Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Zhuo Angel Chen"'
Autor:
Urszula M. McCaughan, Uma Jayachandran, Vadim Shchepachev, Zhuo Angel Chen, Juri Rappsilber, David Tollervey, Atlanta G. Cook
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-8 (2016)
Tsr1 is an essential ribosome biogenesis factor that has known similarity to GTPases. Here, the authors report the Tsr1 crystal structure and show that it is similar to GTPases but that active site residues are not conserved; modelling of the structu
Externí odkaz:
https://doaj.org/article/71478f9399644dc58a00d02238d1c896
Autor:
Helena Barysz, Ji Hun Kim, Zhuo Angel Chen, Damien F. Hudson, Juri Rappsilber, Dietlind L. Gerloff, William C. Earnshaw
Publikováno v:
Open Biology, Vol 5, Iss 2 (2015)
SMC proteins are essential components of three protein complexes that are important for chromosome structure and function. The cohesin complex holds replicated sister chromatids together, whereas the condensin complex has an essential role in mitotic
Externí odkaz:
https://doaj.org/article/cfecd24728e543ecaf2ab0ec2727a225
Autor:
Lara Flacht, Michele Lunelli, Karol Kaszuba, Zhuo Angel Chen, Francis J. O'. Reilly, Juri Rappsilber, Jan Kosinski, Michael Kolbe
Publikováno v:
Flacht, L, Lunelli, M, Kaszuba, K, Chen, Z A, O’Reilly, F J, Rappsilber, J, Kosinski, J & Kolbe, M 2023, ' Integrative structural analysis of the type III secretion system needle complex from shigella flexneri ', Protein Science . https://doi.org/10.1002/pro.4595
The type III secretion system (T3SS) is a large, transmembrane protein machinery used by various pathogenic gram‐negative bacteria to transport virulence factors into the host cell during infection. Understanding the structure of T3SSs is crucial f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::811cfd249d0366bca544bfe510b8043b
Autor:
Zhuo Angel Chen, Juri Rappsilber
Publikováno v:
Current Opinion in Structural Biology. 80:102599
Autor:
Sana Khan Khilji, Felix Goerdeler, Kristin Frensemeier, David Warschkau, Jost Lühle, Zeinab Fandi, Falko Schirmeister, Zhuo Angel Chen, Onur Turak, Alvaro Mallagaray, Stefan Boerno, Bernd Timmermann, Juri Rappsilber, Peter H. Seeberger, Oren Moscovitz
Publikováno v:
Cell Chemical Biology. 29:1353-1361.e6
The development of antibodies that target specific glycan structures on cancer cells or human pathogens poses a significant challenge due to the immense complexity of naturally occurring glycans. Automated glycan assembly enables the production of st
Autor:
Juri Rappsilber, Zhuo Angel Chen
Publikováno v:
Nature Protocols. 14:171-201
Quantitative cross-linking/mass spectrometry (QCLMS/QXL-MS) probes structural changes of proteins in solution. This method has revealed induced conformational changes, composition shifts in conformational ensembles and changes in protein interactions
Autor:
Wei Ming Lim, Julia Locke, Jayant Asthana, Johanna Roostalu, Fabrizio Martino, Milos A. Cvetkovic, Juri Rappsilber, Julian Gannon, Zhuo Angel Chen, Thomas Surrey, Alessandro Costa, Tanja Consolati
Publikováno v:
Biophysical Journal. 120:106a
Publikováno v:
Müller, F, Fischer, L, Chen, Z A, Auchynnikava, T & Rappsilber, J 2017, ' On the Reproducibility of Label-Free Quantitative Cross-Linking/Mass Spectrometry ', Journal of the American Society for Mass Spectrometry . https://doi.org/10.1007/s13361-017-1837-2
Journal of the American Society for Mass Spectrometry
Journal of the American Society for Mass Spectrometry
Quantitative cross-linking/mass spectrometry (QCLMS) is an emerging approach to study conformational changes of proteins and multi-subunit complexes. Distinguishing protein conformations requires reproducibly identifying and quantifying cross-linked
