Zobrazeno 1 - 10
of 15
pro vyhledávání: '"Maksym Tsytlonok"'
Dynamic anticipation by Cdk2/Cyclin A-bound p27 mediates signal integration in cell cycle regulation
Autor:
Maksym Tsytlonok, Hugo Sanabria, Yuefeng Wang, Suren Felekyan, Katherina Hemmen, Aaron H. Phillips, Mi-Kyung Yun, M. Brett Waddell, Cheon-Gil Park, Sivaraja Vaithiyalingam, Luigi Iconaru, Stephen W. White, Peter Tompa, Claus A. M. Seidel, Richard Kriwacki
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
The cyclin-dependent kinase (Cdk) inhibitor p27Kip1 (p27) folds upon binding to Cdk/cyclin complexes and during cell cycle progression p27 becomes phosphorylated, which triggers its ubiquitination and degradation. Here the authors use an integrated a
Externí odkaz:
https://doaj.org/article/68150062dc9d4c4082ba200461d73f70
Autor:
Ken Peeters, Frederik Van Leemputte, Baptiste Fischer, Beatriz M. Bonini, Hector Quezada, Maksym Tsytlonok, Dorien Haesen, Ward Vanthienen, Nuno Bernardes, Carmen Bravo Gonzalez-Blas, Veerle Janssens, Peter Tompa, Wim Versées, Johan M. Thevelein
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
Yeast and cancer cells both favor sugar fermentation in aerobic conditions. Here the authors describe a conserved mechanism from yeast to mammals where the glycolysis intermediate fructose-1,6-bisphosphate binds Cdc25/Sos1 and couples increased glyco
Externí odkaz:
https://doaj.org/article/d62a394b1ae143ca9a071cacf8de2008
Dynamic anticipation by Cdk2/Cyclin A-bound p27 mediates signal integration in cell cycle regulation
Autor:
Mi-Kyung Yun, Maksym Tsytlonok, Peter Tompa, Sivaraja Vaithiyalingam, Suren Felekyan, Claus A. M. Seidel, Aaron H. Phillips, Luigi I. Iconaru, Yuefeng Wang, Hugo Sanabria, Stephen W. White, M. Brett Waddell, Richard W. Kriwacki, Katherina Hemmen, Cheon-Gil Park
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
Nature Communications
Nature Communications
p27$^{Kip1}$ (p27) is an intrinsically disordered protein (IDP) that folds upon binding to cyclin-dependent kinase (Cdk)$/$cyclin complexes (e.g., Cdk2$/$cyclin A), inhibiting their catalytic activity and causing cell cycle arrest. However, cell divi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aebf5b582a25ff50bd576925e3ed1b6a
http://arxiv.org/abs/1812.07009
http://arxiv.org/abs/1812.07009
Autor:
George L. Hamilton, Hugo Sanabria, Peter Tompa, Claus A. M. Seidel, Suren Felekyan, Katherina Hemmen, Narendar Kolimi, Maksym Tsytlonok
Publikováno v:
Biophysical Journal. 118:371a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::987010be39b512eceb00aebb892c06e4
https://doi.org/10.1016/j.bpj.2019.11.2125
https://doi.org/10.1016/j.bpj.2019.11.2125
Autor:
Maksym Tsytlonok, David Klenerman, Wenshu Xu, Angel Orte, Laura S. Itzhaki, Pamela J. E. Rowling, Shehu M. Ibrahim, Maria J. Ruedas-Rama
Publikováno v:
Structure(London, England:1993)
Summary Here, using single-molecule FRET, we reveal previously hidden conformations of the ankyrin-repeat domain of AnkyrinR, a giant adaptor molecule that anchors integral membrane proteins to the spectrin-actin cytoskeleton through simultaneous bin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df6f2da66c902641985a9d354c51e9cb
Autor:
Johan M. Thevelein, Wim Versées, Ward Vanthienen, Baptiste Fischer, Beatriz M. Bonini, Veerle Janssens, Ken Peeters, Héctor Quezada, Nuno Bernardes, Frederik Van Leemputte, Peter Tompa, Dorien Haesen, Maksym Tsytlonok, Carmen Bravo González-Blas
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
Nature Communications
Nature Communications
Yeast and cancer cells share the unusual characteristic of favoring fermentation of sugar over respiration. We now reveal an evolutionary conserved mechanism linking fermentation to activation of Ras, a major regulator of cell proliferation in yeast
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7128f6cc2fb5f5988e7deaa6158940d3
https://lirias.kuleuven.be/handle/123456789/596360
https://lirias.kuleuven.be/handle/123456789/596360
Autor:
David Serquera, Robert B. Best, Elin M. Sivertsson, Sarah Perrett, Patricio O. Craig, Maksym Tsytlonok, Peter G. Wolynes, Laura S. Itzhaki
Publikováno v:
CONICET Digital (CONICET)
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Consejo Nacional de Investigaciones Científicas y Técnicas
instacron:CONICET
Here, we reveal a remarkable complexity in the unfolding of giant HEAT-repeat protein PR65/A, a molecular adaptor for the heterotrimeric PP2A phosphatases. The repeat array ruptures at multiple sites, leading to intermediate states with noncontiguous
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c17785ba2f2d7ea445a1b9f5438c6913
https://doi.org/10.1016/j.str.2013.08.028
https://doi.org/10.1016/j.str.2013.08.028
Autor:
Laura S. Itzhaki, Pamela J. E. Rowling, Michele Vendruscolo, Maksym Tsytlonok, Pietro Sormanni
Publikováno v:
The Journal of Physical Chemistry B. 117:13029-13037
Tandem repeat proteins, which are widespread in the human genome, tend to exhibit high stability and favorable expression, and hence, they are emerging as promising protein scaffolds in alternative to antibodies in biotechnology. In order to investig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ff4e83d14430b445959c07c46526f17
https://doi.org/10.1021/jp402360x
https://doi.org/10.1021/jp402360x
Autor:
Laura S. Itzhaki, Maksym Tsytlonok
Publikováno v:
ChemBioChem. 13:1199-1205
We have investigated the use of FlAsH, a small fluorogenic molecule that binds to tetracysteine motifs, to probe folding of the 15-HEAT repeat protein PR65A. PR65A is one of a special class of modular non-globular proteins known as tandem repeat prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ee31d16d13d6c1fdf8304e6700e3e990
https://doi.org/10.1002/cbic.201200012
https://doi.org/10.1002/cbic.201200012
Publikováno v:
Gene
It is well established that G-quadruplex DNA structures form at ciliate telomeres and their formation throughout the cell-cycle by telomere-end-binding proteins (TEBPs) has been analyzed. During replication telomeric G-quadruplex structure has to be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e453bc723eff53b385bc483ab3bfdde
https://doi.org/10.1016/j.gene.2012.01.068
https://doi.org/10.1016/j.gene.2012.01.068