Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Stefan Schüchner"'
Autor:
Ingrid E. Frohner, Ingrid Mudrak, Stefan Schüchner, Dorothea Anrather, Markus Hartl, Jean-Marie Sontag, Estelle Sontag, Brian E. Wadzinski, Teresa Preglej, Wilfried Ellmeier, Egon Ogris
Publikováno v:
Cell Reports, Vol 30, Iss 9, Pp 3171-3182.e6 (2020)
Summary: Protein phosphatase 2A (PP2A) is an important regulator of signal transduction pathways and a tumor suppressor. Phosphorylation of the PP2A catalytic subunit (PP2AC) at tyrosine 307 has been claimed to inactivate PP2A and was examined in mor
Externí odkaz:
https://doaj.org/article/12025806a45840e6a5dff7f2dc343abb
Autor:
Marko Roblek, Stefan Schüchner, Veronika Huber, Katrin Ollram, Sylvia Vlcek-Vesely, Roland Foisner, Manfed Wehnert, Egon Ogris
Publikováno v:
PLoS ONE, Vol 5, Iss 5, p e10604 (2010)
Disease-linked missense mutations can alter a protein's function with fatal consequences for the affected individual. How a single amino acid substitution in a protein affects its properties, is difficult to study in the context of the cellular prote
Externí odkaz:
https://doaj.org/article/e098ed80ff6e4b34b01d1ee891463f44
Publikováno v:
Sci Signal
The methyl-esterification of the C-terminal leucine of the protein phosphatase 2A (PP2A) catalytic (C) subunit is essential for the assembly of specific trimeric PP2A holoenzymes, and this region of the C subunit also contains two threonine and tyros
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6d7a8298088dcc1706975f89a597b09c
https://doi.org/10.1126/scisignal.aax6490
https://doi.org/10.1126/scisignal.aax6490
Publikováno v:
Science Signaling. 13
Epitope tags are short, linear antibody recognition sequences that enable detection of tagged fusion proteins by antibodies. Epitope tag position and neighboring sequences potentially affect its recognition by antibodies, and such context-dependent d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4c41b1923edfe2581f94eda846210800
https://doi.org/10.1126/scisignal.aax9730
https://doi.org/10.1126/scisignal.aax9730
Autor:
Ingrid E, Frohner, Ingrid, Mudrak, Stefan, Schüchner, Dorothea, Anrather, Markus, Hartl, Jean-Marie, Sontag, Estelle, Sontag, Brian E, Wadzinski, Teresa, Preglej, Wilfried, Ellmeier, Egon, Ogris
Publikováno v:
Cell reports. 30(9)
Protein phosphatase 2A (PP2A) is an important regulator of signal transduction pathways and a tumor suppressor. Phosphorylation of the PP2A catalytic subunit (PP2A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::fb00a49a1089fadfff64adaaffc3095f
https://pubmed.ncbi.nlm.nih.gov/32130916
https://pubmed.ncbi.nlm.nih.gov/32130916
Autor:
Stefan Schüchner, Derek J. Taylor, Abbey L. Perl, David L. Brautigan, Goutham Narla, Wenqing Xu, Zhizhi Wang, Daniela Schlatzer, Danica Wiredja, Daniel Leonard, Nikhil Vasireddi, Wei Huang, Caitlin M. O’Connor, Yinghua Chen, Janna Kiselar, Nilesh Zaware, Egon Ogris, Sudeh Izadmehr, Matthew D. Glasky
Publikováno v:
Cancer Research. 80:2981-2981
Development of molecularly targeted therapies have shifted our clinical approach to cancer allowing for an integrated treatment approach where tumor genotype and molecular profiles are paired in a clinically actionable manner with specific targeted t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ce63126750ce1d7e94a137d9317ecdee
https://doi.org/10.1158/1538-7445.am2020-2981
https://doi.org/10.1158/1538-7445.am2020-2981
Autor:
Stefan Schüchner, Caitlin M. O’Connor, David L. Brautigan, Sudeh Izadmehr, Daniel Leonard, Daniela Schlatzer, Nikhil Vasireddi, Nilesh Zaware, Egon Ogris, Wenqing Xu, Yinghua Chen, Goutham Narla, Derek J. Taylor, Danica Wiredja, Janna Kiselar, Zhizhi Wang, Matthew D. Galsky, Abbey L. Perl, Wei Huang
Publikováno v:
Trends Pharmacol Sci
Summary Impairment of protein phosphatases, including the family of serine/threonine phosphatases designated PP2A, is essential for the pathogenesis of many diseases, including cancer. The ability of PP2A to dephosphorylate hundreds of proteins is re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af5cdf458381f0be1d704910cb47013a
https://doi.org/10.1016/j.cell.2020.03.038
https://doi.org/10.1016/j.cell.2020.03.038
Autor:
Egon Ogris, Ingrid Mudrak, Jean-Marie Sontag, Estelle Sontag, Wilfried Ellmeier, Teresa Preglej, Brian E. Wadzinski, Ingrid E. Frohner, Markus Hartl, Stefan Schüchner, Dorothea Anrather
Publikováno v:
Cell Reports, Vol 30, Iss 9, Pp 3171-3182.e6 (2020)
Summary: Protein phosphatase 2A (PP2A) is an important regulator of signal transduction pathways and a tumor suppressor. Phosphorylation of the PP2A catalytic subunit (PP2AC) at tyrosine 307 has been claimed to inactivate PP2A and was examined in mor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce8fb8b984281938a6983696636d8c28
https://doi.org/10.1016/j.celrep.2020.02.035
https://doi.org/10.1016/j.celrep.2020.02.035
Autor:
Therese Montgomery, Egon Ogris, Thomas Steinkellner, Michael Freissmuth, Harald H. Sitte, Florian Koban, Sonja Sucic, Stefan Schüchner
Publikováno v:
The Journal of Neuroscience. 34:6344-6351
Export of the serotonin transporter (SERT) from the endoplasmic reticulum (ER) is mediated by the SEC24C isoform of the coatomer protein-II complex. SERT must enter the axonal compartment and reach the presynaptic specialization to perform its functi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eeb640e44ec7e8129cab3205ca9caed8
https://doi.org/10.1523/jneurosci.2991-13.2014
https://doi.org/10.1523/jneurosci.2991-13.2014
Publikováno v:
Scientific Reports
Western blotting is one of the most widely used techniques in molecular biology and biochemistry. Prestained proteins are used as molecular weight standards in protein electrophoresis. In the chemiluminescent Western blot analysis, however, these col
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4be18164c7f28d2d756369f93fa516a1
https://pubmed.ncbi.nlm.nih.gov/27531616
https://pubmed.ncbi.nlm.nih.gov/27531616