LIVIVO - Das Suchportal für Lebenswissenschaften

switch to English language
Zurück zur letzten Suche Suchhistorie
Erweiterte Suche

Ihre letzten Suchen

  1. AU="Dene R. Littler"
  2. AU="Zamai, Loris"
  3. AU=Kato Takashi
  4. AU=Haase Michael
  5. AU="Ingrams, Duncan"
  6. AU=Liu Rong
  7. AU="Musselman, Kristin E"
  8. AU=Abrams M J
  9. AU="Paul, Archi Sundar"
  10. AU=Yoon Hyuk
  11. AU="Gonzalez, Emily"
  12. AU="Dunnill, M S"
  13. AU=Kuo Chih-Hung
  14. AU=Geronimo Carly L.
  15. AU=Stafforini D M
  16. AU="Sytse J. Piersma"
  17. AU="Peng, Hongke"
  18. AU="Kelly, Geoffrey"
  19. AU=Schwartzenburg Joshua AU=Schwartzenburg Joshua
  20. AU="Deshpande, Sneha Satish"
  21. AU="Ganhewa, Aparna D" AU="Ganhewa, Aparna D"
  22. AU="Flanagan, T L"
  23. AU=Davila Eduardo
  24. AU="Miroli, Augusto"
  25. AU="Stahl, B"
  26. AU="Dehari, Hironari"
  27. AU="Pinheiro, Silviane Bezerra"
  28. AU="Jamal Al Deen Alkoteesh"
  29. AU="Chen, Dingqiang"
  30. AU="Jeremy C. Ganz"
  31. AU="Lee, Ta-Sheng"
  32. AU="Shi, Jin-Ming"
  33. AU=Kristoffersen K B
  34. AU=Du Chao
  35. AU="Anton I. Skaro"

Suchergebnis

Treffer 1 - 5 von insgesamt 5

Suchoptionen

  1. Artikel ; Online: Inside-out

    Yue Pan / Indu R Chandrashekaran / Luke Tennant / Jamie Rossjohn / Dene R Littler

    PLoS ONE, Vol 18, Iss 4, p e

    Antibody-binding reveals potential folding hinge-points within the SARS-CoV-2 replication co-factor nsp9.

    2023  Band 0283194

    Abstract: Nsp9 is a conserved accessory component of the coronaviral replication and transcription complex. It is the predominant substrate of nsp12's nucleotidylation activity while also serving to recruit proteins required for viral 5'-capping. Anti-nsp9 ... ...

    Abstract Nsp9 is a conserved accessory component of the coronaviral replication and transcription complex. It is the predominant substrate of nsp12's nucleotidylation activity while also serving to recruit proteins required for viral 5'-capping. Anti-nsp9 specific nanobodies have been isolated previously. We confirm that their binding mode is centred upon Trp-53 within SARS-CoV-2 nsp9. Antibody binding at this site surprisingly results in large-scale changes to the overall topology of this coronaviral unique fold. We further characterise the antibody-induced structural dynamism within nsp9, identifying a number of potentially flexible regions. A large expansion of the cavity between the s2-s3 and s4-s5 loops is particularly noteworthy. As is the potential for large-scale movements in the C-terminal GxxxG helix.
    Schlagwörter Medicine ; R ; Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2023-01-01T00:00:00Z
    Verlag Public Library of Science (PLoS)
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

    Volltext online

    Zusatzmaterialien

    Kategorien

    Fernleihe an ZB MED

    Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

  2. Artikel ; Online: Inside-out

    Yue Pan / Indu R. Chandrashekaran / Luke Tennant / Jamie Rossjohn / Dene R. Littler

    PLoS ONE, Vol 18, Iss

    Antibody-binding reveals potential folding hinge-points within the SARS-CoV-2 replication co-factor nsp9

    2023  Band 4

    Abstract: Nsp9 is a conserved accessory component of the coronaviral replication and transcription complex. It is the predominant substrate of nsp12’s nucleotidylation activity while also serving to recruit proteins required for viral 5’-capping. Anti-nsp9 ... ...

