Wyniki wyszukiwania

1

In vitro amplification of the alpha-1-antitrypsin gene for detection of Z mutation

100%

Kowalska A., Schwartzman A. L., Rujner J., Kraszewski A., Gaitkhoki V. S.

Bulletin of the Polish Academy of Sciences. Biological Sciences

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1991

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tom 39

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nr 3

2

Genetic polymorphism of alpha-1-antitrypsin (Locus Pi) in Polish population determined by isoelectric focusing. I. Studies of Poznan and its region

100%

Kowalska A., Titenko N., Rujner J.

Bulletin of the Polish Academy of Sciences. Biological Sciences

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1991

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tom 39

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nr 3

3

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New proteases of the chloroplast envelope – what do they do there?

84%

Adam Z.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2013

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tom 94

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nr 3

4

Extrachromosomal expression of nat05 gene encoding an alkaline serine protease from Bacillus subtilis N05

84%

Thu N. T. A., Chau N. T. T., Thien L. V., Huy N. D., Khue N. T. M., Hung N. B., Luong N. N., Thu L. T. A., Loc N. H.

BioTechnologia. Journal of Biotechnology Computational Biology and Bionanotechnology

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2018

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tom 99

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nr 4

5

Gullo’s syndrome – case report

84%

Rycyk A., Furtak P., Madro A., Kasztelan-Szczerbinska B., Cichoz-Lach H.

Journal of Pre-Clinical and Clinical Research

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2020

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tom 14

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nr 4

6

Activity-based protein profiling of serine proteases in immune cells

84%

Kahler J. P., Vanhoutte R., Verhelst S. H. L.

Archivum Immunologiae et Therapiae Experimentalis

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2020

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tom 68

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nr 4

7

Structure-function relationship of serine protease-protein inhibitor interaction

84%

Otlewski J., Jaskolski M., Buczek O., Cierpicki T., Czapinska H., Krowarsch D., Smalas A. O., Stachowiak D., Szpineta A., Dadlez M.

Acta Biochimica Polonica

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2001

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tom 48

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nr 2

We re port our prog ress in un der stand ing the struc ture-function re la tion ship of the interaction between protein inhibitors and several serine proteases. Recently, we have de ter mined high res o lu tion so lu tion struc tures of two in hib i tors Apis mellifera chymotrypsin in hib i tor-1 (AMCI-I) and Linum usitatissimumtrypsin in hib i tor (LUTI) in the free state and an ul tra high res o lu tion X-ray struc ture of BPTI. All three in hib i tors, de spite to tally dif fer ent scaf folds, con tain a sol vent ex posed loop of sim i lar con- for ma tion which is highly com ple men tary to the en zyme ac tive site. Iso ther mal calorim e try data show that the in ter ac tion be tween wild type BPTI and chymotrypsin is entropy driven and that the enthalpy com po nent op poses com plex for ma tion. Our research is fo cused on ex ten sive mu ta gen e sis of the four po si tions from the pro te ase bind ing loop of BPTI: P1, P1', P3, and P4. We mu tated these res i dues to dif fer ent amino ac ids and the vari ants were char ac ter ized by de ter mi na tion of the as so ci a tion con stants, sta bil ity pa ram e ters and crys tal struc tures of pro te ase–in hib i tor complexes. Ac com mo da tion of the P1 res i due in the S1 pocket of four pro teas es: chymotrypsin, trypsin, neutrophil elastase and cathepsin G was probed with 18 P1 vari ants. High res o lu tion X-ray struc tures of ten com plexes be tween bo vine trypsin and P1 vari ants of BPTI have been de ter mined and com pared with the cog nate P1 Lysside chain. Mu ta tions of the wild type Ala16 (P1') to larger side chains al ways caused a drop of the as so ci a tion con stant. Ac cord ing to the crys tal struc ture of the Leu16 BPTI–trypsin com plex, in tro duc tion of the larger res i due at the P1' po si tion leads to steric con flicts in the vi cin ity of the mu ta tion. Finally, mu ta tions at the P4 site al lowed an im prove ment of the as so ci a tion with sev eral serine pro teas es in volved in blood clot ting. Con versely, in tro duc tion of Ser, Val, and Phe in place of Gly12 (P4) had invariably a destabilizing ef fect on the com plex with these pro teas es.

8

Glutathione transferases and serine proteases: from probing mechanism of enzyme catalysis by rational protein engineering to evolutionary design of enzyme function

84%

Sroga G. E.

Biotechnologia

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2002

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nr 3

9

Structural and functional diversities in lepidopteran serine proteases

84%

Srinivasan A., Giri A. P., Gupta V. S.

Cellular and Molecular Biology Letters

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2006

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tom 11

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nr 1

Primary protein-digestion in Lepidopteran larvae relies on serine proteases like trypsin and chymotrypsin. Efforts toward the classification and characterization of digestive proteases have unraveled a considerable diversity in the specificity and mechanistic classes of gut proteases. Though the evolutionary significance of mutations that lead to structural diversity in serine proteases has been well characterized, detailing the resultant functional diversity has continually posed a challenge to researchers. Functional diversity can be correlated to the adaptation of insects to various host-plants as well as to exposure of insects to naturally occurring antagonistic biomolecules such as plant-derived protease inhibitors (PIs) and lectins. Current research is focused on deciphering the changes in protease specificities and activities arising from altered amino acids at the active site, specificity-determining pockets and other regions, which influence activity. Some insight has been gained through in silico modeling and simulation experiments, aided by the limited availability of characterized proteases. We examine the structurally and functionally diverse Lepidopteran serine proteases, and assess their influence on larval digestive processes and on overall insect physiology.

10

3'Noncoding sequences of the CTA 1 gene enhance expression of the recombinant serine protease inhibitor, CPTI II, in Saccharomyces cerevisiae

84%

Stankiewicz M., Rempola B., Fikus M.

