Auflistung Forschungszentren nach Autor/in "7265c713-64ff-46a6-bf0a-e461ea0e87d8"

Auflistung Forschungszentren nach Autor/in "7265c713-64ff-46a6-bf0a-e461ea0e87d8"

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  • 1H, 13C, and 15N backbone chemical-shift assignments of SARS-CoV-2 non-structural protein 1 (leader protein) 
    Wang, Ying; Kirkpatrick, John; Lage, Susanne zur; Korn, Sophie M.; Neißner, Konstantin; Schwalbe, Harald; Schlundt, Andreas; Carlomagno, Teresa (Dordrecht [u.a.] : Springer Netherlands, 2021)
    The current COVID-19 pandemic caused by the Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has become a worldwide health crisis, necessitating coordinated scientific research and urgent identification of new ...
  • Eukaryotic Box C/D methylation machinery has two non-symmetric protein assembly sites 
    Höfler, Simone; Lukat, Peer; Blankenfeldt, Wulf; Carlomagno, Teresa ([London] : Macmillan Publishers Limited, part of Springer Nature, 2021)
    Box C/D ribonucleoprotein complexes are RNA-guided methyltransferases that methylate the ribose 2’-OH of RNA. The central ‘guide RNA’ has box C and D motifs at its ends, which are crucial for activity. Archaeal guide RNAs ...
  • Histone chaperone exploits intrinsic disorder to switch acetylation specificity 
    Danilenko, Nataliya; Lercher, Lukas; Kirkpatrick, John; Gabel, Frank; Codutti, Luca; Carlomagno, Teresa (London : Nature Publishing Group, 2019)
    Histones, the principal protein components of chromatin, contain long disordered sequences, which are extensively post-translationally modified. Although histone chaperones are known to control both the activity and ...
  • An NMR Study of a 300-kDa AAA+ Unfoldase 
    Krüger, Georg; Kirkpatrick, John; Mahieu, Emilie; Franzetti, Bruno; Gabel, Frank; Carlomagno, Teresa (Amsterdam [u.a.] : Elsevier, 2023)
    AAA+ ATPases are ubiquitous hexameric unfoldases acting in cellular protein quality control. In complex with proteases, they form protein degradation machinery (the proteasome) in both archaea and eukaryotes. Here, we use ...
  • Observing Protein Degradation by the PAN-20S Proteasome by Time-Resolved Neutron Scattering 
    Mahieu, Emilie; Covès, Jaques; Krüger, Georg; Martel, Anne; Moulin, Martine; Carl, Nico; Härtlein, Michael; Carlomagno, Teresa; Franzetti, Bruno; Gabel, Frank (Cambridge, MA : Cell Press, 2020)
    The proteasome is a key player of regulated protein degradation in all kingdoms of life. Although recent atomic structures have provided snapshots on a number of conformations, data on substrate states and populations ...
  • Phosphotyrosine couples peptide binding and SHP2 activation via a dynamic allosteric network 
    Marasco, Michelangelo; Kirkpatrick, John; Nanna, Vittoria; Sikorska, Justyna; Carlomagno, Teresa (Gotenburg : Research Network of Computational and Structural Biotechnology (RNCSB), 2021)
    SHP2 is a ubiquitous protein tyrosine phosphatase, whose activity is regulated by phosphotyrosine (pY)-containing peptides generated in response to extracellular stimuli. Its crystal structure reveals a closed, auto-inhibited ...
  • Structural insights into the activity regulation of full-length non-structural protein 1 from SARS-CoV-2 
    Wang, Ying; Kirkpatrick, John; Lage, Susanne zur; Carlomagno, Teresa (London [u.a.] : Elsevier Science, 2023)
    Non-structural protein 1 (Nsp1) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is a major virulence factor and thus an attractive drug target. The last 33 amino acids of Nsp1 have been shown to bind within ...

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