr 1

Parasites are designed by evolution to invade the host and survive in its organism until they are ready to reproduce. Parasites release a variety of molecules that help them to penetrate the defensive barriers and avoid the immune attack of the host. In this respect, particularly interesting are enzymes and their inhibitors secreted by the parasites. Serine-, aspartic-, cysteine-, and metalloproteinases are involved in tissue invasion and extracellular protein digestion. Helminths secrete inhibitors of these enzymes (serpins, aspins, and cystatins) to inhibit proteinases, both of the host and their own. Proteinases and their inhibitors, as well as helminth homologues of cytokines and molecules containing phosphorylcholine, influence the immune response of the host biasing it towards the anti-inflammatory Th2 type. Nucleotide-metabolizing enzymes and cholinesterase are secreted by worms to reduce inflammation and expel the parasites from the gastrointestinal tract. An intracellular metazoan parasite, Trichinella spiralis, secretes, among others, protein kinases and phosphatases, endonucleases, and DNA-binding proteins, which are all thought to interfere with the host cellular signals for muscle cell differentiation. Secretion of antioxidant enzymes is believed to protect the parasite from reactive oxygen species which arise from the infection-stimulated host phagocytes. Aside from superoxide dismutase, catalase (rarely found in helminths), and glutathione peroxidase (selenium-independent, thus having a poor activity with H2O2), peroxiredoxins are probably the major H2O2-detoxifying enzymes in helminths. Secretion of antioxidant enzymes is stage-specific and there are examples of regulation of their expression by the concentration of reactive oxygen species surrounding the parasite. The majority of parasite-secreted molecules are commonly found in free-living organisms, thus parasites have only adapted them to use in their way of life.

18

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Zbozowe, bialkowe inhibitory enzymow hydrolitycznych i ich znaczenie. Czesc II: Bialkowe inhibitory proteinaz

45%

Piasecka-Kwiatkowska D., Warchalewski J. R.

Żywność Nauka Technologia Jakość

|

2000

|

tom 07

|

nr 3

33-38

W pracy przedstawiono przegląd danych literaturowych na temat zbożowych, białkowych inhibitorów enzymów proteolitycznych. Szczególną uwagę zwrócono na ich właściwości, formy wielorakie, a także ich znaczenie biochemiczne, fizjologiczne i żywieniowe.

19

Extrahepatic synthesis of acute phase proteins and their functions

45%

Aldred A. R., Southwell B., Schreiber G.

Folia Histochemica et Cytobiologica

|

1992

|

tom 30

|

nr 4

Ograniczanie wyników

Target enzymes for plasma proteinase inhibitors

An attempt to isolate High-molecular proteinase inhibitors from boar seminal plasma

Granulocyte proteinases as mediators of unspecific proteolysis in inflammation: a review

Two serine proteinase inhibitors from the larval hemolymph of Heliothis zea

Alteration of hormone secretion by proteinase inhibitors

Serine proteinase inhibitor family in squash seeds: mutational variability mechanism and correlation

Activity of proteinase inhibitors in seminal plasma of vasectomised boars

The intracellular serpin family

The effect of grain aphid [Sitobion avenae F.] feeding on antitrypsin activity in ears of selected spring triticale cultivars

Mechanism of the activation of proteinase inhibitors synthesis by systemic involves beta-sheet structure, a specific DNA binding protein domain

Synthesis, cloning and expression in Escherichia coli of the gene coding for the trypsin inhibitor from Cucurbita pepo

Molecular aspects of plant cell responses to wounding

Jasmonate-signalling in stress-induced gene expression

Effect of serine proteinase inhibitors on intracellular free calcium rise in human polymorphonuclear leukocytes after stimulation with receptor agonists

Phage display of proteins

Engineered resistance against proteinases

Molecules released by helminth parasites involved in host colonization

Zbozowe, bialkowe inhibitory enzymow hydrolitycznych i ich znaczenie. Czesc II: Bialkowe inhibitory proteinaz

Extrahepatic synthesis of acute phase proteins and their functions