Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Bartlomiej, Tomiczek"'
Autor:
Bartlomiej Tomiczek, Wojciech Delewski, Lukasz Nierzwicki, Milena Stolarska, Igor Grochowina, Brenda Schilke, Rafal Dutkiewicz, Marta A Uzarska, Szymon J Ciesielski, Jacek Czub, Elizabeth A Craig, Jaroslaw Marszalek
Publikováno v:
PLoS Computational Biology, Vol 16, Iss 6, p e1007913 (2020)
J-domain proteins (JDPs), obligatory Hsp70 cochaperones, play critical roles in protein homeostasis. They promote key allosteric transitions that stabilize Hsp70 interaction with substrate polypeptides upon hydrolysis of its bound ATP. Although a rec
Externí odkaz:
https://doaj.org/article/6137714d2eb446d5ac4f961e7b40983d
Autor:
Piotr Karaś, Klaudia Kochanowicz, Marcin Pitek, Przemyslaw Domanski, Igor Obuchowski, Bartlomiej Tomiczek, Krzysztof Liberek
Evolution can tinker with multi-protein machines and replace them with simpler single-protein systems performing equivalent functions in equally efficient manner. It is unclear how, on a molecular level, such simplification can arise. With ancestral
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::38d2dcbfe53411dcbd4e741cb7e5443d
https://doi.org/10.1101/2023.05.18.541272
https://doi.org/10.1101/2023.05.18.541272
Autor:
Om Kumar Shrestha, Ruchika Sharma, Bartlomiej Tomiczek, Woonghee Lee, Marco Tonelli, Gabriel Cornilescu, Milena Stolarska, Lukasz Nierzwicki, Jacek Czub, John L Markley, Jaroslaw Marszalek, Szymon J Ciesielski, Elizabeth A Craig
Publikováno v:
PLoS ONE, Vol 14, Iss 5, p e0217098 (2019)
The J-domain protein Zuotin is a multi-domain eukaryotic Hsp70 co-chaperone. Though it is primarily ribosome-associated, positioned at the exit of the 60S subunit tunnel where it promotes folding of nascent polypeptide chains, Zuotin also has off-rib
Externí odkaz:
https://doaj.org/article/b09f12cb237047c2956e4aed7205ec36
Publikováno v:
Subcellular Biochemistry ISBN: 9783031147395
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f8d658f61fa90375f113d0efe6d51361
https://doi.org/10.1007/978-3-031-14740-1_10
https://doi.org/10.1007/978-3-031-14740-1_10
Publikováno v:
Sub-cellular biochemistry. 101
Mitochondrial J-domain protein (JDP) co-chaperones orchestrate the function of their Hsp70 chaperone partner(s) in critical organellar processes that are essential for cell function. These include folding, refolding, and import of mitochondrial prote
Autor:
Adrian M. Altenhoff, Maximilian J. Telford, Bartlomiej Tomiczek, David Dylus, Natasha Glover, Steven Müller, Christophe Dessimoz, Daniel A. Dalquen, Magdalena Zarowiecki, Jeremy Levy, Alex Warwick Vesztrocy
Publikováno v:
Genome research, vol. 29, no. 7, pp. 1152-1163
Genome Research, 29 (7)
Genome Research, 29 (7)
Genomes and transcriptomes are now typically sequenced by individual laboratories but analyzing them often remains challenging. One essential step in many analyses lies in identifying orthologs—corresponding genes across multiple species—but this
Autor:
Igor Konieczny, Urszula Walkow, Rafal Dutkiewicz, Jacek Czub, Miłosz Wieczór, María Moreno-del Álamo, Bartlomiej Tomiczek, Janusz M. Bujnicki, Igor Grochowina, Katarzyna Bury, Katarzyna Wegrzyn, Elzbieta Zabrocka, Rafael Giraldo, Urszula Uciechowska
Publikováno v:
Nucleic Acids Research
Digital.CSIC. Repositorio Institucional del CSIC
instname
Digital.CSIC. Repositorio Institucional del CSIC
instname
15 p.-6 fig.
An essential feature of replication initiation proteins is their ability to bind to DNA. In this work, we describe a new domain that contributes to a replication initiator sequence-specific interaction with DNA. Applying biochemical
An essential feature of replication initiation proteins is their ability to bind to DNA. In this work, we describe a new domain that contributes to a replication initiator sequence-specific interaction with DNA. Applying biochemical
Autor:
Albert J. Poustka, Richard R. Copley, Katharina J. Hoff, Steven Müller, Heiner Kuhl, Bernd Timmermann, Tomoe Hikosaka-Katayama, Pedro Martinez, Philipp H. Schiffer, Christophe Dessimoz, Florian Mertes, Bartlomiej Tomiczek, Morgane Thomas-Chollier, Daryl Domman, Matthias Horn, Andreas Wallberg, Maximilian J. Telford, Thomas Hankeln, Noriyuki Satoh, Marta Chiodin, Hiroaki Nakano, Hervé Philippe, Matthew L. Rowe, Maurice R. Elphick, Jonathan P. Rast
Publikováno v:
Curr. Biol. 29, 1818-1826.e6 (2019)
Current Biology
Current Biology-CB
Current Biology-CB, Elsevier, 2019, 29 (11), pp.1818-1826.e6. ⟨10.1016/j.cub.2019.04.009⟩
Current Biology-CB, 2019, 29 (11), pp.1818-1826.e6. ⟨10.1016/j.cub.2019.04.009⟩
Current Biology
Current Biology-CB
Current Biology-CB, Elsevier, 2019, 29 (11), pp.1818-1826.e6. ⟨10.1016/j.cub.2019.04.009⟩
Current Biology-CB, 2019, 29 (11), pp.1818-1826.e6. ⟨10.1016/j.cub.2019.04.009⟩
International audience; Xenoturbella and the acoelomorph worms (Xenacoelomorpha) are simple marine animals with controversial affinities. They have been placed as the sister group of all other bilaterian animals (Nephrozoa hypothesis), implying their
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6340b271957bcf9d2e3cc1bf7d50b7ef
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=56094
https://push-zb.helmholtz-muenchen.de/frontdoor.php?source_opus=56094
Autor:
Mateusz Manicki, Brenda Schilke, Lukasz Nierzwicki, Jaroslaw Marszalek, Bartlomiej Tomiczek, Wojciech Delewski, Bogumiła Paterkiewicz, Rafal Dutkiewicz, Szymon J. Ciesielski, Elizabeth A. Craig, Jacek Czub
Publikováno v:
Molecular Biology and Evolution. 33:643-656
Biogenesis of iron-sulfur clusters (FeS) is a highly conserved process involving Hsp70 and J-protein chaperones. However, Hsp70 specialization differs among species. In most eukaryotes, including Schizosaccharomyces pombe, FeS biogenesis involves int
Autor:
Maximilian J. Telford, David Dylus, Magdalena Zarowiecki, Jeremy Levy, Natasha Glover, Daniel A. Dalquen, Adrian M. Altenhoff, Steven Müller, Bartlomiej Tomiczek, Christophe Dessimoz, Alex Warwick Vesztrocy
Publikováno v:
Genome Res