Acta Biochimica Polonica

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1996

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tom 43

|

nr 3

Expression of the gene coding for the recombinant trypsin inhibitor, CPTI II, was enhanced tenfold when yeast transcription terminating sequences were added to the expression cassette of the pJK6 yeast vector. The yield was further increased about 20% in the BJ5464 yeast strain, defective in vacuolar proteases.

11

Tissue plasminogen activator in the amygdala: a new role for an old protease

67%

Skrzypiec A. E., Buczko W., Pawlak R.

Journal of Physiology and Pharmacology. Supplement

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2008

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tom 59

|

nr 8

12

Purification and characterization of an extracellular protease from Bacillus subtilis EAG-2 strain isolated from ornamental plant nursery

67%

Ghafoor A., Hasnain S.

Polish Journal of Microbiology

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2010

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tom 59

|

nr 2

107-112

Bacillus subtilis EAG-2 strain isolated from an ornamental plant nursery produced a highly active extracellular protease. It was purified to apparent homogeneity by successive purification steps. The SDS-gel of purified protease revealed a single band of 27 KDa on 10% polyacrylamide gel. Proteolytic activity was confirmed by using two different zymographic methods. Interestingly, the enzyme showed two clear activity bands in both cases. The optimum proteolysis for this protease was observed at pH 8.5 and 65°C. The enzyme was highly stable up to 80% after 30-50°C for 60 minutes. It also remained stable at pH 6.5-9.0 after 4 hours of incubation at 37°C. Its activity was reduced to 16% and 25% by PMSF and APMSF which indicates its relation to serine proteases. An increase in activity was noticed in the presence of Ca⁺², Zn⁺² and Ba⁺². On the other hand, it worked effectively with different natural substrates. Hence EAG-2 protease might be a useful contribution to the enzyme industry in Pakistan based upon its distinctive properties.

13

The preparation of specific sorbents with polyclonal antibodies as a ligand for purification of human antithrombin III

67%

Rogalski J., Dawidowicz A. L., Wiater A., Gibula K., Winiarczyk S.

Acta Microbiologica Polonica

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1998

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tom 47

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nr 2

14

Changes in expression of serine proteases HtrA1 and HtrA2 during estrogen-induced oxidative stress and nephrocarcinogenesis in male Syrian hamster

67%

Zurawa-Janicka D., Kobiela J., Stefaniak T., Wozniak A., Narkiewicz J., Wozniak M., Limon J., Lipinska B.

Acta Biochimica Polonica

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2008

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tom 55

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nr 1

Serine proteases HtrA1 and HtrA2 are involved in cellular stress response and development of several diseases, including cancer. Our aim was to examine the involvement of the HtrA proteins in acute oxidative stress response induced in hamster kidney by estrogen treatment, and in nephrocarcinogenesis caused by prolonged estrogenization of male Syrian hamster. We used semi-quantitative RT-PCR to estimate the HtrA1 and HtrA2 mRNA levels in kidney tissues, and Western blotting to monitor the amount of the HtrA proteins. Within the first five hours following estrogen administration both HtrA1 mRNA and the protein levels were increased significantly. No changes in the expression of HtrA2 were observed. This indicates that HtrA1 may be involved in the response against oxidative stress induced by estrogen treatment in hamster kidney. During prolonged estrogenization, a significant reduction of the HtrA1 mRNA and protein levels was observed after 6 months of estradiol treatment, while the expression of HtrA2 was significantly elevated starting from the third month. This suggests an involvement of the HtrA proteins in estrogen-induced nephrocarcinogenesis in hamster. Using fluorescence in situ hybridization we localized the HtrA1 gene at the qb3-4 region of Syrian hamster chromosome 2, the region known to undergo a nonrandom deletion upon prolonged estrogenization. It is possible that the reduced level of HtrA1 expression is due to this chromosomal aberration. A full-length cDNA sequence of the hamster HtrA1 gene was obtained. It codes for a 50 kDa protein which has 98 and 96% identity with mouse and human counterparts, respectively.

15

A new alpha-1-antitrypsin phenotype [PiZ Lodz] in Polish population with reduced level in serum

51%

Pilacik B., Kowalska A., Rujner J., Deron Z.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

1992

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tom 40

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nr 3

Ograniczanie wyników

In vitro amplification of the alpha-1-antitrypsin gene for detection of Z mutation

Genetic polymorphism of alpha-1-antitrypsin (Locus Pi) in Polish population determined by isoelectric focusing. I. Studies of Poznan and its region

New proteases of the chloroplast envelope – what do they do there?

Extrachromosomal expression of nat05 gene encoding an alkaline serine protease from Bacillus subtilis N05

Gullo’s syndrome – case report

Activity-based protein profiling of serine proteases in immune cells

Structure-function relationship of serine protease-protein inhibitor interaction

Glutathione transferases and serine proteases: from probing mechanism of enzyme catalysis by rational protein engineering to evolutionary design of enzyme function

Structural and functional diversities in lepidopteran serine proteases

3'Noncoding sequences of the CTA 1 gene enhance expression of the recombinant serine protease inhibitor, CPTI II, in Saccharomyces cerevisiae

Tissue plasminogen activator in the amygdala: a new role for an old protease

Purification and characterization of an extracellular protease from Bacillus subtilis EAG-2 strain isolated from ornamental plant nursery

The preparation of specific sorbents with polyclonal antibodies as a ligand for purification of human antithrombin III

Changes in expression of serine proteases HtrA1 and HtrA2 during estrogen-induced oxidative stress and nephrocarcinogenesis in male Syrian hamster

A new alpha-1-antitrypsin phenotype [PiZ Lodz] in Polish population with reduced level in serum