Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Przemyslaw Karpowicz"'
Autor:
Malgorzata Gizynska, Julia Witkowska, Przemyslaw Karpowicz, Fabian Henneberg, Ashwin Chari, Artur Gieldon, Elzbieta Jankowska
Publikováno v:
Proceedings, Vol 22, Iss 1, p 99 (2019)
The proteasome degrade most of the proteins in eukaryotic cells, thereby controlling the keycellular processes [...]
Externí odkaz:
https://doaj.org/article/899f23a8feb541569c1a5ccd2d8538b0
Autor:
Maria Gaczynska, Przemyslaw Karpowicz, Christine E Stuart, Malgorzata G Norton, Jeffrey H Teckman, Ewa Marszal, Pawel A Osmulski
Publikováno v:
PLoS ONE, Vol 11, Iss 3, p e0151902 (2016)
α1-Proteinase inhibitor (antitrypsin) is a canonical example of the serpin family member that binds and inhibits serine proteases. The natural metastability of serpins is crucial to carry out structural rearrangements necessary for biological activi
Externí odkaz:
https://doaj.org/article/9d2345f5effb4458b7c0bf04237c4ffa
Autor:
E. Sandra Chocron, Erin Munkácsy, Harper S. Kim, Przemyslaw Karpowicz, Nisi Jiang, Candice E. Van Skike, Nicholas DeRosa, Andy Q. Banh, Juan P. Palavicini, Paweł Wityk, Leszek Kalinowski, Veronica Galvan, Pawel A. Osmulski, Elzbieta Jankowska, Maria Gaczynska, Andrew M. Pickering
Publikováno v:
Science Advances. 8
The proteasome has key roles in neuronal proteostasis, including the removal of misfolded and oxidized proteins, presynaptic protein turnover, and synaptic efficacy and plasticity. Proteasome dysfunction is a prominent feature of Alzheimer’s diseas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f1d0c249675ddb11b594b4f2b710fb99
https://doi.org/10.1126/sciadv.abk2252
https://doi.org/10.1126/sciadv.abk2252
Autor:
Tim H M Huang, Elżbieta Jankowska, Maria Gaczynska, Matt Giletto, Jetze J. Tepe, Pawel A. Osmulski, Theresa A. Lansdell, Przemyslaw Karpowicz
Publikováno v:
Biophysical Journal. 110(3)
Proteasome is the essential multicatalytic protease from the ubiquitin-proteasome pathway, responsible for the regulated degradation of the bulk of intracellular proteins. Cancer cells are more susceptible than healthy cells to blocking of the protea
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d426a8d274f218563d957f21005b0fd3
Autor:
Pawel A. Osmulski, Jeffrey Teckman, Christine Stuart, Maria Gaczynska, Ewa Marszal, Przemyslaw Karpowicz, Malgorzata G. Norton
Publikováno v:
PLoS ONE
PLoS ONE, Vol 11, Iss 3, p e0151902 (2016)
PLoS ONE, Vol 11, Iss 3, p e0151902 (2016)
α1-Proteinase inhibitor (antitrypsin) is a canonical example of the serpin family member that binds and inhibits serine proteases. The natural metastability of serpins is crucial to carry out structural rearrangements necessary for biological activi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7d81a2d885a05290920d478290ffcb5e
https://pubmed.ncbi.nlm.nih.gov/27008547
https://pubmed.ncbi.nlm.nih.gov/27008547
Autor:
Elzbieta, Jankowska, Piotr, Stefanowicz, Marta, Sosnowska, Przemyslaw, Karpowicz, Karolina, Radziszewska, Zbigniew, Szewczuk, Aneta, Szymańska
Publikováno v:
Proteins. 80(10)
Recently, we presented a convenient method combining a deuterium-hydrogen exchange and electrospray mass spectrometry for studying high-pressure denaturation of proteins (Stefanowicz et al., Biosci Rep 2009; 30:91-99). Here, we present results of pre
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::387955d7774b9feb333071e3e31acea3
https://pubmed.ncbi.nlm.nih.gov/22674847
https://pubmed.ncbi.nlm.nih.gov/22674847
Publikováno v:
Biophysical Journal. 106:799a
Conformational transitions and allosteric signaling are the major contributors to catalytic activity of enzymes. The proteasome is a giant, multisubunit enzyme constituting a prime example of highly dynamic and allosterically regulated structure. Thi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::590a67fafa78e142ce432a836e05b860
https://doi.org/10.1016/j.bpj.2013.11.4383
https://doi.org/10.1016/j.bpj.2013.11.4383
Autor:
Przemyslaw Karpowicz, Ewa Marszal, Wesley Jong, Christine Stuart, Pawel A. Osmulski, Martha C. Anderson, Maria Gaczynska, Malgorzata Mikolajczyk
Publikováno v:
Biophysical Journal. 104:513a
Polymerization of a mutated form of antitrypsin is postulated to cause serpinopathy, a rare and incurable genetic disease. Antitrypsin is the canonical member of the serpin superfamily of structurally homologous proteins with metastable native struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1c88cfb8bb8564a3b5305e334884b677
https://doi.org/10.1016/j.bpj.2012.11.2832
https://doi.org/10.1016/j.bpj.2012.11.2832
Autor:
Katarzyna Cekała, Karolina Trepczyk, Daria Sowik, Przemysław Karpowicz, Artur Giełdoń, Julia Witkowska, Małgorzata Giżyńska, Elżbieta Jankowska, Ewa Wieczerzak
Publikováno v:
Biomolecules, Vol 12, Iss 6, p 777 (2022)
Degradation of misfolded, redundant and oxidatively damaged proteins constitutes one of the cellular processes which are influenced by the 20S proteasome. However, its activity is generally thought to decrease with age which leads to the gradual accu
Externí odkaz:
https://doaj.org/article/561b7e4e95df42fea9091894664d8b27
Autor:
Julia Witkowska, Małgorzata Giżyńska, Przemysław Grudnik, Przemysław Golik, Przemysław Karpowicz, Artur Giełdoń, Grzegorz Dubin, Elżbieta Jankowska
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Abstract Proteasomes are responsible for protein turnover in eukaryotic cells, degrading short-lived species but also removing improperly folded or oxidatively damaged ones. Dysfunction of a proteasome results in gradual accumulation of misfolded/dam
Externí odkaz:
https://doaj.org/article/d403208b73eb48f4be63d1e3819f8b3b