SwePub
Sök i SwePub databas

  Extended search

Träfflista för sökning "WFRF:(Kaspar Miroslav) "

Search: WFRF:(Kaspar Miroslav)

  • Result 1-2 of 2
Sort/group result
   
EnumerationReferenceCoverFind
1.
  • Bubnov, Alexej, et al. (author)
  • Polar liquid crystalline monomers with two or three lactate groups for the preparation of side chain polysiloxanes
  • 2006
  • In: Liquid Crystals. - : Informa UK Limited. - 0267-8292 .- 1366-5855. ; 33:5, s. 559-566
  • Journal article (peer-reviewed)abstract
    • Two new chiral liquid crystalline monomers with bilactate or trilactate chiral units were synthesized and studied. The monomers show the paraelectric SmA and ferroelectric SmC* phases. The antiferroelectric phase was detected only for the monomer possessing the bilactate unit. The temperature dependences of the spontaneous polarization and spontaneous tilt angle were measured. Real and imaginary parts of the complex permittivity were studied as a function of frequency and temperature. The synthesized monomers contain a double bond at the end of the achiral terminal chain, and were used to prepare liquid crystalline polysiloxanes.
  •  
2.
  • Diaz-Holguin, Alejandro, et al. (author)
  • When Two Become One : Conformational Changes in FXR/RXR Heterodimers Bound to Steroidal Antagonists
  • 2023
  • In: ChemMedChem. - : John Wiley & Sons. - 1860-7179 .- 1860-7187. ; 18:4
  • Journal article (peer-reviewed)abstract
    • Farnesoid X receptor (FXR) is a nuclear receptor with an essential role in regulating bile acid synthesis and cholesterol homeostasis. FXR activation by agonists is explained by an alpha AF-2-trapping mechanism; however, antagonism mechanisms are diverse. We discuss microsecond molecular dynamics (MD) simulations investigating our recently reported FXR antagonists 2a and 2 h. We study the antagonist-induced conformational changes in the FXR ligand-binding domain, when compared to the synthetic (GW4064) or steroidal (chenodeoxycholic acid, CDCA) FXR agonists in the FXR monomer or FXR/RXR heterodimer r, and in the presence and absence of the coactivator. Our MD data suggest ligand-specific influence on conformations of different FXR-LBD regions, including the alpha 5/alpha 6 region, alpha AF-2, and alpha 9-11. Changes in the heterodimerization interface induced by antagonists seem to be associated with alpha AF-2 destabilization, which prevents both co-activator and co-repressor recruitment. Our results provide new insights into the conformational behaviour of FXR, suggesting that FXR antagonism/agonism shift requires a deeper assessment than originally proposed by crystal structures.
  •  
Skapa referenser, mejla, bekava och länka
  • Result 1-2 of 2

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 Close

Copy and save the link in order to return to this view