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1

Computer modelling of human alpha 1-antitrypsin reactive site loop behaviour under mild conditions

100%
Koloczek H., Jezierski G., Pasenkiewicz-Gierula M.
Acta Biochimica Polonica
|
1996
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tom 43
|
nr 3
Human ai-antitrypsin (cti-PI) is a member of the serpin superfamily of proteins. The reactive site loop (RSL) of the serpin binds to the active site of its target proteinase. Deficiency of ai-antitrypsin is associated with a spontaneous conformational transition in the molecule which leads to a polymer formation. Mild conditions (1 M guanidinium-HCl), temperature and point mutations within the RSL are the factors that induce polymerisation. Initiation of this process has been associated with the disruption of a salt bridge Glu342-»Lys290. In this paper the interaction of guani- dinium ion with Glu342 and Lys290 as well as the effect of this interaction on the mobility of RSL is studied by molecular modelling.
2

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

86%
Kowalska A., Schwartzman A. L., Rujner J., Kraszewski A., Gaitkhoki V. S.
Bulletin of the Polish Academy of Sciences. Biological Sciences
|
1991
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tom 39
|
nr 3
3

Detection of inhibitory inactive fraction of alpha-1-antitrypsin in human serum

86%
Pajdak W., Pajdak E.
Folia Histochemica et Cytobiologica
|
1986
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tom 24
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nr 2
4

The effects of Fasciola hepatica infection on the total antioxidant status (TAS) and the activity of proteases and their inhibitors in rat serum

72%
Kolodziejczyk L., Jarocka I., Skrzydlewska E.
Folia Biologica
|
2013
|
tom 61
|
nr 3-4
5

Evidence for the presence of different alpha-1-proteinase inhibitor genes products in mouse plasma

72%
Dubin A., Mak P., Travis J.
Acta Biochimica Polonica
|
1996
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tom 43
|
nr 3
The plasma alpha-l-proteinase inhibitor (API) of three mouse species Mus domes- ticus, M. caroli and M. pahori was isolated. Each of the species isoforms were then separated by chromatofocusing; however, no significant differences in association rate constants toward human neutrophil elastase and bovine chymotrypsin were observed. The amino-acid sequence of the P'i-P'15 C-terminal fragments of the API variants indicate that mouse plasma contains at least two different active API isoforms in the case of M. domesticus (five API genes) but only one active API isoform in M. pahori and M. caroli (one API gene).
6

The effect of the Glu342Lys mutation in alpha1-antitrypsin on its structure, studied by molecular modelling medhods

72%
Jezierski G., Pasenkiewicz-Gierula M.
Acta Biochimica Polonica
|
2001
|
tom 48
|
nr 1
The structure of native α1-antitrypsin, the most abundant protease inhibitor in human plasma, is characterised primarily by a reactive loop containing the centre of proteinase inhibition, and aβ-sheet composed of five strands. Mobility of the reactive loop is confined as a result of electrostatic interactions between side chains of Glu342 and Lys290, both lo­cated at the junction of the reactive loop and the β structure. The most common mutation in the protein, resulting in its inactivation, is Glu342->Lys, named the Z mutation. The main goal of this work was to investigate the influence of the Z mutation on the structure of α1-antitrypsin. Commonly used molecular modelling methods have been ap­plied in a comparative study of two protein models: the wild type and the Z mutant. The results indicate that the Z mutation introduces local instabilities in the region of the reactive loop. Moreover, even parts of the protein located far apart from the mutation re­gion are affected. The Z mutation causes a relative change in the total energy of about 3%. Relatively small root mean square differences between the optimised structures of the wild type and the Z mutant, together with detailed analysis of 'conformational searching' process, lead to the hypothesis that the Z mutation principally induces a change in the dy­namics of α1-antitrypsin.
7

Alpha-1 antitrypsin: a potent anti-inflammatory and potential novel therapeutic agent

58%
Bergin D. A., Hurley K., McElvaney N. G., Reeves E. P.
Archivum Immunologiae et Therapiae Experimentalis
|
2012
|
tom 60
|
nr 2
8

Serum acute phase proteins in neuroblastoma children at diagnosis and during the clinical treatment. A preliminary report

58%
Lipinska L., Laskowska-KLita T., Izbicki T.
Folia Histochemica et Cytobiologica
|
1992
|
tom 30
|
nr 4
9

Molecular evolution and acute phase change of guinea pig contrapsin and alpha-1-antiproteinase

58%
Suzuki Y., Sinohara H.
Folia Histochemica et Cytobiologica
|
1992
|
tom 30
|
nr 4
10

Extrahepatic synthesis of acute phase proteins and their functions

51%
Aldred A. R., Southwell B., Schreiber G.
Folia Histochemica et Cytobiologica
|
1992
|
tom 30
|
nr 4
11

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

44%
Pilacik B., Kowalska A., Rujner J., Deron Z.
Bulletin of the Polish Academy of Sciences. Biological Sciences
|
1992
|
tom 40
|
nr 3
12

Zachowanie sie niektorych bialek ostrej fazy w surowicy chorych z rakiem pierwotnym watroby, w porownaniu z przypadkami nowotworu przerzutowego i marskosci pozapalnej

37%
Paszkiewicz J., Witczak K., Kiszkis H., Ciesielski D., Zoltowska A., Zielinska W.
Acta Biologica et Medica
|
1992
|
tom 18
117-127
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