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Thomas Walzthoeni

Researcher at ETH Zurich

Publications -  18
Citations -  4027

Thomas Walzthoeni is an academic researcher from ETH Zurich. The author has contributed to research in topics: Protein structure & Mass spectrometry. The author has an hindex of 16, co-authored 16 publications receiving 3722 citations. Previous affiliations of Thomas Walzthoeni include University of Innsbruck & University of Zurich.

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Molecular architecture of the 26S proteasome holocomplex determined by an integrative approach

TL;DR: In this paper, the molecular structure of the 26S holocomplex was determined by an integrative approach based on data from cryoelectron microscopy, X-ray crystallography, residue-specific chemical cross-linking, and several proteomics techniques.
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Probing Native Protein Structures by Chemical Cross-linking, Mass Spectrometry, and Bioinformatics

TL;DR: In this article, the authors discuss the critical steps of chemical cross-linking and its implications for (structural) biology: reagent design and cross-link protocols, separation and mass spectrometric analysis of cross-linked samples, dedicated software for data analysis, and the use of crosslink data for computational modeling.
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Identification of cross-linked peptides from large sequence databases

TL;DR: It is shown that xQuest can identify cross-linked peptides from a total Escherichia coli lysate with an unrestricted database search and reduces the search space by an upstream candidate-peptide search before the recombination step.

Probing Native Protein Structures by Chemical Cross-linking, Mass Spectrometry, and Bioinformatics

TL;DR: The critical steps of chemical cross-linking and its implications for (structural) biology are discussed: reagent design and cross- linking protocols, separation and mass spectrometric analysis of cross-linked samples, dedicated software for data analysis, and the use ofCross-l linking data for computational modeling.
Journal ArticleDOI

Structural Probing of a Protein Phosphatase 2A Network by Chemical Cross-Linking and Mass Spectrometry

TL;DR: This study establishes XL-MS as an integral part of hybrid structural biology approaches for the analysis of endogenous protein complexes by gaining distance restraints on a modular interaction network of protein complexes affinity-purified from human cells by applying an adaptedXL-MS protocol.