The Structure of Amyloid Versus the Structure of Globular Proteins

Alternative Structures of α-Synuclein

(2020) Dawid Dułak et al.   MOLECULES

Alternative Hydrophobic Core in Proteins—The Effect of Specific Synergy

(2020) Piotr Fabian et al.   Symmetry-Basel

Cryo-EM structure of cardiac amyloid fibrils from an immunoglobulin light chain AL amyloidosis patient

(2019) Paolo Swuec et al.   Nature Communications

Structural analysis of the Aβ(11–42) amyloid fibril based on hydrophobicity distribution

(2019) Irena Roterman et al.   JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN

The Amyloid as a Ribbon-Like Micelle in Contrast to Spherical Micelles Represented by Globular Proteins

(2019) Mateusz Banach et al.   MOLECULES

Model of Early Stage Intermediate in Respect to Its Final Structure

(2019) Piotr Fabian et al.   Biomolecules

Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model

(2018) Dawid Dułak et al.   INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES

Is the hydrophobic core a universal structural element in proteins?

(2017) Barbara Kalinowska et al.   JOURNAL OF MOLECULAR MODELING

Cryo-EM structures of tau filaments from Alzheimer’s disease

(2017) Anthony W. P. Fitzpatrick et al.   NATURE

Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils

(2016) Michael T. Colvin et al.   JOURNAL OF THE AMERICAN CHEMICAL SOCIETY

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

(2016) Marcus D Tuttle et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Application of Divergence Entropy to Characterize the Structure of the Hydrophobic Core in DNA Interacting Proteins

(2015) Barbara Kalinowska et al.   Entropy

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

(2015) Yiling Xiao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Modeling an In-Register, Parallel “Iowa” Aβ Fibril Structure Using Solid-State NMR Data from Labeled Samples with Rosetta

(2015) Nikolaos G. Sgourakis et al.   STRUCTURE

Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease

(2015) Yiling Xiao et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation

(2014) Anne K. Schütz et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Edge strand engineering prevents native-like aggregation inSulfolobus solfataricusacylphosphatase

(2014) Matteo de Rosa et al.   FEBS Journal

Polypeptide chain collapse and protein folding

(2012) Jayant B. Udgaonkar   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

Protein Misfolded Oligomers: Experimental Approaches, Mechanism of Formation, and Structure-Toxicity Relationships

(2012) Francesco Bemporad et al.   CHEMISTRY & BIOLOGY

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

(2011) A. De Simone et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA

Is Alzheimer's Disease a Result of Presynaptic Failure? - Synaptic Dysfunctions Induced by Oligomeric β-Amyloid

(2011) Volker Nimmrich et al.   REVIEWS IN THE NEUROSCIENCES

Understanding protein non-folding

(2010) Vladimir N. Uversky et al.   BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS

Amyloidogenic determinants are usually not buried

(2009) Kimon K Frousios et al.   BMC STRUCTURAL BIOLOGY