Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Hans-Michael Zenn"'
Autor:
Kyoko Hiragami-Hamada, Szabolcs Soeroes, Miroslav Nikolov, Bryan Wilkins, Sarah Kreuz, Carol Chen, Inti A. De La Rosa-Velázquez, Hans Michael Zenn, Nils Kost, Wiebke Pohl, Aleksandar Chernev, Dirk Schwarzer, Thomas Jenuwein, Matthew Lorincz, Bastian Zimmermann, Peter Jomo Walla, Heinz Neumann, Tuncay Baubec, Henning Urlaub, Wolfgang Fischle
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-16 (2016)
Heterochromatin protein 1 (HP1), including HP1 α, β and γ, is a family of non-histone chromatin factors thought to be involved in chromatin organization. Here, the authors show that dimeric HP1β interacts dynamically with H3K9me3, a hallmark of h
Externí odkaz:
https://doaj.org/article/daad9f601a9746829955629c5cc1bf39
Autor:
Tuncay Baubec, Sarah Kreuz, Henning Urlaub, Carol Chen, Matthew C. Lorincz, Dirk Schwarzer, Wiebke H. Pohl, Szabolcs Soeroes, Bastian Zimmermann, Thomas Jenuwein, Miroslav Nikolov, Inti A. De La Rosa-Velázquez, Wolfgang Fischle, Aleksandar Chernev, Peter Walla, Bryan J. Wilkins, Heinz Neumann, Nils Kost, Hans Michael Zenn, Kyoko Hiragami-Hamada
Publikováno v:
Europe PubMed Central
Nature communications
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-16 (2016)
Nature communications
Nature Communications
Nature Communications, Vol 7, Iss 1, Pp 1-16 (2016)
Histone H3 trimethylation of lysine 9 (H3K9me3) and proteins of the heterochromatin protein 1 (HP1) family are hallmarks of heterochromatin, a state of compacted DNA essential for genome stability and long-term transcriptional silencing. The mechanis
Autor:
Anke Prinz, Mandy Diskar, Daniel Sohmen, Michael Boshart, Alexandra Kaupisch, Hans-Michael Zenn, Manuela Zaccolo, Melanie Kaufholz, Marco Berrera, Friedrich W. Herberg, Stefanie Brockmeyer
Publikováno v:
Journal of Biological Chemistry. 285:35910-35918
cAMP-dependent protein kinases are reversibly complexed with any of the four isoforms of regulatory (R) subunits, which contain either a substrate or a pseudosubstrate autoinhibitory domain. The human protein kinase X (PrKX) is an exemption as it is
Autor:
Hans-Michael Zenn, Viola Popara, Christian Hundsrucker, Walter Rosenthal, Friedrich W. Herberg, Bernd Reif, Burkhard Wiesner, Mangesh Joshi, Enno Klussmann, Philipp Skroblin, Jenny Eichhorst, Frank Christian
Publikováno v:
The journal of biological chemistry, 285: 5507-5521
A-kinase anchoring proteins (AKAPs) include a family of scaffolding proteins that target protein kinase A (PKA) and other signaling proteins to cellular compartments and thereby confine the activities of the associated proteins to distinct regions wi
Publikováno v:
Cellular Signalling. 19:2024-2034
Protein kinase A (PKA) isozymes are distinguishable by the inhibitory pattern of their regulatory (R) subunits with RI subunits containing a pseudophosphorylation P 0 -site and RII subunits being a substrate. Under physiological conditions, RII does
Autor:
Enno Klussmann, Philipp Skroblin, Friedrich W. Herberg, Eva K. von der Heide, Daniela Bertinetti, Laura E. Hanold, Hans-Michael Zenn, Eileen J. Kennedy, Jennifer S. Hermann, Eva-Maria Wagener
Publikováno v:
Biochimica et biophysica acta. 1854(10 Pt)
Protein kinase activity is regulated not only by direct strategies affecting activity but also by spatial and temporal regulatory mechanisms. Kinase signaling pathways are coordinated by scaffolding proteins that orchestrate the assembly of multi-pro
Autor:
Peter Walla, Markus Zweckstetter, Stefan Becker, Nasrollah Rezaei-Ghaleh, Wolfgang Fischle, Francesca Munari, Nils Kost, Alexandra Stützer, Rebecca Klingberg, Dirk Schwarzer, Kathy Ann Gelato, Bastian Zimmermann, Hans Michael Zenn, Sabrina Schröder, Adrian Schomburg, Szabolcs Soeroes
Publikováno v:
The journal of biological chemistry 287(40), 33756-33765 (2012). doi:10.1074/jbc.M112.390849
The journal of biological chemistry, 287: 33756-33765
Journal of Biological Chemistry
The journal of biological chemistry, 287: 33756-33765
Journal of Biological Chemistry
CAPSULE: BACKGROUND: Chromatin-HP1 (heterochromatin protein 1) interaction is crucial for heterochromatin assembly. RESULTS: hHP1β uses alternative interfaces to bind nucleosomes depending on histone 3 methylation within a highly dynamic complex. CO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7f67324e819c48c3733b935768b83f9
http://hdl.handle.net/11562/973712
http://hdl.handle.net/11562/973712
Publikováno v:
Antibody Engineering ISBN: 9783642011436
The hexahistidine tag is one of most commonly used fusion tags in affinity purification of recombinantly expressed proteins. Real-time binding analysis using Biacore technology allows in-depth characterization of respective association and dissociati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1bdfa3128a60e883b3a044248384f33a
https://doi.org/10.1007/978-3-642-01144-3_42
https://doi.org/10.1007/978-3-642-01144-3_42