Zobrazeno 1 - 10
of 29
pro vyhledávání: '"Filip Yabukarski"'
Autor:
Guillaume Communie, Johnny Habchi, Filip Yabukarski, David Blocquel, Robert Schneider, Nicolas Tarbouriech, Nicolas Papageorgiou, Rob W H Ruigrok, Marc Jamin, Malene Ringkjøbing Jensen, Sonia Longhi, Martin Blackledge
Publikováno v:
PLoS Pathogens, Vol 9, Iss 9, p e1003631 (2013)
Hendra virus (HeV) is a recently emerged severe human pathogen that belongs to the Henipavirus genus within the Paramyxoviridae family. The HeV genome is encapsidated by the nucleoprotein (N) within a helical nucleocapsid. Recruitment of the viral po
Externí odkaz:
https://doaj.org/article/f545aa83c6b2468d878c9bf9a27c5149
Autor:
Cédric Leyrat, Filip Yabukarski, Nicolas Tarbouriech, Euripedes A Ribeiro, Malene Ringkjøbing Jensen, Martin Blackledge, Rob W H Ruigrok, Marc Jamin
Publikováno v:
PLoS Pathogens, Vol 7, Iss 9, p e1002248 (2011)
Replication of non-segmented negative-strand RNA viruses requires the continuous supply of the nucleoprotein (N) in the form of a complex with the phosphoprotein (P). Here, we present the structural characterization of a soluble, heterodimeric comple
Externí odkaz:
https://doaj.org/article/8fe48d2fbfa1475aa5082b35f025072a
Publikováno v:
Acta Crystallographica Section D Structural Biology. 79:212-223
X-ray crystallography has been invaluable in delivering structural information about proteins. Previously, an approach has been developed that allows high-quality X-ray diffraction data to be obtained from protein crystals at and above room temperatu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::64d2fde5905d7d68bb3af736171742ec
https://doi.org/10.1107/s205979832300089x
https://doi.org/10.1107/s205979832300089x
Publikováno v:
Acta Crystallographica Section D Structural Biology. 78:945-963
Cryo-cooling has been nearly universally adopted to mitigate X-ray damage and facilitate crystal handling in protein X-ray crystallography. However, cryo X-ray crystallographic data provide an incomplete window into the ensemble of conformations that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e6409031b5cadd501fa7b61f66c0a9c
https://doi.org/10.1107/s2059798322005939
https://doi.org/10.1107/s2059798322005939
Autor:
Siyuan Du, Stephanie A. Wankowicz, Filip Yabukarski, Tzanko Doukov, Daniel Herschlag, James S. Fraser
Publikováno v:
bioRxiv
Conformational ensembles underlie all protein functions. Thus, acquiring atomic-level ensemble models that accurately represent conformational heterogeneity is vital to deepen our understanding of how proteins work. Modeling ensemble information from
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c9000ca71fa40b7aafe2c85e3eda6f6
https://europepmc.org/articles/PMC10187334/
https://europepmc.org/articles/PMC10187334/
Autor:
Filip Yabukarski, Tzanko Doukov, Margaux M. Pinney, Justin T. Biel, James S. Fraser, Daniel Herschlag
Publikováno v:
Science advances, vol 8, iss 41
Decades of structure-function studies have established our current extensive understanding of enzymes. However, traditional structural models are snapshots of broader conformational ensembles of interchanging states. We demonstrate the need for confo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a15fe39cb8c99e51d68f4343373e5dc
https://pubmed.ncbi.nlm.nih.gov/36240280
https://pubmed.ncbi.nlm.nih.gov/36240280
Autor:
Jean-Marie Bourhis, Filip Yabukarski, Guillaume Communie, Robert Schneider, Valentina A. Volchkova, Mickaël Frénéat, Francine C. Gérard, Corinne Ducournau, Caroline Mas, Nicolas Tarbouriech, Malene Ringkjøbing Jensen, Viktor E. Volchkov, Martin Blackledge, Marc Jamin
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, 2022, 434 (10), pp.167551. ⟨10.1016/j.jmb.2022.167551⟩
Journal of Molecular Biology, 2022, 434 (10), pp.167551. ⟨10.1016/j.jmb.2022.167551⟩
International audience; To understand the dynamic interactions between the phosphoprotein (P) and the nucleoprotein (N) within the transcription/replication complex of the $Paramyxoviridae$ and to decipher their roles in regulating viral multiplicati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::deec8a0b5e039148bbb6bb0ac3086267
https://pubmed.ncbi.nlm.nih.gov/35317998
https://pubmed.ncbi.nlm.nih.gov/35317998
Autor:
Justin T Biel, Margaux M. Pinney, James S. Fraser, Tzanko Doukov, Daniel Herschlag, Filip Yabukarski
Following decades of insights from structure–function studies, there is now a need to progress from a static to dynamic view of enzymes. Comparison of prior cryo X-ray structures suggested that deleterious effects from ketosteroid isomerase (KSI) m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f506fdba27ab8f0866ea5c3d7d89601
https://doi.org/10.1101/2021.09.29.461692
https://doi.org/10.1101/2021.09.29.461692
X-ray crystallography is a cornerstone of biochemistry. Traditional freezing of protein crystals to cryo-temperatures mitigates X-ray damage and facilitates crystal handling but provides an incomplete window into the ensemble of conformations at the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d618df2b57b2121f1be04735c5723815
https://doi.org/10.1101/2021.06.27.450091
https://doi.org/10.1101/2021.06.27.450091
Autor:
Margaux M. Pinney, Alexander S. Powers, Tzanko Doukov, James S. Fraser, Justin T Biel, Daniel Herschlag, Filip Yabukarski
Publikováno v:
Proc Natl Acad Sci U S A
Proceedings of the National Academy of Sciences of the United States of America, vol 117, iss 52
Proceedings of the National Academy of Sciences of the United States of America, vol 117, iss 52
How enzymes achieve their enormous rate enhancements remains a central question in biology, and our understanding to date has impacted drug development, influenced enzyme design, and deepened our appreciation of evolutionary processes. While enzymes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::980314f56315980133dc67ec127108b3
https://pubmed.ncbi.nlm.nih.gov/33376217
https://pubmed.ncbi.nlm.nih.gov/33376217