SwePub
Sök i SwePub databas

  Utökad sökning

Träfflista för sökning "WFRF:(Gaullier G) "

Sökning: WFRF:(Gaullier G)

  • Resultat 1-4 av 4
Sortera/gruppera träfflistan
   
NumreringReferensOmslagsbildHitta
1.
  • 2019
  • Tidskriftsartikel (refereegranskat)
  •  
2.
  • Rowan, Mark G., et al. (författare)
  • Sand, salt, and models : The legacy of Bruno Vendeville
  • 2024
  • Ingår i: Journal of Structural Geology. - : Elsevier. - 0191-8141 .- 1873-1201. ; 185
  • Tidskriftsartikel (refereegranskat)abstract
    • Bruno Vendeville (1961-2022) was the foremost practitioner of analog modeling applied to the field of salt tectonics, with his work providing and promoting significant advances in our understanding of this field over more than three decades. Bruno and his collaborators contributed major works in: the mechanics of salt-related deformation; the key processes of extensional, contractional, loading-induced, and strike-slip salt tectonics; the drivers and patterns of gravity-driven, linked systems of salt-detached deformation; and the structural style and evolution of specific salt basins. In this Special Issue devoted to his legacy, we offer a series of papers that build on his foundational work and honor his critical role in advancing the theory and application of salt tectonics.
  •  
3.
  •  
4.
  • Gaullier, Guillaume, et al. (författare)
  • A higher-order entity formed by the flexible assembly of RAP1 with TRF2.
  • 2016
  • Ingår i: Nucleic Acids Research. - : Oxford University Press (OUP). - 0305-1048 .- 1362-4962. ; 44:4, s. 1962-76
  • Tidskriftsartikel (refereegranskat)abstract
    • Telomere integrity is essential to maintain genome stability, and telomeric dysfunctions are associated with cancer and aging pathologies. In human, the shelterin complex binds TTAGGG DNA repeats and provides capping to chromosome ends. Within shelterin, RAP1 is recruited through its interaction with TRF2, and TRF2 is required for telomere protection through a network of nucleic acid and protein interactions. RAP1 is one of the most conserved shelterin proteins although one unresolved question is how its interaction may influence TRF2 properties and regulate its capacity to bind multiple proteins. Through a combination of biochemical, biophysical and structural approaches, we unveiled a unique mode of assembly between RAP1 and TRF2. The complete interaction scheme between the full-length proteins involves a complex biphasic interaction of RAP1 that directly affects the binding properties of the assembly. These results reveal how a non-DNA binding protein can influence the properties of a DNA-binding partner by mutual conformational adjustments.
  •  
Skapa referenser, mejla, bekava och länka
  • Resultat 1-4 av 4

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Stäng

Kopiera och spara länken för att återkomma till aktuell vy