LIVIVO - Das Suchportal für Lebenswissenschaften

switch to English language
Zurück zur letzten Suche Suchhistorie
Erweiterte Suche

Ihre letzten Suchen

  1. AU="Adly, Armin N"
  2. AU="Sorabjee, Jehangir S"
  3. AU="Torres, Ximena"
  4. AU="Ladislav?Holko"
  5. AU="Butterworth, Jessica"
  6. AU="Aziz, Masood"
  7. AU="Piovanello, Fabio"
  8. AU="Norman, Aurora"
  9. AU="Zoumpourlis, Vassilis"
  10. AU="Coleman-McCray, Joann D"
  11. AU="Carroll, Kaitlin M"
  12. AU="Zhu, Wen-Yi"
  13. AU="Bartolomé-Comas, Rosa"
  14. AU="Mathew, Josey"
  15. AU="Ali A. Shati"
  16. AU="Tavares, Guilherme M"
  17. AU="Deoni, Sean"
  18. AU="Byrne, Michael E"
  19. AU=Edwards Adrianne N.
  20. AU=Mehr Reyhaneh Niayesh
  21. AU="Par-Young, Jennefer"
  22. AU="Yon, Yongjie"
  23. AU="Laisi, Arttu"
  24. AU="Huang, Haibing"
  25. AU="Volk, Michelle"
  26. AU="Zijlstra, J. G."
  27. AU="Aditya Narayan"
  28. AU="Soliño, S. López"
  29. AU="Bervoets, Lieven"
  30. AU=Perween Reshma AU=Perween Reshma
  31. AU="Wang, Zhenduo"

Suchergebnis

Treffer 1 - 4 von insgesamt 4

Suchoptionen

  1. Artikel: Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing.

    Ng, Henry Y / Adly, Armin N / Whelpley, Devon H / Suhandynata, Raymond T / Zhou, Huilin / Morgan, David O

    bioRxiv : the preprint server for biology

    2024  

    Abstract: Cell cycle progression is governed by complexes of the cyclin-dependent kinases (CDKs) and their regulatory subunits cyclin and Cks1. CDKs phosphorylate hundreds of substrates, often at multiple sites. Multisite phosphorylation depends on Cks1, which ... ...

    Abstract Cell cycle progression is governed by complexes of the cyclin-dependent kinases (CDKs) and their regulatory subunits cyclin and Cks1. CDKs phosphorylate hundreds of substrates, often at multiple sites. Multisite phosphorylation depends on Cks1, which binds initial priming phosphorylation sites to promote secondary phosphorylation at other sites. Here, we describe a similar role for a recently discovered phosphate-binding pocket (PP) on B-type cyclins. Mutation of the PP in Clb2, the major mitotic cyclin of budding yeast, alters bud morphology and delays the onset of anaphase. Using phosphoproteomics
    Sprache Englisch
    Erscheinungsdatum 2024-02-29
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2024.02.28.582599
    Datenquelle MEDical Literature Analysis and Retrieval System 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: Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation.

    Carlson, Christopher R / Adly, Armin N / Bi, Maxine / Cheng, Yifan / Morgan, David O

    bioRxiv : the preprint server for biology

    2022  

    Abstract: The nucleocapsid (N) protein of coronaviruses is responsible for compaction of the ∼30-kb RNA genome in the ∼100-nm virion. Cryo-electron tomography suggests that each virion contains 35-40 viral ribonucleoprotein (vRNP) complexes, or ribonucleosomes, ... ...

    Abstract The nucleocapsid (N) protein of coronaviruses is responsible for compaction of the ∼30-kb RNA genome in the ∼100-nm virion. Cryo-electron tomography suggests that each virion contains 35-40 viral ribonucleoprotein (vRNP) complexes, or ribonucleosomes, arrayed along the genome. There is, however, little mechanistic understanding of the vRNP complex. Here, we show that N protein, when combined with viral RNA fragments in vitro, forms cylindrical 15-nm particles similar to the vRNP structures observed within coronavirus virions. These vRNPs form in the presence of stem-loop-containing RNA and depend on regions of N protein that promote protein-RNA and protein-protein interactions. Phosphorylation of N protein in its disordered serine/arginine (SR) region weakens these interactions and disrupts vRNP assembly. We propose that unmodified N binds stem-loop-rich regions in genomic RNA to form compact vRNP complexes within the nucleocapsid, while phosphorylated N maintains uncompacted viral RNA to promote the protein's transcriptional function.
    Sprache Englisch
    Erscheinungsdatum 2022-05-24
    Erscheinungsland United States
    Dokumenttyp Preprint
    DOI 10.1101/2022.05.23.493138
    Datenquelle MEDical Literature Analysis and Retrieval System 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: Assembly of SARS-CoV-2 ribonucleosomes by truncated N

    Adly, Armin N / Bi, Maxine / Carlson, Christopher R / Syed, Abdullah M / Ciling, Alison / Doudna, Jennifer A / Cheng, Yifan / Morgan, David O

    The Journal of biological chemistry

    2023  Band 299, Heft 12, Seite(n) 105362

    Abstract: The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) compacts the RNA genome into viral ribonucleoprotein (vRNP) complexes within virions. Assembly of vRNPs is inhibited by phosphorylation of the N protein serine/ ... ...

