Zobrazeno 1 - 10
of 79
pro vyhledávání: '"Andreas, Ostermann"'
Autor:
Takeshi Yokoyama, Shiho Fujii, Andreas Ostermann, Tobias E. Schrader, Yuko Nabeshima, Mineyuki Mizuguchi
Publikováno v:
IUCrJ, Vol 9, Iss 5, Pp 562-572 (2022)
The 70 kDa heat-shock proteins (Hsp70s) are ATP-dependent molecular chaperones that contain an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain. Hsp70s bind to misfolded/unfolded proteins and thereby prevent their
Externí odkaz:
https://doaj.org/article/2cdf4ed11871441197288c334d5d25ed
Autor:
Ai Woon Yee, Matteo Aldeghi, Matthew P. Blakeley, Andreas Ostermann, Philippe J. Mas, Martine Moulin, Daniele de Sanctis, Matthew W. Bowler, Christoph Mueller-Dieckmann, Edward P. Mitchell, Michael Haertlein, Bert L. de Groot, Elisabetta Boeri Erba, V. Trevor Forsyth
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
A number of disease-causing human transthyretin (TTR) mutations are known to lead to amyloid formation. Here the authors combine neutron crystallography, native mass spectrometry and modelling studies to characterize the T119M and S52P-TTR mutants, p
Externí odkaz:
https://doaj.org/article/d3204d9671444e838d043f4321cfd3bb
Autor:
Johannes Schiebel, Roberto Gaspari, Tobias Wulsdorf, Khang Ngo, Christian Sohn, Tobias E. Schrader, Andrea Cavalli, Andreas Ostermann, Andreas Heine, Gerhard Klebe
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
Trypsin is a serine protease. Here the authors present the high resolution X-ray and neutron diffraction structures of uncomplexed and inhibitor bound trypsin that provide insights into the geometry of H-bonds in the active site of the enzyme and mol
Externí odkaz:
https://doaj.org/article/dfa101099f7848ffada5601ea4aa65b1
Autor:
Hanna Kwon, Jaswir Basran, Cecilia M. Casadei, Alistair J. Fielding, Tobias E. Schrader, Andreas Ostermann, Juliette M. Devos, Pierre Aller, Matthew P. Blakeley, Peter C. E. Moody, Emma L. Raven
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-6 (2016)
The nature of the ferryl intermediate generated in reactions catalysed by heme-containing enzymes is uncertain, due to the ambiguity of X-ray crystallography data. Here, the authors apply neutron diffraction, kinetics and other spectroscopy to direct
Externí odkaz:
https://doaj.org/article/ba0cf1877308498b991c38c8062c0431
Autor:
Andreas Ostermann, Christopher Lampert, Yannic Volz, Martina Rudelius, Michael Staehler, Benedikt Ebner, Jürgen Behr, Dieter Munker, Katrin Milger-Kneidinger, Christian G. Stief, Stephan Ledderose, Madeleine Gapp, Oliver T. Keppler, Johannes C. Hellmuth, Max Münchhoff, Severin Rodler, Michael von Bergwelt-Baildon, Clemens Scherer, Theresa Vilsmaier, Jan-Niclas Mumm, Giuseppe Magistro, Clemens Giessen-Jung, Stephanie Schneider
Publikováno v:
Infection
Purpose To investigate the expression of the receptor protein ACE-2 alongside the urinary tract, urinary shedding and urinary stability of SARS-CoV-2 RNA. Methods Immunohistochemical staining was performed on tissue from urological surgery of 10 pati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9af0753f082b866d88822fe84376e26
https://doi.org/10.1007/s15010-021-01724-4
https://doi.org/10.1007/s15010-021-01724-4
Autor:
Tatsuya Joutsuka, Ryota Nanasawa, Keisuke Igarashi, Kazuki Horie, Masakazu Sugishima, Yoshinori Hagiwara, Kei Wada, Keiichi Fukuyama, Naomine Yano, Seiji Mori, Andreas Ostermann, Katsuhiro Kusaka, Masaki Unno
Publikováno v:
Journal of Biological Chemistry. 299:102763
PcyA, a ferredoxin-dependent bilin pigment reductase, catalyzes the site-specific reduction of the two vinyl groups of biliverdin (BV), producing phycocyanobilin. Previous neutron crystallography detected both the neutral BV and its protonated form (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c687e77ede960aea9949717b5dc3f4a3
https://doi.org/10.1016/j.jbc.2022.102763
https://doi.org/10.1016/j.jbc.2022.102763
Autor:
Rumi Shimizu, Tobias E. Schrader, Motoyasu Adachi, Chie Shibazaki, Yuji Kagotani, Andreas Ostermann
Publikováno v:
The journal of physical chemistry letters 11, 492-496 (2020). doi:10.1021/acs.jpclett.9b03252
Neutron crystallography has been used to elucidate the protonation states for the enhanced green fluorescent protein, which has revolutionized imaging technologies. The structure has a deprotonated hydroxyl group in the fluorescent chromophore. Also,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::05f78b3ecd6c3ff38ebacd44986fc4a9
https://doi.org/10.1021/acs.jpclett.9b03252
https://doi.org/10.1021/acs.jpclett.9b03252
Autor:
Andreas Ostermann, Tobias Schrader
Publikováno v:
Journal of large-scale research facilities JLSRF, Vol 1, p A2 (2015)
The single crystal diffractometer BIODIFF, which is jointly operated by the Technische Universität München and JCNS, Forschungszentrum Jülich, is designed to handle crystals with large unit cells and is dedicated to the structure determination of
Externí odkaz:
https://doaj.org/article/e98b66952f4a494f8b80fa61631d192c
Autor:
Andreas Ostermann, Tobias E. Schrader, Mineyuki Mizuguchi, Kazunori Matsumoto, Yuko Nabeshima, Takeshi Yokoyama
Publikováno v:
The FEBS Journal. 286:1656-1667
Bromodomain-containing protein 4 (BRD4) recognizes the acetylated lysine of histone H4 via its bromodomains, leading to the recruitment of positive transcription elongation factor b. Small molecules that inhibit BRD4 have potential as anticancer agen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ae410664b4c54e353aa9ef7a96c65b04
https://doi.org/10.1111/febs.14736
https://doi.org/10.1111/febs.14736
Autor:
Andreas Ostermann, Tobias E. Schrader, Tomoko Sunami, Takayoshi Kinoshita, Shigeki Arai, Motoyasu Adachi, Morihisa Saeki, Yuzuru Kurosaki, Ryota Kuroki, Rumi Shimizu, Chie Shibazaki
Publikováno v:
Journal of Molecular Biology. 430(24):5094-5104
Casein kinase 2 (CK2) has broad phosphorylation activity against various regulatory proteins, which are important survival factors in eukaryotic cells. To clarify the hydration structure and catalytic mechanism of CK2, we determined the crystal struc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3b842d5800c37e836adbdadfdd7661c
https://repo.qst.go.jp/records/49344
https://repo.qst.go.jp/records/49344