M
Markus Wiederstein
Researcher at University of Salzburg
Publications - 25
Citations - 4821
Markus Wiederstein is an academic researcher from University of Salzburg. The author has contributed to research in topics: Protein structure database & Web service. The author has an hindex of 14, co-authored 23 publications receiving 3919 citations.
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ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins.
TL;DR: The quality scores of a protein are displayed in the context of all known protein structures and problematic parts of a structure are shown and highlighted in a 3D molecule viewer in the ProSA-web service.
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A note on difficult structure alignment problems
TL;DR: The use of the TopMatch web service is described, an effective computational tool for protein structure alignment, for the visualization of structural similarities, and for highlighting relationships found in protein classifications.
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Assessment of the CASP4 fold recognition category
Manfred J. Sippl,Peter Lackner,Francisco S. Domingues,Andreas Prlić,Rainer Malik,Antonina Andreeva,Markus Wiederstein +6 more
TL;DR: The CASP4 assessment included the automated servers of the parallel CAFASP experiment and several groups submitted models that were much closer to the respective target structures than any of the known folds in the Protein Data Bank.
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Detection of Spatial Correlations in Protein Structures and Molecular Complexes
TL;DR: The structure-matching problem for oligomers and large molecular aggregates, including the largest molecular complexes known today, is solved and a number of remarkable correlations are reported.
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Nanoparticle-allergen interactions mediate human allergic responses: protein corona characterization and cellular responses
Isabella Radauer-Preiml,Ancuela Andosch,Thomas Hawranek,Ursula Luetz-Meindl,Markus Wiederstein,Jutta Horejs-Hoeck,Martin Himly,Matthew S. P. Boyles,Albert Duschl +8 more
TL;DR: It is presented that conjugation of allergens to ENMs can modulate the human allergic response, and that protease activity can be increased.