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Birk, Sebastian; Chapman, Daniel; Carvalho, Laurence; Spears, Bryan M; Andersen, Hans Estrup; Argillier, Christine; Auer, Stefan; Baattrup-Pedersen, Annette; Banin, Lindsay; Beklioglu, Meryem; Bondar-Kunze, Elisabeth; Borja, Angel; Branco, Paulo; Bucak, Tuba; Buijse, Anthonie D; Cardoso, Ana Cristina; Couture, Raoul-Marie; Cremona, Fabien; de Zwart, Dick; Feld, Christian K; Ferreira, M Teresa; Feuchtmayr, Heidrun; Gessner, Mark O; Gieswein, Alexander; Globevnik, Lidija; Graeber, Daniel; Graf, Wolfram; Gutiérrez-Cánovas, Cayetano; Hanganu, Jenica; Iskin, Ugur; Järvinen, Marko; Jeppesen, Erik; Kotamäki, Niina; Kuijper, Marijn; Lemm, Jan U; Lu, Shenglan; Solheim, Anne Lyche; Mischke, Ute; Moe, S Jannicke; Nõges, Peeter; Nõges, Tiina; Ormerod, Steve J; Panagopoulos, Yiannis; Phillips, Geoff; Posthuma, Leo; Pouso, Sarai; Prudhomme, Christel; Rankinen, Katri; Rasmussen, Jes J; Richardson, Jessica.

Nat Ecol Evol ; 4(8): 1060-1068, 2020 08.

Artículo en Inglés | MEDLINE | ID: mdl-32541802

16.

A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates.

Auer, Stefan; Meersman, Filip; Dobson, Christopher M; Vendruscolo, Michele.

PLoS Comput Biol ; 4(11): e1000222, 2008 Nov.

Artículo en Inglés | MEDLINE | ID: mdl-19008938

17.

Simple Model of the Effect of Solution Conditions on the Nucleation of Amyloid Fibrils.

Auer, Stefan.

J Phys Chem B ; 121(38): 8893-8901, 2017 09 28.

Artículo en Inglés | MEDLINE | ID: mdl-28707467

18.

Effects of river bank heterogeneity and time of day on drift and stranding of juvenile European grayling (Thymallus thymallus L.) caused by hydropeaking.

Auer, Stefan; Zeiringer, Bernhard; Führer, Simon; Tonolla, Diego; Schmutz, Stefan.

Sci Total Environ ; 575: 1515-1521, 2017 Jan 01.

Artículo en Inglés | MEDLINE | ID: mdl-27793351

19.

Amyloid fibril nucleation: effect of amino acid hydrophobicity.

Auer, Stefan.

J Phys Chem B ; 118(20): 5289-99, 2014 May 22.

Artículo en Inglés | MEDLINE | ID: mdl-24784223

20.

Tracking polypeptide folds on the free energy surface: effects of the chain length and sequence.

Brukhno, Andrey V; Ricchiuto, Piero; Auer, Stefan.

J Phys Chem B ; 116(29): 8703-13, 2012 Jul 26.

Artículo en Inglés | MEDLINE | ID: mdl-22624618

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Thermodynamic phase diagram of amyloid-ß (16-22) peptide.

A numerical study to determine the effect of ligament stiffness on kinematics of the lumbar spine during flexion.

Nucleation of polymorphic amyloid fibrils.

Confounding the paradigm: peculiarities of amyloid fibril nucleation.

Breakdown of nucleation theory for crystals with strongly anisotropic interactions between molecules.

Size distribution of amyloid nanofibrils.

Phase diagram of polypeptide chains.

Communication: Conformation state diagram of polypeptides: a chain length induced α-ß transition.

Insight into the correlation between lag time and aggregation rate in the kinetics of protein aggregation.

Phase diagram of alpha-helical and beta-sheet forming peptides.

A condensation-ordering mechanism in nanoparticle-catalyzed peptide aggregation.

Nucleation of amyloid fibrils.

Atomistic theory of amyloid fibril nucleation.

Efficient high-quality volume rendering of SPH data.

Impacts of multiple stressors on freshwater biota across spatial scales and ecosystems.

A generic mechanism of emergence of amyloid protofilaments from disordered oligomeric aggregates.

Simple Model of the Effect of Solution Conditions on the Nucleation of Amyloid Fibrils.

Effects of river bank heterogeneity and time of day on drift and stranding of juvenile European grayling (Thymallus thymallus L.) caused by hydropeaking.

Amyloid fibril nucleation: effect of amino acid hydrophobicity.

Tracking polypeptide folds on the free energy surface: effects of the chain length and sequence.