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Your search keyword '"Karolina Rucinska"' showing total 9 results
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9 results on '"Karolina Rucinska"'

2. PLASMA STEROID PROFILE IN WOMEN WITH FIBROMUSCULAR DYSPLASIA - THE ARCADIA-GYN STUDY

Author

Anna Aniszczuk-Hybiak, Elzbieta Florczak, Piotr Dobrowolski, Justyna Teliga-Czajkowska, Aleksander Prejbisz, Agnieszka Dobrowolska-Redo, Joanna Was, Karolina Rucinska, Anna Lutynska, Przemyslaw Kosinski, Laretta Grabowska-Derlatka, Magdalena Januszewicz, Marco Papaccoggli, Alexandre Persu, and Andrzej Januszewicz

Subjects
Physiology, Internal Medicine, Cardiology and Cardiovascular Medicine
Published
2022

5. Physical Characterization of Silver Nanoparticles for Nanodetection

Author

Joanna P. Patalas, Augustyn Molinski, Maciej Kozak, Michał Taube, Żaneta Polańska, Karolina Rucinska, Zuzanna Pietralik, Barbara Peplińska, Agnieszka Boś-Liedke, and Agata Szymbor

Subjects
Materials science, Biophysics, Nanotechnology, Silver nanoparticle, Characterization (materials science)
Published
2020

9. Oligomerization of Human Cystatin C—An Amyloidogenic Protein: An Analysis of Small Oligomeric Subspecies

Author

Daria Wojciechowska, Michał Taube, Karolina Rucińska, Joanna Maksim, and Maciej Kozak

Subjects
human cystatin C, oligomer, amyloid, small-angle X-ray scattering, dynamic light scattering, Biology (General), QH301-705.5, Chemistry, QD1-999
Abstract

Human cystatin C (HCC), an amyloidogenic protein, forms dimers and higher oligomers (trimers, tetramers and donut like large oligomers) via a domain-swapping mechanism. The aim of this study was the characterization of the HCC oligomeric states observed within the pH range from 2.2 to 10.0 and also in conditions promoting oligomerization. The HCC oligomeric forms obtained in different conditions were characterized using size exclusion chromatography, dynamic light scattering and small-angle X-ray scattering. The marked ability of HCC to form tetramers at low pH (2.3 or 3.0) and dimers at pH 4.0–5.0 was observed. HCC remains monomeric at pH levels above 6.0. Based on the SAXS data, the structure of the HCC tetramer was proposed. Changes in the environment (from acid to neutral) induced a breakdown of the HCC tetramers to dimers. The tetrameric forms of human cystatin C are formed by the association of the dimers without a domain-swapping mechanism. These observations were confirmed by their dissociation to dimers at pH 7.4.

Published
2022
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