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Markus Häner

Researcher at University of Basel

Publications -  23
Citations -  2082

Markus Häner is an academic researcher from University of Basel. The author has contributed to research in topics: Protein filament & Intermediate filament. The author has an hindex of 18, co-authored 21 publications receiving 1995 citations.

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Structure and Assembly Properties of the Intermediate Filament Protein Vimentin: The Role of its Head, Rod and Tail Domains

TL;DR: The functional role of the non-helical end domains of vimentin on its assembly properties using truncated Xenopus and human recombinant proteins suggests that assembly occurred by a principally similar mechanism involving the end-on-fusion or annealing of unit-length filaments.
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Characterization of distinct early assembly units of different intermediate filament proteins.

TL;DR: The mass-per-length (MPL) composition of distinct early assembly products of recombinant intermediate filament (IF) proteins from the four cytoplasmic sequence homology classes is determined, indicating that individual types of IF proteins generate filaments with distinctly different numbers of molecules per cross-section.
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Expression of chicken lamin B2 in Escherichia coli: characterization of its structure, assembly, and molecular interactions.

TL;DR: Phosphorylation of chicken lamin B2 by cdc2 kinase interferes with the head-to-tail polymerization of the lamin dimers, which supports the notion that cdc1 kinase plays a major, direct role in triggering mitotic disassembly of the nuclear lamina.
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Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin.

TL;DR: It is proposed that hCT aggregation begins with the formation of approximately 4-nm-thick protofibrils, which interact via lateral association and coiling to form higher-order fibrillar assemblies, i.e., prot ofibril-ribbons, fibrils and tubes, tubes, and multistranded cables.
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The intermediate filament protein consensus motif of helix 2B: its atomic structure and contribution to assembly.

TL;DR: It is indicated that the YRKLLEGEE-motif is crucial for the formation of authentic tetrameric complexes and also for the control of filament width, rather than elongation, during assembly.