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Bejelentkezés
A Tudóstér funkcióinak nagy része bejelentkezés nélkül is elérhető. Bejelentkezésre az alábbi műveletekhez van szükség:
Debreceni Egyetem. Általános Orvostudományi Kar. Orvosi Vegytani Intézet / University of Debrecen. Faculty of Medicine. Department of Medical Chemistry
Ghani, M.,
Szabó, B.,
Alkhatibe, M.,
Amsalu, H.,
Zohar, P.,
Janka, E. A.,
Mótyán, J. A.,
Tar, K.:
Serine 39 in the GTP-binding domain of Drp1 is involved in shaping mitochondrial morphology.
FEBS Open Bio. 14 (7), 1147-1165, 2024.
Q2
Biochemistry, Genetics and Molecular Biology (miscellaneous)
2.
Ghani, M.,
Zohar, P.,
Ujlaki, G.,
Tóth, M.,
Amsalu, H.,
Póliska, S.,
Tar, K.:
Stable knockdown of Drp1 improves retinoic acid-BDNF-induced neuronal differentiation through global transcriptomic changes and results in reduced phosphorylation of ERK1/ 2 independently of DUSP1 and 6.
Front. Cell. Dev. Biol. 12, 1-25, 2024.
Alatshan, A.,
Kovács, G. E.,
Aladdin, A.,
Czimmerer, Z.,
Tar, K.,
Benkő, S.:
All-Trans Retinoic Acid Enhances both the Signaling for Priming and the Glycolysis for Activation of NLRP3 Inflammasome in Human Macrophage.
Cells. 9 (7), 1591, 2020.
Lontay, B.,
Kiss, A.,
Virág, L.,
Tar, K.:
How Do Post-Translational Modifications Influence the Pathomechanistic Landscape of Huntington's Disease? A Comprehensive Review.
Int. J. Mol. Sci. 21 (12), 1-34, 2020.
Douida, A.,
Batista, F.,
Robaszkiewicz, A.,
Botó, P.,
Aladdin, A.,
Szenykiv, M.,
Czinege, R.,
Virág, L.,
Tar, K.:
The proteasome activator PA200 regulates expression of genes involved in cell survival upon selective mitochondrial inhibition in neuroblastoma cells.
J. Cell. Mol. Med. 24 (12), 6716-6730, 2020.
Aladdin, A.,
Yao, Y.,
Yang, C.,
Kahlert, G.,
Ghani, M.,
Király, N.,
Boratkó, A.,
Uray, K.,
Dittmar, G.,
Tar, K.:
The Proteasome Activators Blm10/PA200 Enhance the Proteasomal Degradation of N-Terminal Huntingtin.
Biomolecules. 10 (11), 1-33, 2020.
Aladdin, A.,
Király, R.,
Botó, P.,
Regdon, Z.,
Tar, K.:
Juvenile Huntington's disease skin fibroblasts respond with elevated parkin level and increased proteasome activity as a potential mechanism to counterbalance the pathological consequences of mutant huntingtin protein.
Int. J. Mol. Sci. 20 (21), 1-39, 2019.
Bonnet-Garnier, A.,
Kiêu, K.,
Aguirre-Lavin, T.,
Tar, K.,
Flores, P.,
Liu, Z.,
Peynot, N.,
Chebrout, M.,
Dinnyés, A.,
Duranthon, V.,
Beaujean, N.:
Three-dimensional analysis of nuclear heterochromatin distribution during early development in the rabbit.
Chromosoma. 127 (3), 387-403, 2018.
Yao, Y.,
Tsuchiyama, S.,
Yang, C.,
Bulteau, A. L.,
He, C.,
Robison, B.,
Tsuchiya, M.,
Miller, D.,
Briones, V.,
Tar, K.,
Potrero, A.,
Friguet, B.,
Kennedy, B. K.,
Schmidt, M.:
Proteasomes, Sir2, and Hxk2 form an interconnected aging network that impinges on the AMPK/Snf1-regulated transcriptional repressor Mig1.
PLoS Genet. 11 (1), 1-27, 2015.
Tar, K.,
Dange, T.,
Yang, C.,
Yao, Y.,
Bulteau, A. L.,
Salcedo, E. F.,
Braigen, S.,
Bouillaud, F.,
Finley, D.,
Schmidt, M.:
Proteasomes associated with the Blm10 activator protein antagonize mitochondrial fission through degradation of the fission protein Dnm1.
