scispace - formally typeset
M

Manfred Schmid

Researcher at Aarhus University

Publications -  44
Citations -  5571

Manfred Schmid is an academic researcher from Aarhus University. The author has contributed to research in topics: RNA & Transcription (biology). The author has an hindex of 19, co-authored 39 publications receiving 5053 citations. Previous affiliations of Manfred Schmid include University of Geneva & Research Institute of Molecular Pathology.

Papers
More filters
Journal ArticleDOI

Regulation of chromatin structure by site-specific histone H3 methyltransferases

TL;DR: A functional interdependence of site-specific H3 tail modifications is revealed and a dynamic mechanism for the regulation of higher-order chromatin is suggested.
Journal ArticleDOI

Functional mammalian homologues of the Drosophila PEV‐modifier Su(var)3‐9 encode centromere‐associated proteins which complex with the heterochromatin component M31

TL;DR: Immodetection of endogenous Suv39h1/SUV39H1 proteins in a variety of mammalian cell lines reveals enriched distribution at heterochromatic foci during interphase and centromere‐specific localization during metaphase, and indicates the existence of a mammalian SU(VAR) complex.
Journal ArticleDOI

Isolation and Characterization of Suv39h2, a Second Histone H3 Methyltransferase Gene That Displays Testis-Specific Expression

TL;DR: Immunolocalization of Suv39h2 protein during spermatogenesis indicates enriched distribution at the heterochromatin from the leptotene to the round sperMatid stage, suggesting an additional function of the Suv 39h2 HMTase in organizing meiotic heterochromeatin that may even impart an epigenetic imprint to the male germ line.
Journal ArticleDOI

Nup-PI: the nucleopore-promoter interaction of genes in yeast.

TL;DR: The data identify the NPC basket as a new, integral participant in gene expression by showing that a specific nucleopore-to-gene-promoter interaction (Nup-PI) is an early physiological event of gene activation.
Journal ArticleDOI

The exosome: a multipurpose RNA-decay machine.

TL;DR: Structural and functional data regarding this fascinating complex and its many co-factors illuminate its diverse biochemical properties and indicate mechanisms by which RNAs are targeted for either processing or degradation.