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COVID19-NMR

COVID19-NMR

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Publications

Biomol. NMR Assign. (2021). Online ahead of print

The 1H, 15N, and 13C resonance assignments of the N-terminal domain of the nucleocapsid protein from the Middle East respiratory syndrome coronavirus

T. S. de Araujo et al.

Details

J. Am. Chem. Soc. (2021) preprint

Conformational Ensembles of Noncoding Elements in the SARS-CoV-2 Genome from Molecular Dynamics Simulations

S. Bottaro et al.

Details

Biomolecular NMR Assignments (2021), 15, 219–227.

The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR

M. Schiavina, L. Pontoriero et al.

Details

RNA 2020 27(3):253-264. Online ahead of print.

The viral protein NSP1 acts as a ribosome gatekeeper for shutting down host translation and fostering SARS-CoV-2 translation

A. Tidu et al.

Details

Biomolecular NMR Assignments (2021) published online

1H, 13C, 15N and 31P chemical shift assignment for stem‐loop 4 from the 5′‐UTR of SARS‐CoV‐2

J. Vögele et al.

Details

Journal of the American Chemical Society (2021) 143:4942-4948

3D Heteronuclear Magnetization Transfers for the Establishment of Secondary Structures in SARS-CoV-2-Derived RNAs

J. Kim et al.

Details

Biomolecular NMR Assignments (2021) published online

1 H, 13 C, and 15 N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein)

Y. Wang et al.

Details

Biomolecular NMR Assignments (2021) published online

Backbone chemical shift spectral assignments of SARS coronavirus-2 non-structural protein nsp9

E. F. Dudás et al.

Details

Biomolecular NMR Assignments (2021) published online

1H, 13C and 15N Backbone chemical shift assignments of the n-terminal and central intrinsically disordered domains of SARS-CoV-2 nucleoprotein

S. Guseva et al.

Details

Angewandte Chemie International Edition (2021) Online ahead of print

Magnetization transfer to enhance NOE cross-peaks among labile protons: Applications to imino-imino sequential walks in SARS-CoV-2-derived RNAs

M. Novakovic et al.

Details

Biomolecular NMR Assignments (2021) 15:219–227

The highly flexible disordered regions of the SARS-CoV-2 nucleocapsid N protein within the 1–248 residue construct: sequence-specific resonance assignments through NMR

M. Schiavina et al.

Details

Frontiers in Molecular Biosciences (2021) published online

Large-scale recombinant production of the SARS-CoV-2 proteome for high-throughput and structural biology applications

N. Altincekic et al.

Details

PLOS Pathogens (2021) 17(2): e1009243

Metabolomic/lipidomic profiling of COVID-19 and individual response to tocilizumab

G. Meoni et al.

Details

Biomolecular NMR Assignments (2021) 15:203–211

1H, 13C and 15N chemical shift assignment of the stem-loop 5a from the 5′-UTR of SARS-CoV-2

R. Schnieders et al.

Details

Biomolecular NMR Assignments (2021) 15:173–176

1H, 13C and 15N backbone chemical shift assignments of SARS-CoV-2 nsp3a

N. Salvi et al.

Details

Biomolecular NMR Assignments (2021) 15:165–171

1H,13C and 15N chemical shift assignments of the SUD domains of SARS-CoV-2 non-structural protein 3c: “The SUD-M and SUD-C domains”

A. Gallo, A. C. Tsika, N. K. Fourkiotis et al.

Details
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Funded by


Goethe Corona Fonds

DFG

Volkswagen Stiftung

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Coordination

Prof. Dr. Harald Schwalbe (Coordinator)
Institut für Organische Chemie und Chemische Biologie
Zentrum für Biomolekulare Magnetische Resonanz

Johann Wolfgang Goethe-Universität
N160-3.13
Max-von-Laue-Strasse 7
D-60438 Frankfurt am Main

Contact us

++49 69 798 29737
schwalbe@nmr.uni-frankfurt.de

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