Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Artur Pirog"'
Autor:
Michal Bista, David Smithson, Aleksandra Pecak, Gabriella Salinas, Katarzyna Pustelny, Jaeki Min, Artur Pirog, Kristin Finch, Michal Zdzalik, Brett Waddell, Benedykt Wladyka, Sylwia Kedracka-Krok, Michael A Dyer, Grzegorz Dubin, R Kiplin Guy
Publikováno v:
PLoS ONE, Vol 7, Iss 6, p e37518 (2012)
SJ-172550 (1) was previously discovered in a biochemical high throughput screen for inhibitors of the interaction of MDMX and p53 and characterized as a reversible inhibitor (J. Biol. Chem. 2010; 285:10786). Further study of the biochemical mode of a
Externí odkaz:
https://doaj.org/article/50c3d2a731444c08bd0b42fc618a17eb
Autor:
Natalia Marek-Trzonkowska, David R. Goodlett, Jakub Faktor, Ryszard T. Smolenski, Borek Vojtesek, Zuzanna Urban-Wójciuk, Ted R. Hupp, Łukasz Arcimowicz, Elżbieta Chruściel, Paul Brennan, Sofian Al Shboul, Irena Dapic, Artur Pirog, Sachin Kote
Publikováno v:
Pirog, A, Faktor, J, Urban-wojciuk, Z, Kote, S, Chruściel, E, Arcimowicz, Ł, Marek-trzonkowska, N, Vojtesek, B, Hupp, T R, Al Shboul, S, Brennan, P M, Smoleński, R T, Goodlett, D R & Dapic, I 2021, ' Comparison of different digestion methods for proteomic analysis of isolated cells and FFPE tissue samples ', Talanta, vol. 233, pp. 122568 . https://doi.org/10.1016/j.talanta.2021.122568
Proteomics of human tissues and isolated cellular subpopulations create new opportunities for therapy and monitoring of a patients’ treatment in the clinic. Important considerations in such analysis include recovery of adequate amounts of protein f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3552e8f091953e30bc9b2131a5e348a1
https://doi.org/10.1016/j.talanta.2021.122568
https://doi.org/10.1016/j.talanta.2021.122568
Autor:
Adrian Kobiela, Weronika Hewelt-Belka, Joanna E. Frąckowiak, Natalia Kordulewska, Lilit Hovhannisyan, Aleksandra Bogucka, Rachel Etherington, Artur Piróg, Irena Dapic, Susanne Gabrielsson, Sara J. Brown, Graham S. Ogg, Danuta Gutowska-Owsiak
Publikováno v:
Frontiers in Immunology, Vol 15 (2024)
IntroductionExosome-enriched small extracellular vesicles (sEVs) are nanosized organelles known to participate in long distance communication between cells, including in the skin. Atopic dermatitis (AD) is a chronic inflammatory skin disease for whic
Externí odkaz:
https://doaj.org/article/593e29e6575c497eac22c075c0ba127e
Autor:
Bartłomiej Tomiczek, Jacek Czub, Artur Pirog, Igor Obuchowski, Krzysztof Liberek, Francesca Cantini, Łukasz Nierzwicki
Publikováno v:
Journal of Molecular Biology. 433:167054
Small heat shock proteins (sHsps) are a conserved class of ATP-independent chaperones which in stress conditions bind to unfolded protein substrates and prevent their irreversible aggregation. Substrates trapped in sHsps-containing aggregates are eff
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5ed9d5f03ca9e6053f0d771f10d710f
https://doi.org/10.1016/j.jmb.2021.167054
https://doi.org/10.1016/j.jmb.2021.167054
Autor:
Szymon Żwirowski, Szymon Ziętkiewicz, Krzysztof Liberek, Axel Mogk, Bernd Bukau, Agnieszka Kłosowska, Nadinath B. Nillegoda, Artur Pirog, Igor Obuchowski
Publikováno v:
The EMBO Journal. 36:783-796
Small heat shock proteins (sHsps) are an evolutionary conserved class of ATP-independent chaperones that protect cells against proteotoxic stress. sHsps form assemblies with aggregation-prone misfolded proteins, which facilitates subsequent substrate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a602c78067c56cb3239dfba593af0e98
https://doi.org/10.15252/embj.201593378
https://doi.org/10.15252/embj.201593378
Publikováno v:
PLoS Genetics, Vol 15, Iss 10, p e1008479 (2019)
PLoS Genetics
PLoS Genetics
Small heat shock proteins (sHsps) are a conserved class of ATP-independent chaperones that bind to aggregation-prone polypeptides at stress conditions. sHsps encage these polypeptides in assemblies, shielding them from further aggregation. To facilit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2073377999883bd6648d978130d5178e
https://doaj.org/article/e6bae949cadb421fa2da2f6e752e22fb
https://doaj.org/article/e6bae949cadb421fa2da2f6e752e22fb
Publikováno v:
Cancers
Cancers, Vol 12, Iss 3, p 535 (2020)
Cancers, Vol 12, Iss 3, p 535 (2020)
Neoantigen-based immunotherapies promise to improve patient outcomes over the current standard of care. However, detecting these cancer-specific antigens is one of the significant challenges in the field of mass spectrometry. Even though the first se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c8e7f3b8286071d98c98d19120f5174
https://doi.org/10.3390/cancers12030535
https://doi.org/10.3390/cancers12030535
Autor:
Artur Pirog, Sylwia Kedracka-Krok, Marta Dziedzicka-Wasylewska, Urszula Jankowska, Ewelina Fic
Publikováno v:
ELECTROPHORESIS. 31:3573-3579
Sample preparation is a fundamental step in proteomic methodologies. The quality of the results from a proteomic experiment is dependent on the nature of the sample and the properties of the proteins. In this study, various pre-treatment methods were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa01ee63f8973263736e4e926ec62f00
https://doi.org/10.1002/elps.201000197
https://doi.org/10.1002/elps.201000197
Autor:
Kornelia M. Mikula, Artur Pirog, Sylwia Kedracka-Krok, Andrzej Łyskowski, Jack C. Leo, Adrian Goldman
Trimeric autotransporter adhesins (TAAs) comprise one of the secretion pathways of the type V secretion system. The mechanism of their translocation across the outer membrane remains unclear, but it most probably occurs by the formation of a hairpin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c089099d3c16e4f0989a1b583d82922
https://ruj.uj.edu.pl/xmlui/handle/item/69472
https://ruj.uj.edu.pl/xmlui/handle/item/69472
Publikováno v:
PLoS Genetics, Vol 15, Iss 10, p e1008479 (2019)
Small heat shock proteins (sHsps) are a conserved class of ATP-independent chaperones that bind to aggregation-prone polypeptides at stress conditions. sHsps encage these polypeptides in assemblies, shielding them from further aggregation. To facilit
Externí odkaz:
https://doaj.org/article/e6bae949cadb421fa2da2f6e752e22fb