    Abstract Nsp9 is a conserved accessory component of the coronaviral replication and transcription complex. It is the predominant substrate of nsp12’s nucleotidylation activity while also serving to recruit proteins required for viral 5’-capping. Anti-nsp9 specific nanobodies have been isolated previously. We confirm that their binding mode is centred upon Trp-53 within SARS-CoV-2 nsp9. Antibody binding at this site surprisingly results in large-scale changes to the overall topology of this coronaviral unique fold. We further characterise the antibody-induced structural dynamism within nsp9, identifying a number of potentially flexible regions. A large expansion of the cavity between the s2-s3 and s4-s5 loops is particularly noteworthy. As is the potential for large-scale movements in the C-terminal GxxxG helix.
    Schlagwörter Medicine ; R ; Science ; Q
    Sprache Englisch
    Erscheinungsdatum 2023-01-01T00:00:00Z
    Verlag Public Library of Science (PLoS)
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

    Volltext online

    Zusatzmaterialien

    Kategorien

    Fernleihe an ZB MED

    Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

  3. Artikel ; Online: Binding Studies of the Prodrug HAO472 to SARS-Cov‑2 Nsp9 and Variants

    Miaomiao Liu / Dene R. Littler / Jamie Rossjohn / Ronald J Quinn

    ACS Omega, Vol 7, Iss 8, Pp 7327-

    2022  Band 7332

    Schlagwörter Chemistry ; QD1-999
    Sprache Englisch
    Erscheinungsdatum 2022-02-01T00:00:00Z
    Verlag American Chemical Society
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

    Volltext online

    Zusatzmaterialien

    Kategorien

    Fernleihe an ZB MED

    Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

  4. Artikel ; Online: Crystal Structure of the SARS-CoV-2 Non-structural Protein 9, Nsp9

    Dene R. Littler / Benjamin S. Gully / Rhys N. Colson / Jamie Rossjohn

    iScience, Vol 23, Iss 7, Pp 101258- (2020)

    2020  

    Abstract: Summary: Many of the SARS-CoV-2 proteins have related counterparts across the Severe Acute Respiratory Syndrome (SARS-CoV) family. One such protein is non-structural protein 9 (Nsp9), which is thought to mediate viral replication, overall virulence, and ... ...

    Abstract Summary: Many of the SARS-CoV-2 proteins have related counterparts across the Severe Acute Respiratory Syndrome (SARS-CoV) family. One such protein is non-structural protein 9 (Nsp9), which is thought to mediate viral replication, overall virulence, and viral genomic RNA reproduction. We sought to better characterize the SARS-CoV-2 Nsp9 and subsequently solved its X-ray crystal structure, in an apo form and, unexpectedly, in a peptide-bound form with a sequence originating from a rhinoviral 3C protease sequence (LEVL). The SARS-CoV-2 Nsp9 structure revealed the high level of structural conservation within the Nsp9 family. The exogenous peptide binding site is close to the dimer interface and impacted the relative juxtapositioning of the monomers within the homodimer. We have established a protocol for the production of SARS-CoV-2 Nsp9, determined its structure, and identified a peptide-binding site that warrants further study to understanding Nsp9 function.
    Schlagwörter Virology ; Structural Biology ; Protein Structure Aspects ; 3D Reconstruction of Protein ; Science ; Q ; covid19
    Sprache Englisch
    Erscheinungsdatum 2020-07-01T00:00:00Z
    Verlag Elsevier
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

    Volltext online

    Zusatzmaterialien

    Kategorien

    Fernleihe an ZB MED

    Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

  5. Artikel ; Online: OZITX, a pertussis toxin-like protein for occluding inhibitory G protein signalling including Gαz

    Alastair C. Keen / Maria Hauge Pedersen / Laura Lemel / Daniel J. Scott / Meritxell Canals / Dene R. Littler / Travis Beddoe / Yuki Ono / Lei Shi / Asuka Inoue / Jonathan A. Javitch / J. Robert Lane

    Communications Biology, Vol 5, Iss 1, Pp 1-

    2022  Band 10

    Abstract: A recently identified pertussis toxin-like AB5 toxin, OZITX, is found to inhibit Gαi/o and Gαz G proteins. In combination with directed mutations, it is a useful tool for interrogating Gαi/o/z G protein subunits individually. ...

    Abstract A recently identified pertussis toxin-like AB5 toxin, OZITX, is found to inhibit Gαi/o and Gαz G proteins. In combination with directed mutations, it is a useful tool for interrogating Gαi/o/z G protein subunits individually.
    Schlagwörter Biology (General) ; QH301-705.5
    Sprache Englisch
    Erscheinungsdatum 2022-03-01T00:00:00Z
    Verlag Nature Portfolio
    Dokumenttyp Artikel ; Online
    Datenquelle BASE - Bielefeld Academic Search Engine (Lebenswissenschaftliche Auswahl)

    Volltext online

    Zusatzmaterialien

    Kategorien

    Fernleihe an ZB MED

    Sie können sich den gewünschten Titel als lokale Nutzerin oder lokaler Nutzer von ZB MED direkt an den Standort Köln schicken lassen.

Zum Seitenanfang