Dennis Claessen

Two novel homologous proteins of Streptomyces coelicolor and Streptomyces lividans are involved in the formation of the rodlet layer and mediate attachment to a hydrophobic surface.

Differentiation and anaerobiosis in standing liquid cultures of Streptomyces coelicolor.

A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils.

The formation of the rodlet layer of streptomycetes is the result of the interplay between rodlins and chaplins.

Amyloids--a functional coat for microorganisms.

Regulation of Streptomyces development: reach for the sky!

Aerial hyphae in surface cultures of Streptomyces lividans and Streptomyces coelicolor originate from viable segments surviving an early programmed cell death event.

Control of the cell elongation-division cycle by shuttling of PBP1 protein in Bacillus subtilis.

NepA is a structural cell wall protein involved in maintenance of spore dormancy in Streptomyces coelicolor.

Attachment of Streptomyces coelicolor is mediated by amyloidal fimbriae that are anchored to the cell surface via cellulose.

The assembly of individual chaplin peptides from Streptomyces coelicolor into functional amyloid fibrils.

SapB and the rodlins are required for development of Streptomyces coelicolor in high osmolarity media.

Exploiting amyloid: how and why bacteria use cross-β fibrils.

A sandwich-culture technique for controlling antibiotic production and morphological development in Streptomyces coelicolor.

Analysis of two distinct mycelial populations in liquid-grown Streptomyces cultures using a flow cytometry-based proteomics approach.

Chaplins of Streptomyces coelicolor self-assemble into two distinct functional amyloids.

The conserved DNA-binding protein WhiA is involved in cell division in Bacillus subtilis.

Bacterial solutions to multicellularity: a tale of biofilms, filaments and fruiting bodies.

Surface modification using interfacial assembly of the Streptomyces chaplin proteins.