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Andrea Hermann
Researcher at University of Giessen
Publications - 54
Citations - 4411
Andrea Hermann is an academic researcher from University of Giessen. The author has contributed to research in topics: Fear conditioning & Medicine. The author has an hindex of 25, co-authored 43 publications receiving 3803 citations.
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Biochemistry and biology of mammalian DNA methyltransferases
TL;DR: The current understanding of the molecular enzymology of the mammalian DNA methyltransferases Dnmt1, DNmt3a, DnMT3b and Dn mt2 and the roles of the enzymes in the above-mentioned biological processes are reviewed.
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Don't fear 'fear conditioning': Methodological considerations for the design and analysis of studies on human fear acquisition, extinction, and return of fear
Tina B. Lonsdorf,Mareike M. Menz,Marta Andreatta,Miguel A. Fullana,Armita Golkar,Jan Haaker,Ivo Heitland,Andrea Hermann,Manuel Kuhn,Onno Kruse,Shira Meir Drexler,Ann Meulders,Frauke Nees,Andre Pittig,Jan Richter,Sonja Römer,Youssef Shiban,Anja Schmitz,Benjamin Straube,Bram Vervliet,Julia Wendt,Johanna M.P. Baas,Christian J. Merz +22 more
TL;DR: This compendium is intended to provide a basis for the development of a common procedural and terminology framework for the field of human fear conditioning and provides evidence‐based guidance for methodological decisions on study design, outcome measures, and analyses.
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The Dnmt1 DNA-(cytosine-C5)-methyltransferase methylates DNA processively with high preference for hemimethylated target sites.
TL;DR: It is demonstrated that unmethylated sites embedded in a hemimethylated context are modified at an approximately 24-fold reduced rate, which demonstrates that the enzyme accurately copies existing patterns of methylation.
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Binge-eating disorder: reward sensitivity and brain activation to images of food.
TL;DR: This study provides first evidence of differential brain activation to visual food stimuli in patients suffering from BED and bulimia nervosa, and displays greater arousal, ACC activation, and insula activation than the other groups.
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Mechanism of stimulation of catalytic activity of Dnmt3A and Dnmt3B DNA-(cytosine-C5)-methyltransferases by Dnmt3L.
TL;DR: Dnmt3L acts as a substrate exchange factor that accelerates DNA and AdoMet binding to de novo DNA methyltransferases and induces a conformational change of DnMT3A that opens the active site of the enzyme and promotes binding of DNA and the Ado Met.