    Abstract The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) compacts the RNA genome into viral ribonucleoprotein (vRNP) complexes within virions. Assembly of vRNPs is inhibited by phosphorylation of the N protein serine/arginine (SR) region. Several SARS-CoV-2 variants of concern carry N protein mutations that reduce phosphorylation and enhance the efficiency of viral packaging. Variants of the dominant B.1.1 viral lineage also encode a truncated N protein, termed N
    Mesh-Begriff(e) Humans ; COVID-19/virology ; Nucleocapsid Proteins/genetics ; Nucleocapsid Proteins/metabolism ; Nucleocapsid Proteins/ultrastructure ; RNA, Viral/metabolism ; RNA, Viral/ultrastructure ; SARS-CoV-2/genetics ; SARS-CoV-2/metabolism ; SARS-CoV-2/ultrastructure ; Phosphorylation ; Virus Assembly/genetics
    Chemische Substanzen Nucleocapsid Proteins ; RNA, Viral ; nucleocapsid phosphoprotein, SARS-CoV-2
    Sprache Englisch
    Erscheinungsdatum 2023-10-19
    Erscheinungsland United States
    Dokumenttyp Journal Article
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2023.105362
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Uc I Zs.108: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

  4. Artikel ; Online: Reconstitution of the SARS-CoV-2 ribonucleosome provides insights into genomic RNA packaging and regulation by phosphorylation.

    Carlson, Christopher R / Adly, Armin N / Bi, Maxine / Howard, Conor J / Frost, Adam / Cheng, Yifan / Morgan, David O

    The Journal of biological chemistry

    2022  Band 298, Heft 11, Seite(n) 102560

    Abstract: The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 is responsible for compaction of the ∼30-kb RNA genome in the ∼90-nm virion. Previous studies suggest that each virion contains 35 to 40 viral ribonucleoprotein (vRNP) ... ...

    Abstract The nucleocapsid (N) protein of severe acute respiratory syndrome coronavirus 2 is responsible for compaction of the ∼30-kb RNA genome in the ∼90-nm virion. Previous studies suggest that each virion contains 35 to 40 viral ribonucleoprotein (vRNP) complexes, or ribonucleosomes, arrayed along the genome. There is, however, little mechanistic understanding of the vRNP complex. Here, we show that N protein, when combined in vitro with short fragments of the viral genome, forms 15-nm particles similar to the vRNP structures observed within virions. These vRNPs depend on regions of N protein that promote protein-RNA and protein-protein interactions. Phosphorylation of N protein in its disordered serine/arginine region weakens these interactions to generate less compact vRNPs. We propose that unmodified N protein binds structurally diverse regions in genomic RNA to form compact vRNPs within the nucleocapsid, while phosphorylation alters vRNP structure to support other N protein functions in viral transcription.
    Mesh-Begriff(e) Humans ; SARS-CoV-2/genetics ; Phosphorylation ; RNA, Viral/metabolism ; COVID-19/genetics ; Nucleocapsid Proteins/metabolism ; Ribonucleoproteins/metabolism ; Genomics
    Chemische Substanzen RNA, Viral ; Nucleocapsid Proteins ; Ribonucleoproteins
    Sprache Englisch
    Erscheinungsdatum 2022-10-04
    Erscheinungsland United States
    Dokumenttyp Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1016/j.jbc.2022.102560
    Datenquelle MEDical Literature Analysis and Retrieval System OnLINE

    Zusatzmaterialien

    Kategorien

    Verfügbar in ZB MED Köln/Königswinter

    Uc I Zs.108: Hefte anzeigen Standort:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
    ab Jg. 2022: Lesesaal (EG)

    Über subito bestellen

    Dieser Service ist kostenpflichtig (siehe Lieferbedingungen von subito). Bestellungen, die einen Artikel nebst Supplementary Material umfassen, werden grundsätzlich wie mehrfache Bestellungen bearbeitet. Gebühren fallen in diesen Fällen für jede einzelne Bestellung an.

Zum Seitenanfang