scispace - formally typeset
P

Philipp Milkereit

Researcher at University of Regensburg

Publications -  54
Citations -  2646

Philipp Milkereit is an academic researcher from University of Regensburg. The author has contributed to research in topics: Ribosomal protein & Ribosomal RNA. The author has an hindex of 25, co-authored 46 publications receiving 2391 citations. Previous affiliations of Philipp Milkereit include Heidelberg University & University of California, Santa Cruz.

Papers
More filters
Journal ArticleDOI

Roles of Eukaryotic Ribosomal Proteins in Maturation and Transport of Pre-18S rRNA and Ribosome Function

TL;DR: Comparative analysis of dynamic and steady-state maturation assays revealed that several r-proteins are required for efficient nuclear export of pre-18S rRNA, suggesting that they form an interaction platform with the export machinery.
Journal ArticleDOI

Nucleotide-induced Conformational Changes in the ATPase and Substrate Binding Domains of the DnaK Chaperone Provide Evidence for Interdomain Communication

TL;DR: Fluorescence analysis of the N-terminally located single tryptophan residue of DnaK revealed that the known ATP-induced alteration of the emission spectrum, proposed to result directly from conformational changes in the ATPase domain, requires the presence of the C-terminal domain and therefore mainly results from altered domain interaction.
Journal ArticleDOI

Maturation and Intranuclear Transport of Pre-Ribosomes Requires Noc Proteins

TL;DR: It is proposed that the dynamic interaction of Noc proteins is crucial for intranuclear movement of ribosomal precursor particles, and, thereby represent a prerequisite for proper maturation.
Journal ArticleDOI

The recruitment of RNA polymerase I on rDNA is mediated by the interaction of the A43 subunit with Rrn3

TL;DR: The results suggest that Rrn3 plays a central role in Pol I recruitment to rDNA promoters by bridging the enzyme to the core factor.
Journal ArticleDOI

Analysis of the in vivo assembly pathway of eukaryotic 40S ribosomal proteins.

TL;DR: The results show that key aspects of the assembly of eukaryotic r-proteins into distinct structural parts of the SSU are similar to the in vitro assembly pathway of their prokaryotic counterparts.