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Wyszukujesz frazę "Kaczmarek, Radosław" wg kryterium: Autor


Wyświetlanie 1-3 z 3
Tytuł:
Shall intraoperative OCT become standard equipment of modern operating room?
Autorzy:
Kaczmarek, Dorota Maria
Kaczmarek, Radosław
Powiązania:
https://bibliotekanauki.pl/articles/23202392.pdf
Data publikacji:
2023-09-30
Wydawca:
Medical Education
Tematy:
intraoperative OCT
retinal surgery
corneal surgery
vitrectomy
keratoplasty
Opis:
The role of intraoperative OCT (iOCT) in ophthalmic surgery is still a matter of active research and enhancements to integrative technologies. Further research is necessary to better define the specific applications of iOCT that impact surgical decision-making and as such help to achieve better patient outcomes, both in anterior and in posterior segment of the eye. In time to come advancements in integrative systems, OCT-friendly instrumentation, and software algorithms will most likely expand the horizon of iOCT even further.
Źródło:
OphthaTherapy; 2023, 10, 3; 173-177
2353-7175
2543-9987
Pojawia się w:
OphthaTherapy
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Characteristic of monotonicity of Orlicz function spaces equipped with the Orlicz norm
Autorzy:
Foralewski, Paweł
Hudzik, Henryk
Kaczmarek, Radosław
Krbec, Miroslav
Powiązania:
https://bibliotekanauki.pl/articles/746439.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Matematyczne
Tematy:
Orlicz space
Orlicz norm
Kothe space
Kothe dual
characteristic of monotonicity
strict monotonicity
point of order smoothness
Opis:
We first prove that the property of strict monotonicity of a~K\"othe space \((E,\|.\|_E)\) and\slash or of its K\"othe dual \((E',\|.\|_{E'})\) can be used successfully to compare the supports of \(x\in E\backslash\{\theta\}\) and \(y\in S(E')\), where \(=\|x\|_E\). Next we prove that any element \(x\in S_{+}(E)\) with \(\mu(T\backslash\operatorname{supp} x)=0\) is a~point of order smoothness in \(E\), whenever \(E\) is an order continuous K\"othe space. Finally, we present formulas for the characteristic of monotonicity of Orlicz function spaces endowed with the Orlicz norm in the case when the generating Orlicz function does not satisfy suitable \(\Delta_2\)-condition or the measure is non-atomic infinite, and some lower and upper estimates for the characteristic of monotonicity of this spaces when the measure is non-atomic and finite.
Źródło:
Commentationes Mathematicae; 2013, 53, 2
0373-8299
Pojawia się w:
Commentationes Mathematicae
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Bacterially expressed truncated F2 domain of Plasmodium falciparum EBA-140 antigen can bind to human erythrocytes
Autorzy:
Rydzak, Joanna
Kryńska, Katarzyna
Suchanowska, Anna
Kaczmarek, Radosław
Łukasiewicz, Jolanta
Czerwiński, Marcin
Jaśkiewicz, Ewa
Powiązania:
https://bibliotekanauki.pl/articles/1039687.pdf
Data publikacji:
2012
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
truncated F2 domain purification
human erythrocyte binding
EBA-140 antigen
Plasmodium falciparum
recombinant F2 domain expression
Opis:
The recently identified erythrocyte binding antigen-140 (EBA-140) is a member of the Plasmodium falciparum DBL family of erythrocyte binding proteins, which are considered as prospective candidates for malaria vaccine development. The EBA-140 ligand is a paralogue of the well-characterized P. falciparum EBA-175 antigen. They share homology of domain structure, including Region II, which consists of two homologous F1 and F2 domains and is responsible for ligand-erythrocyte interaction during invasion. It was shown that the F2 domain of EBA-175 antigen seems to be more important for erythrocyte binding. In order to study activity and immunogenicity of EBA-140 antigen F2 domain, it is necessary to obtain recombinant protein of high purity and in a sufficient amount, which used to pose a challenge due to the high content of disulphide bridges. Here, we present a new method for expression and purification of Plasmodium falciparum EBA-140 antigen F2 domain in E. coli Rosetta-gami strain in fusion with the maltose binding protein (MBP). The truncated F2 domain formed by spontaneous proteolytic degradation of the fusion protein was purified by affinity chromatography on Ni-NTA resin followed by size exclusion chromatography. Molecular mass of this protein was confirmed by mass spectrometry. Its N-terminal amino acid sequencing revealed a proteolytic cleavage site within the F2 domain. The proper folding of the recombinant, truncated F2 domain of EBA-140 antigen was confirmed by circular dichroism analysis. The truncated F2 domain can specifically bind to human erythrocytes but its binding is not as efficient as that of full Region II. This confirms that both the F1 and F2 domains of EBA-140 antigen are required for effective erythrocyte binding.
Źródło:
Acta Biochimica Polonica; 2012, 59, 4; 685-691
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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