The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides
Published 2017 View Full Article
- Home
- Publications
- Publication Search
- Publication Details
Title
The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides
Authors
Keywords
-
Journal
Interface Focus
Volume 7, Issue 6, Pages 20170027
Publisher
The Royal Society
Online
2017-10-20
DOI
10.1098/rsfs.2017.0027
References
Ask authors/readers for more resources
Related references
Note: Only part of the references are listed.- Cryo-EM structures of tau filaments from Alzheimer’s disease
- (2017) Anthony W. P. Fitzpatrick et al. NATURE
- Modification of β-Sheet Forming Peptide Hydrophobic Face: Effect on Self-Assembly and Gelation
- (2016) Mohamed A. Elsawy et al. LANGMUIR
- A modular self-assembly approach to functionalised β-sheet peptide hydrogel biomaterials
- (2016) Patrick J. S. King et al. Soft Matter
- Implantable amyloid hydrogels for promoting stem cell differentiation to neurons
- (2016) Subhadeep Das et al. NPG Asia Materials
- A critical role for the self-assembly of Amyloid-β1-42 in neurodegeneration
- (2016) Karen E. Marshall et al. Scientific Reports
- Chemically and thermally stable silica nanowires with a β-sheet peptide core for bionanotechnology
- (2016) Zahraa S. Al-Garawi et al. JOURNAL OF NANOBIOTECHNOLOGY
- Silica Nanowires Templated by Amyloid-like Fibrils
- (2015) Zahraa S. Al-Garawi et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Biomimetic Topography and Chemistry Control Cell Attachment to Amyloid Fibrils
- (2015) Nicholas P. Reynolds et al. BIOMACROMOLECULES
- Self healing hydrogels composed of amyloid nano fibrils for cell culture and stem cell differentiation
- (2015) Reeba S. Jacob et al. BIOMATERIALS
- Enhancement and Induction of HIV-1 Infection through an Assembled Peptide Derived from the CD4 Binding Site of gp120
- (2015) Andrea Groß et al. CHEMBIOCHEM
- X-ray Crystallographic Structures of Oligomers of Peptides Derived from β2-Microglobulin
- (2015) Ryan K. Spencer et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Structural basis for amyloidogenic peptide recognition by sorLA
- (2015) Yu Kitago et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- Beta-Sheet-Forming, Self-Assembled Peptide Nanomaterials towards Optical, Energy, and Healthcare Applications
- (2015) Sungjin Kim et al. Small
- Structural basis for amyloidogenic peptide recognition by sorLA
- (2015) Yu Kitago et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy
- (2015) Annette E. Langkilde et al. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
- Self-Assembly of a Model Peptide Incorporating a Hexa-Histidine Sequence Attached to an Oligo-Alanine Sequence, and Binding to Gold NTA/Nickel Nanoparticles
- (2014) Ian W. Hamley et al. BIOMACROMOLECULES
- Silica templating of a self-assembling peptide amphiphile that forms nanotapes
- (2014) Ashkan Dehsorkhi et al. Soft Matter
- Self-Assembly in Biosilicification and Biotemplated Silica Materials
- (2014) Francisco Fernandes et al. Nanomaterials
- The Structure of Cross-β Tapes and Tubes Formed by an Octapeptide, αSβ1
- (2013) Kyle L. Morris et al. ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- Exploring the sequence–structure relationship for amyloid peptides
- (2013) Kyle L. Morris et al. BIOCHEMICAL JOURNAL
- A central role for dityrosine crosslinking of Amyloid-β in Alzheimer’s disease
- (2013) Youssra K Al-Hilaly et al. Acta Neuropathologica Communications
- Role of Aromatic Side Chains in Amyloid β-Protein Aggregation
- (2012) Risto Cukalevski et al. ACS Chemical Neuroscience
- Amyloid Directed Synthesis of Titanium Dioxide Nanowires and Their Applications in Hybrid Photovoltaic Devices
- (2012) Sreenath Bolisetty et al. ADVANCED FUNCTIONAL MATERIALS
- Hydrophobic, Aromatic, and Electrostatic Interactions Play a Central Role in Amyloid Fibril Formation and Stability
- (2011) Karen E. Marshall et al. BIOCHEMISTRY
- Functional fibrils derived from the peptide TTR1-cycloRGDfK that target cell adhesion and spreading
- (2011) Marie N. Bongiovanni et al. BIOMATERIALS
- Protein aggregation and amyloid fibril formation prediction software from primary sequence: towards controlling the formation of bacterial inclusion bodies
- (2011) Stavros J. Hamodrakas FEBS Journal
- Molecular basis for amyloid- polymorphism
- (2011) J.-P. Colletier et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Characterizing the Assembly of the Sup35 Yeast Prion Fragment, GNNQQNY: Structural Changes Accompany a Fiber-to-Crystal Switch
- (2010) Karen E. Marshall et al. BIOPHYSICAL JOURNAL
- Exploring the sequence determinants of amyloid structure using position-specific scoring matrices
- (2010) Sebastian Maurer-Stroh et al. NATURE METHODS
- Tuning the pH Responsiveness of β-Hairpin Peptide Folding, Self-Assembly, and Hydrogel Material Formation
- (2009) Karthikan Rajagopal et al. BIOMACROMOLECULES
- Self-Assembly of Phenylalanine Oligopeptides: Insights from Experiments and Simulations
- (2009) Phanourios Tamamis et al. BIOPHYSICAL JOURNAL
- Engineered disulfides improve mechanical properties of recombinant spider silk
- (2009) S. Grip et al. PROTEIN SCIENCE
- Self-Assembly and Hydrogelation of an Amyloid Peptide Fragment
- (2008) Marta J. Krysmann et al. BIOCHEMISTRY
- Facial Symmetry in Protein Self-Assembly
- (2008) Anil K. Mehta et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Templating Silica Nanostructures on Rationally Designed Self-Assembled Peptide Fibers
- (2008) Stewart C. Holmström et al. LANGMUIR
- Amyloid as a Depot for the Formulation of Long-Acting Drugs
- (2008) Samir K Maji et al. PLOS BIOLOGY
- Structural analysis of hydrophobins
- (2007) Margaret Sunde et al. MICRON
Find Funding. Review Successful Grants.
Explore over 25,000 new funding opportunities and over 6,000,000 successful grants.
ExplorePublish scientific posters with Peeref
Peeref publishes scientific posters from all research disciplines. Our Diamond Open Access policy means free access to content and no publication fees for authors.
Learn More