about
Novel DNA-binding element within the C-terminal extension of the nuclear receptor DNA-binding domainThe molecular basis of conformational instability of the ecdysone receptor DNA binding domain studied by in silico and in vitro experimentsNucleoplasmin-like domain of FKBP39 from Drosophila melanogaster forms a tetramer with partly disordered tentacle-like C-terminal segments.Multidomain sumoylation of the ecdysone receptor (EcR) from Drosophila melanogaster.Sequences that direct subcellular traffic of the Drosophila methoprene-tolerant protein (MET) are located predominantly in the PAS domains.Regulatory elements in the juvenile hormone binding protein gene from Galleria mellonella--topography of binding sites for Usp and EcRDBD.Homodimerization propensity of the intrinsically disordered N-terminal domain of Ultraspiracle from Aedes aegypti.The DNA-binding domain of the ultraspiracle drives deformation of the response element whereas the DNA-binding domain of the ecdysone receptor is responsible for a slight additional change of the preformed structure.Plasticity of the ecdysone receptor DNA binding domain.Conformational changes in the DNA-binding domains of the ecdysteroid receptor during the formation of a complex with the hsp27 response element.Molecular determinants of Drosophila immunophilin FKBP39 nuclear localization.The intrinsically disordered C-terminal F domain of the ecdysteroid receptor from Aedes aegypti exhibits metal ion-binding abilityIntrinsically disordered N-terminal domain of the Helicoverpa armigera Ultraspiracle stabilizes the dimeric form via a scorpion-like structureCopper(II)-Binding Induces a Unique Polyproline Type II Helical Structure within the Ion-Binding Segment in the Intrinsically Disordered F-Domain of Ecdysteroid Receptor from Aedes aegypti.
P50
Q27644402-09CC6460-2B69-47B3-8226-B7F5D779DCF3Q28539078-3F57FAA5-AF04-46FB-AB9B-118018015A5EQ37578820-91CDF005-3230-43BD-9FE6-473337996013Q39145071-14DAF0B2-415A-4BC0-BF19-AB6E618BCAA5Q39508950-DC15ABC3-E2FC-4203-B8C5-CF4F683B1B4FQ39976670-A4F48065-92DE-4E56-A1AB-D726E8EDB115Q40211531-4366CB6B-C732-46F1-AA3F-5A411AF92A44Q42163976-E8D35400-DA0F-440F-9872-CDFA61E2AADBQ44932576-67EB6283-C1D4-4F99-B8E5-BA8C74059FFEQ47628209-22D29456-7E2E-4BBB-A9A8-6CBBB99FFA0EQ48235903-BD64CC4B-5462-4BAD-BBD5-E73D443B2B36Q61442856-4AE6F428-5CC6-41FA-B692-77235783CCFEQ89260023-D3A9F008-5B3C-4E47-A4EE-6AEDA4871DFCQ91176249-F666EBE6-436A-4EB6-9305-807591DA0C12
P50
description
Polish researcher
@en
Pools onderzoeker
@nl
investigador polacu
@ast
polnischer Forscher
@de
polski naukowiec
@pl
taighdeoir Polannach
@ga
name
Marek Orłowski
@ast
Marek Orłowski
@ca
Marek Orłowski
@de
Marek Orłowski
@en
Marek Orłowski
@es
Marek Orłowski
@fr
Marek Orłowski
@ga
Marek Orłowski
@gl
Marek Orłowski
@it
Marek Orłowski
@nl
type
label
Marek Orłowski
@ast
Marek Orłowski
@ca
Marek Orłowski
@de
Marek Orłowski
@en
Marek Orłowski
@es
Marek Orłowski
@fr
Marek Orłowski
@ga
Marek Orłowski
@gl
Marek Orłowski
@it
Marek Orłowski
@nl
altLabel
Marek Orlowski
@en
prefLabel
Marek Orłowski
@ast
Marek Orłowski
@ca
Marek Orłowski
@de
Marek Orłowski
@en
Marek Orłowski
@es
Marek Orłowski
@fr
Marek Orłowski
@ga
Marek Orłowski
@gl
Marek Orłowski
@it
Marek Orłowski
@nl
P106
P1412
P1559
Marek Orłowski
@pl
P21
P27
P31
P496
0000-0003-1282-2282