Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Frederic H.-T. Allain"'
Autor:
Sabina Schütz, Erich Michel, Fred F. Damberger, Michaela Oplová, Cohue Peña, Alexander Leitner, Ruedi Aebersold, Frederic H.-T. Allain, Vikram Govind Panse
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Ribosomal proteins are transported to the nucleus with the help of importins, from which they are released prior to incorporation into the nascent ribosome. Here the authors report the NMR structure of the ribosomal protein eS26 in complex with the e
Externí odkaz:
https://doaj.org/article/6a9a3ed39ff54d0fae4c92979ac96f5c
Autor:
Giacomo Padroni, Maria Bikaki, Mihajlo Novakovic, Antje C. Wolter, Simon H. Rüdisser, Alvar D. Gossert, Alexander Leitner, Frederic H.-T Allain
Publikováno v:
Nucleic Acids Research, 51 (9)
The pandemic caused by SARS-CoV-2 has called for concerted efforts to generate new insights into the biology of betacoronaviruses to inform drug screening and development. Here, we establish a workflow to determine the RNA recognition and druggabilit
Autor:
Piotr Klukowski, Fred F. Damberger, Frédéric H.-T. Allain, Hideo Iwai, Harindranath Kadavath, Theresa A. Ramelot, Gaetano T. Montelione, Roland Riek, Peter Güntert
Publikováno v:
Scientific Data, Vol 11, Iss 1, Pp 1-13 (2024)
Abstract Multidimensional NMR spectra are the basis for studying proteins by NMR spectroscopy and crucial for the development and evaluation of methods for biomolecular NMR data analysis. Nevertheless, in contrast to derived data such as chemical shi
Externí odkaz:
https://doaj.org/article/d607f976b6f94288a6a64321321d3e7a
Autor:
Ahmed Moursy, Antoine Cléry, Stefan Gerhardy, Katharina M. Betz, Sanjana Rao, Jarosław Mazur, Sébastien Campagne, Irene Beusch, Malgorzata M. Duszczyk, Mark D. Robinson, Vikram Govind Panse, Frédéric H.-T. Allain
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-15 (2023)
Abstract The conserved SR-like protein Npl3 promotes splicing of diverse pre-mRNAs. However, the RNA sequence(s) recognized by the RNA Recognition Motifs (RRM1 & RRM2) of Npl3 during the splicing reaction remain elusive. Here, we developed a split-iC
Externí odkaz:
https://doaj.org/article/4a88fb1ca6af451d9d41da0376069163
Autor:
Georg Dorn, Christoph Gmeiner, Tebbe de Vries, Emil Dedic, Mihajlo Novakovic, Fred F. Damberger, Christophe Maris, Esteban Finol, Chris P. Sarnowski, Joachim Kohlbrecher, Timothy J. Welsh, Sreenath Bolisetty, Raffaele Mezzenga, Ruedi Aebersold, Alexander Leitner, Maxim Yulikov, Gunnar Jeschke, Frédéric H.-T. Allain
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-16 (2023)
Abstract RNA-binding proteins (RBPs) are crucial regulators of gene expression, often composed of defined domains interspersed with flexible, intrinsically disordered regions. Determining the structure of ribonucleoprotein (RNP) complexes involving s
Externí odkaz:
https://doaj.org/article/6ecfd082137440199e61e0254d4f1997
Publikováno v:
Methods in enzymology. 614
Understanding the RNA binding specificity of protein is of primary interest to decipher their function in the cell. Here, we review the methodology used to solve the structures of protein-RNA complexes using solution-state NMR spectroscopy: from samp
Autor:
Malgorzata M. Duszczyk, Harry Wischnewski, Tamara Kazeeva, Rajika Arora, Fionna E. Loughlin, Christine von Schroetter, Ugo Pradère, Jonathan Hall, Constance Ciaudo, Frédéric H.-T. Allain
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-17 (2022)
The authors report an unusual mode of AU-rich RNA recognition by the RNA recognition motifs of DND1, a protein essential for germline development, in a 27.5 kDa NMR structure and provide additional insight on DND1 function from cell-based experiments
Externí odkaz:
https://doaj.org/article/e56fd6d7edc04090b57e471e350a8a05
Autor:
Anna Knörlein, Chris P. Sarnowski, Tebbe de Vries, Moritz Stoltz, Michael Götze, Ruedi Aebersold, Frédéric H.-T. Allain, Alexander Leitner, Jonathan Hall
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-12 (2022)
Although UV-induced cross-linking is a widely used method to study RNA-protein complexes, the cross-linking reactions are poorly understood. Here, the authors show that π-stacking interactions between nucleobases and aromatic amino acids play a key
Externí odkaz:
https://doaj.org/article/2cd6d485f0bf4ae2b1dfd7988cfbb5cd
Autor:
Antoine Cléry, Miroslav Krepl, Cristina K. X. Nguyen, Ahmed Moursy, Hadi Jorjani, Maria Katsantoni, Michal Okoniewski, Nitish Mittal, Mihaela Zavolan, Jiri Sponer, Frédéric H.-T. Allain
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
SRSF1 is an oncoprotein that plays important roles in RNA metabolism. We reveal the structure of the human SRSF1 RRM1 bound to RNA, and propose a bimodal mode of interaction of the protein with RNA. A single mutation in RRM1 changed SRSF1 specificity
Externí odkaz:
https://doaj.org/article/f3116688ba6245dbbc7d39591d69df23
Publikováno v:
Journal of biomolecular NMR. 31(1)