X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
biochemistry & molecular biology (43) 43
index medicus (42) 42
amyloid - chemistry (35) 35
humans (30) 30
protein structure, secondary (29) 29
cross-β structure (27) 27
proteins (27) 27
models, molecular (25) 25
amyloid (24) 24
aggregation (22) 22
cross-β (22) 22
amyloid fibrils (21) 21
animals (18) 18
cross-beta structure (18) 18
protein (17) 17
amino acid sequence (15) 15
biophysics (15) 15
peptides (15) 15
fibrils (13) 13
protein aggregation (13) 13
alzheimers-disease (12) 12
amyloid - ultrastructure (12) 12
cross-beta (12) 12
in-vitro (12) 12
protein folding (12) 12
solid-state nmr (12) 12
amyloid - metabolism (11) 11
cell biology (11) 11
molecular sequence data (11) 11
x-ray diffraction (11) 11
peptide (10) 10
peptide fragments - chemistry (10) 10
protein conformation (10) 10
secondary structure (10) 10
alpha-synuclein (9) 9
amyloid fibril (9) 9
circular dichroism (8) 8
electron microscopy (8) 8
fibril formation (8) 8
oligomer (8) 8
oligomers (8) 8
peptides - chemistry (8) 8
prion (8) 8
protein binding (8) 8
x-ray-diffraction (8) 8
article (7) 7
biological sciences (7) 7
chemistry, multidisciplinary (7) 7
cross‐β structure (7) 7
electron-microscopy (7) 7
fibril (7) 7
model (7) 7
molecular dynamics simulation (7) 7
protein misfolding (7) 7
biology (6) 6
diffraction (6) 6
mice (6) 6
multidisciplinary sciences (6) 6
prion protein (6) 6
review (6) 6
self-assembly (6) 6
sequence (6) 6
stability (6) 6
structure (6) 6
alzheimer's disease (5) 5
amyloid - genetics (5) 5
atomic force microscopy (5) 5
biochemistry, general (5) 5
core structure (5) 5
cross-β-sheet (5) 5
cross-β-structure (5) 5
crystal-structure (5) 5
hydrogen bonding (5) 5
macromolecular substances (5) 5
models, biological (5) 5
mutation (5) 5
protofilament (5) 5
steric zipper (5) 5
β-sheet (5) 5
amyloid beta-peptides - chemistry (4) 4
amyloidosis - metabolism (4) 4
analysis (4) 4
beta-sheet (4) 4
binding sites (4) 4
biochemistry (4) 4
biomaterials (4) 4
biomedicine general (4) 4
circular-dichroism (4) 4
conformations (4) 4
congo red (4) 4
cross-beta-sheet (4) 4
cryoelectron microscopy (4) 4
crystallography, x-ray (4) 4
fibers (4) 4
fibrille (4) 4
fibrillogenesis (4) 4
glycoproteins (4) 4
inclusion bodies (4) 4
kinetics (4) 4
mechanism (4) 4
more...
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Biomaterials, ISSN 0142-9612, 2014, Volume 35, Issue 19, pp. 5196 - 5205
EAK16-II (AEAEAKAKAEAEAKAK) is one of the first building blocks of environmentally responsive materials. This self-assembling peptide undergoes solution-to-gel... 
Self-assembly | Amphiphilic peptides | Protein formulation | Cross-β fibrils | EAK16
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 09/2019, Volume 116, Issue 36, pp. 17963 - 17969
Many neurodegenerative diseases are characterized by the accumulation of abnormal protein aggregates in the brain. In Parkinson’s disease (PD), α-synuclein... 
cross-β structure | X-ray diffraction | Biological Sciences | Parkinson’s disease | Lewy body
Journal Article
Angewandte Chemie (International Ed. in English), ISSN 1433-7851, 11/2015, Volume 54, Issue 45, pp. 13327 - 13331
Many peptides self-assemble to form amyloid fibrils. We previously explored the sequence propensity to form amyloid using variants of a designed peptide with... 
tetraethylorthosilicate | nanotubes | amyloid fibrils | silica | Communications | cross-β-structure
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 02/2017, Volume 114, Issue 7, pp. E1111 - E1117
Journal Article
Journal of Biomolecular Structure and Dynamics, ISSN 0739-1102, 05/2019, Volume 37, Issue 8, pp. 2143 - 2153
X-ray fiber diffraction experiments on Alzheimer Aβ(1-40) fibrils formed in an assembly process thought to simulate a portion of the pathophysiological process... 
β-helix | Molecular dynamics simulation | shear number | cross-β | β-barrel
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 08/2012, Volume 421, Issue 2-3, pp. 256 - 269
Mutations in the polypeptide sequence that forms the core structure of amyloid fibrils are known to impact on fibril assembly and stability but the effect of... 
cross-β core | cross-seeding | seed | fragmentation | structure
Journal Article
Biochemical Journal, ISSN 0264-6021, 11/2015, Volume 471, Issue 3, pp. 323 - 333
Parkinson's disease (PD) is an age-related movement disorder characterized by a progressive degeneration of dopaminergic neurons in the midbrain. Although the... 
Cross-β structure | Amyloid fibril | Nucleotide oligomerization domain-like receptor pyrin domain containing 3 (NLRP3) inflammasome | Oligomer | Structure-inflammatory properties relationship | α-synuclein | structure-inflammatory | AMIDE-ONE VIBRATION | ALZHEIMERS-DISEASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ANTIPARALLEL BETA-SHEET | INNATE IMMUNE-RESPONSE | oligomer | nucleotide oligomerization domain-like receptor pyrin domain containing 3 (NLRP3) inflammasome | INFRARED-SPECTROSCOPY | alpha-synuclein | properties relationship | ALPHA-SYNUCLEIN OLIGOMERS | RESONANCE INTERACTION | ACTIVATES MICROGLIA | MOUSE MODEL | cross-beta structure | amyloid fibril | NF-KAPPA-B | Tumor Necrosis Factor-alpha - metabolism | Cell Line | Inflammation - pathology | Parkinson Disease - pathology | Inflammasomes - metabolism | NLR Family, Pyrin Domain-Containing 3 Protein | Humans | Immunity, Innate - genetics | Signal Transduction - genetics | Toll-Like Receptor 2 - metabolism | Protein Aggregation, Pathological | alpha-Synuclein - chemistry | Protein Structure, Secondary - genetics | Inflammation - metabolism | Carrier Proteins - metabolism | Amyloid - metabolism | Interleukin-1beta - metabolism | Carrier Proteins - chemistry | Parkinson Disease - metabolism | Toll-Like Receptor 2 - chemistry | alpha-Synuclein - metabolism | Index Medicus
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 08/2012, Volume 421, Issue 4-5, pp. 417 - 426
Journal Article