Detailansicht

Wissensnetz

Person

Dorothee Dormann (1976-)

Biochemikerin

Name	Dorothee Dormann
Zeit	1976- (Lebensdaten)
Ort	Schorndorf (Rems-Murr-Kreis) (Geburtsort) Deutschland
Geschlecht	weiblich
Beruf	Biochemikerin (charakteristischer Beruf) Cytologin
Variante	Dorothee Schmid (früherer Name)
Weitere Angaben	bis 2007 veröffentlichte sie auch unter ihrem Geburtsnamen Schmid
Datensatztyp	Person
GND-Nummer	1217618783
Datensatz-ID	1217618783
Beteiligt an alle anzeigen Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation Multi-omics profiling identifies a deregulated FUS-MAP1B axis in ALS/FTD-associated UBQLN2 mutants Gestörter Kerntransport und Phasentrennung von RNA-Bindeproteinen Phosphorylation Regulates CIRBP Arginine Methylation, Transportin-1 Binding and Liquid-Liquid Phase Separation Lysine/RNA-interactions drive and regulate biomolecular condensation Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1 Identification of the nuclear export pathways of TDP‐43 and FUS Interaction modulation through arrays of clustered methyl-arginine protein modifications Pathomechanisms driving phase separation and aggregation of the fused in sarcoma protein in neurodegenerative diseases Motor neuron intrinsic and extrinsic mechanisms contribute to the pathogenesis of FUS-associated amyotrophic lateral sclerosis Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS

Hinweis

Die Betaversion beinhaltet noch nicht alle Funktionen und Informationen des Katalogs des DNB-Portals. Falls Sie Informationen vermissen oder ein Medium bestellen wollen, besuchen Sie bitte die entsprechende Seite im Katalog des DNB-Portals über folgenden Link:

Katalog der Deutschen Nationalbibliothek

Dorothee Dormann (1976-)

Targeting the glycine-rich domain of TDP-43 with antibodies prevents its aggregation in vitro and reduces neurofilament levels in vivo

Disease‐linked TDP‐43 hyperphosphorylation suppresses TDP‐43 condensation and aggregation

Multi-omics profiling identifies a deregulated FUS-MAP1B axis in ALS/FTD-associated UBQLN2 mutants

Gestörter Kerntransport und Phasentrennung von RNA-Bindeproteinen

Phosphorylation Regulates CIRBP Arginine Methylation, Transportin-1 Binding and Liquid-Liquid Phase Separation

Lysine/RNA-interactions drive and regulate biomolecular condensation

Nuclear egress of TDP-43 and FUS occurs independently of Exportin-1/CRM1

Identification of the nuclear export pathways of TDP‐43 and FUS

Interaction modulation through arrays of clustered methyl-arginine protein modifications

Pathomechanisms driving phase separation and aggregation of the fused in sarcoma protein in neurodegenerative diseases

Motor neuron intrinsic and extrinsic mechanisms contribute to the pathogenesis of FUS-associated amyotrophic lateral sclerosis

Cytoplasmic poly-GA aggregates impair nuclear import of TDP-43 in C9orf72 ALS/FTLD

Monomethylated and unmethylated FUS exhibit increased binding to Transportin and distinguish FTLD-FUS from ALS-FUS