about
Structural basis for the accommodation of bis- and tris-aromatic derivatives in vitamin D nuclear receptorThe coarse-grained OPEP force field for non-amyloid and amyloid proteins.Structures of Aβ17-42 trimers in isolation and with five small-molecule drugs using a hierarchical computational procedure.Phosphorylation of the retinoic acid receptor alpha induces a mechanical allosteric regulation and changes in internal dynamics.Crucial role of nonspecific interactions in amyloid nucleation.The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systemsThe asymmetric binding of PGC-1α to the ERRα and ERRγ nuclear receptor homodimers involves a similar recognition mechanismTargeting the Two Oncogenic Functional Sites of the HPV E6 Oncoprotein with a High-Affinity Bivalent Ligand.Intrinsically disordered energy landscapes.Replica exchange molecular dynamics simulations of coarse-grained proteins in implicit solvent.Protein structural statistics with PSS.Structures and thermodynamics of Alzheimer's amyloid-beta Abeta(16-35) monomer and dimer by replica exchange molecular dynamics simulations: implication for full-length Abeta fibrillation.The conversion of helix H2 to beta-sheet is accelerated in the monomer and dimer of the prion protein upon T183A mutation.Substitutions at residue 211 in the prion protein drive a switch between CJD and GSS syndrome, a new mechanism governing inherited neurodegenerative disorders.Targeting the early steps of Abeta16-22 protofibril disassembly by N-methylated inhibitors: a numerical study.
P50
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P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Yassmine Chebaro
@ast
Yassmine Chebaro
@en
Yassmine Chebaro
@es
Yassmine Chebaro
@nl
Yassmine Chebaro
@sl
type
label
Yassmine Chebaro
@ast
Yassmine Chebaro
@en
Yassmine Chebaro
@es
Yassmine Chebaro
@nl
Yassmine Chebaro
@sl
prefLabel
Yassmine Chebaro
@ast
Yassmine Chebaro
@en
Yassmine Chebaro
@es
Yassmine Chebaro
@nl
Yassmine Chebaro
@sl
P106
P21
P31
P496
0000-0002-5970-2117