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c3d4f67ca1447960e9350863be982ba
https://depositonce.tu-berlin.de/handle/11303/12719
https://depositonce.tu-berlin.de/handle/11303/12719
Autor:
Christos Spanos, Alberto Riera, Zuanning Yuan, Juri Rappsilber, Saikat Nandi, Jingchuan Sun, Huilin Li, Christian Speck, Zhuo Angel Chen, Lin Bai, Marta Barbon, Bruce Stillman
Publikováno v:
Yuan, Z, Riera, A, Bai, L, Sun, J, Nandi, S, Spanos, C, Chen, Z A, Barbon, M, Rappsilber, J, Stillman, B, Speck, C & Li, H 2017, ' Structural basis of Mcm2–7 replicative helicase loading by ORC–Cdc6 and Cdt1 ', Nature Structural & Molecular Biology . https://doi.org/10.1038/nsmb.3372
Nature structural & molecular biology
Nature structural & molecular biology
To initiate DNA replication, the origin recognition complex (ORC) and Cdc6 load an Mcm2–7 double hexamer onto DNA. Without ATP hydrolysis, ORC–Cdc6 recruits one Cdt1-bound Mcm2–7 hexamer, thus forming an ORC–Cdc6–Cdt1–Mcm2–7 (OCCM) heli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0fcdecd578913d690bff6d0a8ab20bf
https://hdl.handle.net/20.500.11820/8d002902-f842-43a9-a4c8-30b7c230834f
https://hdl.handle.net/20.500.11820/8d002902-f842-43a9-a4c8-30b7c230834f
Autor:
Juri Rappsilber, Martin Jechlinger, Zhuo Angel Chen, Hueseyin Besir, Attila Gyenesei, Mirella Wawryszyn, Kapil Gupta, Ksenija Radic, Juan Zou, Markus Hsi-Yang Fritz, Imre Berger, Jonathan J M Landry, Christine Koehler, Stefan Braese, Vladimir Benes, Paul F. Sauter, Peggy Stolt-Bergner, Piau Siong Tan, Jan O. Korbel, Sini Junttila, Edward A. Lemke, Gemma Estrada Girona, Bence Galik, Carsten Schultz, Jan Erik Hoffmann, Moritz Bosse Biskup, Giancarlo Pruneri
Publikováno v:
Koehler, C, Sauter, P F, Wawryszyn, M, Girona, G E, Gupta, K, Landry, J J M, Fritz, M H Y, Radic, K, Hoffmann, J E, Chen, Z A, Zou, J, Tan, P S, Galik, B, Junttila, S, Stolt-Bergner, P, Pruneri, G, Gyenesei, A, Schultz, C, Biskup, M B, Besir, H, Benes, V, Rappsilber, J, Jechlinger, M, Korbel, J O, Berger, I, Braese, S & Lemke, E A 2016, ' Genetic code expansion for multiprotein complex engineering ', Nature Methods, vol. 13, no. 12, pp. 997-1000 . https://doi.org/10.1038/nmeth.4032
Koehler, C, Sauter, P F, Wawryszyn, M, Girona, G E, Gupta, K, Landry, J J M, Fritz, M H Y, Radic, K, Hoffmann, J E, Chen, Z A, Zou, J, Tan, P S, Galik, B, Junttila, S, Stolt-Bergner, P, Pruneri, G, Gyenesei, A, Schultz, C, Biskup, M B, Besir, H, Benes, V, Rappsilber, J, Jechlinger, M, Korbel, J O, Berger, I, Braese, S & Lemke, E A 2016, ' Genetic code expansion for multiprotein complex engineering ', Nature Methods, vol. 13, no. 12, pp. 997–1000 . https://doi.org/10.1038/nmeth.4032
Koehler, C, Sauter, P F, Wawryszyn, M, Girona, G E, Gupta, K, Landry, J J M, Fritz, M H Y, Radic, K, Hoffmann, J E, Chen, Z A, Zou, J, Tan, P S, Galik, B, Junttila, S, Stolt-Bergner, P, Pruneri, G, Gyenesei, A, Schultz, C, Biskup, M B, Besir, H, Benes, V, Rappsilber, J, Jechlinger, M, Korbel, J O, Berger, I, Braese, S & Lemke, E A 2016, ' Genetic code expansion for multiprotein complex engineering ', Nature Methods, vol. 13, no. 12, pp. 997–1000 . https://doi.org/10.1038/nmeth.4032
We present a baculovirus-based protein engineering method that enables site-specific introduction of unique functionalities in a eukaryotic protein complex recombinantly produced in insect cells. We demonstrate the versatility of this efficient and r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5c2ba09e5ec8b2f696169ad003dea91a
https://hdl.handle.net/20.500.11820/d43a4262-d2fb-415b-82ab-e8dfb28a0add
https://hdl.handle.net/20.500.11820/d43a4262-d2fb-415b-82ab-e8dfb28a0add