Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Natalia A Szulc"'
Autor:
Abhishek Anil Dubey, Anwesha Sarkar, Karolina Milcz, Natalia A Szulc, Pankaj Thapa, Małgorzata Piechota, Remigiusz A Serwa, Wojciech Pokrzywa
Publikováno v:
PLoS Genetics, Vol 20, Iss 7, p e1011371 (2024)
The ubiquitin-proteasome system (UPS) is critical for maintaining proteostasis, influencing stress resilience, lifespan, and thermal adaptability in organisms. In Caenorhabditis elegans, specific proteasome subunits and activators, such as RPN-6, PBS
Externí odkaz:
https://doaj.org/article/3150a55118cd41d0b5c28ec8aaf968af
Publikováno v:
PLoS Computational Biology, Vol 18, Iss 6, p e1009783 (2022)
Computational methods play a pivotal role in drug discovery and are widely applied in virtual screening, structure optimization, and compound activity profiling. Over the last decades, almost all the attention in medicinal chemistry has been directed
Externí odkaz:
https://doaj.org/article/6cbd49b2c37344c7a5bbee1e99d33373
Autor:
Argho Aninda Paul, Natalia A. Szulc, Adrian Kobiela, Sara J. Brown, Wojciech Pokrzywa, Danuta Gutowska-Owsiak
Publikováno v:
Frontiers in Molecular Biosciences, Vol 10 (2023)
Background: Loss of function mutation in FLG is the major genetic risk factor for atopic dermatitis (AD) and other allergic manifestations. Presently, little is known about the cellular turnover and stability of profilaggrin, the protein encoded by F
Externí odkaz:
https://doaj.org/article/ae85490f1e744dfe9463f6a41ecd8718
Publikováno v:
Frontiers in Molecular Biosciences, Vol 8 (2021)
The proteolytic machinery activity diminishes with age, leading to abnormal accumulation of aberrant proteins; furthermore, a decline in protein degradation capacity is associated with multiple age-related proteinopathies. Cellular proteostasis can b
Externí odkaz:
https://doaj.org/article/daa381c1a9d34a4891758fb03b2be2b4
Autor:
Abhishek Anil Dubey, Magdalena Krygier, Natalia A Szulc, Karolina Rutkowska, Joanna Kosińska, Agnieszka Pollak, Małgorzata Rydzanicz, Tomasz Kmieć, Maria Mazurkiewicz-Bełdzińska, Wojciech Pokrzywa, Rafał Płoski
Publikováno v:
Human Molecular Genetics. 32:1152-1161
The principal component of the protein homeostasis network is the ubiquitin-proteasome system. Ubiquitination is mediated by an enzymatic cascade involving, i.e. E3 ubiquitin ligases, many of which belong to the cullin-RING ligases family. Genetic de
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4038c97e86f0ee313e09bae356d61b72
https://doi.org/10.1093/hmg/ddac276
https://doi.org/10.1093/hmg/ddac276
SummaryThe ubiquitin-proteasome system (UPS) removes damaged and unwanted proteins by attaching ubiquitin to lysines in a process termed ubiquitination. Little is known how functional components of the UPS, often exposed to erroneous labeling by ubiq
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1af6206a9d6aa25c6698dae9efd7f612
https://doi.org/10.1101/2023.01.18.524605
https://doi.org/10.1101/2023.01.18.524605
Ribonucleic acids (RNA) play crucial roles in living organisms as they are involved in key processes necessary for proper cell functioning. Some RNA molecules, such as bacterial ribosomes and precursor messenger RNA, are targets of small molecule dru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06633725ec57c0fe545091b5cfaf7afd
https://doi.org/10.1101/2023.01.11.523582
https://doi.org/10.1101/2023.01.11.523582
Autor:
Aniruddha Das, Pankaj Thapa, Ulises Santiago, Nilesh Shanmugam, Katarzyna Banasiak, Katarzyna Dąbrowska, Hendrik Nolte, Natalia A Szulc, Rose M Gathungu, Dominik Cysewski, Marcus Krüger, Michał Dadlez, Marcin Nowotny, Carlos J Camacho, Thorsten Hoppe, Wojciech Pokrzywa
Publikováno v:
The EMBO Journal. 41
CHIP (C-terminus of Hsc70-interacting protein) and its worm ortholog CHN-1 are E3 ubiquitin ligases that link the chaperone system with the ubiquitin-proteasome system (UPS). CHN-1 can cooperate with UFD-2, another E3 ligase, to accelerate ubiquitin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::329161793ceb2cd8c910af9e669aa886
https://doi.org/10.15252/embj.2021109566
https://doi.org/10.15252/embj.2021109566
Autor:
Janusz Bujnicki, Malgorzata Piechota, Andrea Cappannini, Filip Stefaniak, Wojciech Pokrzywa, Natalia Anna Szulc
The ubiquitin-proteasome system is a proteolytic pathway that removes damaged and unwanted proteins. Their selective turnover is initiated by ubiquitin (Ub) attachment, mainly by Ub ligases that recognize substrates through their short linear motifs
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8051ece06a30afc0b49f5bf90da340c2
https://doi.org/10.1101/2022.05.19.492622
https://doi.org/10.1101/2022.05.19.492622
The nucleolus is a dynamic nuclear biomolecular condensate involved in cellular stress response. Under proteotoxic stress, the nucleolus can store damaged proteins for refolding or degradation. HSP70 chaperone is a well-documented player in the recov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::53abf90a2279034295d0bc29d3c19c3b
https://doi.org/10.1101/2022.05.17.492288
https://doi.org/10.1101/2022.05.17.492288