J. Biol. Chem. 289 (17), 12145-12156, 2014.
Short, M. K.,
Hallett, J. P.,
Tar, K.,
Dange, T.,
Schmidt, M.,
Moir, R.,
Willis, I. M.,
Jubinsky, P. T.:
The yeast magmas ortholog pam16 has an essential function in fermentative growth that involves sphingolipid metabolism.
PLoS One. 7 (7), 1-16, 2012.
Lopez, A. D.,
Tar, K.,
Krügel, U.,
Dange, T.,
Ros, I. G.,
Schmidt, M.:
Proteasomal degradation of Sfp1 contributes to the repression of ribosome biogenesis during starvation and is mediated by the proteasome activator Blm10.
Mol. Biol. Cell. 22 (5), 528-540, 2011.
Rungarunlert, S.,
Tar, K.,
Muenthaisong, S.,
Techakumphu, M.,
Pirity, M. K.,
Dinnyés, A.:
Differentiation of mouse embryonic stem cells into cardiomyocytes by using slow turning lateral vessel (stlv/bioreactor).
Reprod. Fertil. Dev. 22 (1), 355, 2010.
Pospisilik, J. A.,
Schramek, D.,
Schnidar, H.,
Cronin, S. J. F.,
Nehme, N. T.,
Zhang, X.,
Knauf, C.,
Cani, P. D.,
Aumayr, K.,
Todoric, J.,
Bayer, M.,
Haschemi, A.,
Puviindran, V.,
Tar, K.,
Orthofer, M.,
Neely, G. G.,
Dietzl, G.,
Manoukian, A.,
Funovics, M.,
Prager, G.,
Wagner, O.,
Ferrandon, D.,
Aberger, F.,
Hui, C. c.,
Esterbauer, H.,
Penninger, J. M.:
Drosophila genome-wide obesity screen reveals hedgehog as a determinant of brown versus white adipose cell fate.
Cell. 140 (1), 148-160, 2010.
D1
Biochemistry, Genetics and Molecular Biology (miscellaneous)
2009
20.
Kobolák, J.,
Kiss, K.,
Polgár, Z.,
Mamo, S.,
Rogel-Gaillard, C.,
Táncos, Z.,
Bock, I.,
Baji, Á. G.,
Tar, K.,
Pirity, M. K.,
Dinnyés, A.:
Promoter analysis of the rabbit POU5F1 gene and its expression in preimplantation stage embryos.
BMC Mol. Biol. 10 (1), 1-12, 2009.
Tar, K.,
Csortos, C.,
Czikora, I.,
Oláh, G.,
Ma, S. F.,
Wadgaonkar, R.,
Gergely, P.,
Garcia, J. G. N.,
Verin, A.:
Role of protein phosphatase 2A in the regulation of endothelial cell cytoskeleton structure.
J. Cell. Biochem. 98 (4), 931-953, 2006.
Tar, K.,
Csortos, C.,
Czikora, I.,
Oláh, G.,
Ma, S. F.,
Wadgaonkar, R.,
Gergely, P.,
Garcia, J.,
Verin, A.:
The role of protein phosphatase 2A in the regulation of endothelial cell cytoskeleton structure.
J. Invest. Med. 54 (2), 350, 2006.
Teckchandani, A. M.,
Birukova, A. A.,
Tar, K.,
Verin, A.,
Tsygankov, A. Y.:
The multidomain protooncogenic protein c-Cb1 binds to tubulin and stabilizes microtubules.
Exp. Cell Res. 306 (1), 114-127, 2005.
Tar, K.,
Birukova, A. A.,
Csortos, C.,
Bakó, É.,
Garcia, J. G. N.,
Verin, A.:
Phosphatase 2A is involved in endothelial cell microtubule remodeling and barrier regulation.
J. Cell. Biochem. 92 (3), 534-546, 2004.
Tar, K.,
Csortos, C.,
Birukova, A. A.,
Garcia, J.,
Verin, A.:
Role of phosphatase 2A antivity in microtubule-mediated endothelial cell cytoskeleton rearrangement.
Faseb J. 18 (4), 716-717, 2004.
