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Person
ISNI: 
0000 0000 5489 9526
Name: 
Ehud Gazit
Ehud Gazit (biologo israeliano)
Ehud Gazit (bioloog uit Israël)
Ehud Gazit (Israeli biochemist)
Gazit, E.
Gazit, Ehud
Gaziyt, ʾEhwd
Эхуд Газит
אהוד גזית
גזית, אהוד
Dates: 
1967-...
Creation class: 
article
Computer file
Language material
Text
txt
Creation role: 
author
editor
Related names: 
Mitraki, Anna
Nussinov, Ruth
Ûnîversîṭā (Tēl-Āvîv) Affiliation (see also from)
Titles: 
Alignment of Aromatic Peptide Tubes in Strong Magnetic Fields
Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity.
alpha-5 segment of Bacillus thuringiensis delta-endotoxin: in vitro activity, ion channel formation and molecular modelling., The
Amyloid fibril formation by pentapeptide and tetrapeptide fragments of human calcitonin.
Amyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragments
Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials
assembly and organization of the alpha 5 and alpha 7 helices from the pore-forming domain of Bacillus thuringiensis delta-endotoxin. Relevance to a functional model., The
Bacillus thuringiensis cytolytic toxin associates specifically with its synthetic helices A and C in the membrane bound state. Implications for the assembly of oligomeric transmembrane pores
Bioinspired design of nanocages by self-assembling triskelion peptide elements.
Bioinspired peptide nanotubes: Deposition technology and physical properties
Biological and Chemical Decoration of Peptide Nanostructures via Biotin-Avidin Interactions
Blue luminescence based on quantum confinement at peptide nanotubes.
Casting metal nanowires within discrete self-assembled peptide nanotubes
Cognitive-performance recovery of Alzheimer's disease model mice by modulation of early soluble amyloidal assemblies.
Complete Phenotypic Recovery of an Alzheimer's Disease Model by a Quinone-Tryptophan Hybrid Aggregation Inhibitor
Completely different amyloidogenic potential of nearly identical peptide fragments.
Controlled assembly of peptide nanotubes triggered by enzymatic activation of self-immolative dendrimers.
Controlled patterning of aligned self-assembled peptide nanotubes.
Controlled patterning of peptide nanotubes and nanospheres using inkjet printing technology.
"Correctly Folded" state of proteins: is it a metastable state?, The
Correctly Folded State of Proteins, The : Is It a Metastable State?
Creating Prebiotic Sanctuary: Self-Assembling Supramolecular Peptide Structures Bind and Stabilize RNA
Crystallization of Doc and the Phd-Doc toxin-antitoxin complex
Design of metal-binding sites onto self-assembled peptide fibrils
Designed aromatic homo-dipeptides: formation of ordered nanostructures and potential nanotechnological applications.
Direct observation of the release of phenylalanine from diphenylalanine nanotubes.
Doc Toxin and Phd Antidote Proteins of the Bacteriophage P1 Plasmid Addiction System Form a Heterotrimeric Complex, The
early stages of amyloid formation: Biophysical and structural characterization of human calcitonin pre-fibrillar assemblies, The
Elementary building blocks of self-assembled peptide nanotubes.
Energy landscape of amyloidogenic peptide oligomerization by parallel-tempering molecular dynamics simulation: significant role of Asn ladder.
Exploring the self-assembly of glycopeptides using a diphenylalanine scaffold.
Formation of Escherichia coli Curli Amyloid Fibrils is Mediated by Prion-like Peptide Repeats, The
Formation of Well-Organized Self-Assembled Films from Peptide Nanotubes
From green bacteria to human dementia: a novel model for discovering amyloid assembly inhibitors.
Genetic Engineering of Biomolecular Scaffolds for the Fabrication of Organic and Metallic Nanowires
Global analysis of tandem aromatic octapeptide repeats : The significance of the aromatic-glycine motif
Green tea extracts interfere with the stress-protective activity of PrPC and the formation of PrPSc
human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies., The
Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide.
In vivo aggregation of a single enzyme limits growth of Escherichia coli at elevated temperatures.
Inhibition of amyloid fibril formation by peptide analogues modified with alpha-aminoisobutyric acid.
Inhibition of amyloid fibril formation by polyphenols: structural similarity and aromatic interactions as a common inhibition mechanism.
Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions.
Integrating peptide nanotubes in micro-fabrication processes
Interaction of the mammalian antibacterial peptide cecropin P1 with phospholipid vesicles
Mechanically functional amyloid fibrils in the adhesive of a marine invertebrate as revealed by Raman spectroscopy and atomic force microscopy.
Mechanisms of amyloid fibril self-assembly and inhibition. Model short peptides as a key research tool.
Mechanistic studies of the process of amyloid fibrils formation by the use of peptide fragments and analogues: implications for the design of fibrillization inhibitors.
minimal amyloid-forming fragment of the islet amyloid polypeptide is a glycolipid-binding domain, The
MINIREVIEW
Mode of action of the antibacterial cecropin B2: A spectrofluorometric study
model for the role of short self-assembled peptides in the very early stages of the origin of life., A
molecular dynamics of assembly of the ubiquitous aortic medial amyloidal medin fragment, The
Molecular dynamics simulation of the aggregation of the core-recognition motif of the islet amyloid polypeptide in explicit water
Molecular mapping of the recognition interface between the islet amyloid polypeptide and insulin.
molecular mechanisms of the anti-amyloid effects of phenols, The
Molecular self-assembly: bioactive nanostructures branch out.
Molecular Self-Assembly of Peptide Nanostructures: Mechanism of Association and Potential Uses
Nanostructure design: methods and protocols. Preface.
Novel electrochemical biosensing platform using self-assembled peptide nanotubes.
Orally administrated cinnamon extract reduces β-amyloid oligomerization and corrects cognitive impairment in Alzheimer's disease animal models.
Patterned Arrays of Ordered Peptide Nanostructures
Peptide Nanotube-Modified Electrodes for Enzyme-Biosensor Applications
Peptide self-assembly at the nanoscale: a challenging target for computational and experimental biotechnology.
Peptide sequence and amyloid formation; molecular simulations and experimental study of a human islet amyloid polypeptide fragment and its analogs.
Phenolsulfonphthalein, but Not Phenolphthalein, Inhibits Amyloid Fibril Formation: Implications for the Modulation of Amyloid Self-Assembly
Plenty of room for biology at the bottom : an introduction to bionanotechnology
Polyphenol-induced dissociation of various amyloid fibrils results in a methionine-independent formation of ROS
possible role for pi-stacking in the self-assembly of amyloid fibrils., A
preferred conformation of the tripeptide Ala-Phe-Ala in water is an inverse gamma-turn: implications for protein folding and drug design., The
Quantitative structure-activity relationship analysis of beta -amyloid aggregation inhibitors
Quantum confinement in self-assembled bioinspired peptide hydrogels.
Review: Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism
Rigid, Self-Assembled Hydrogel Composed of a Modified Aromatic Dipeptide
Role of Bacillus thuringiensis Cry1C and Cry1E Separate Structural Domains in the Interaction with Spodoptera littoralis Gut Epithelial Cells, The
role of the 14-20 domain of the islet amyloid polypeptide in amyloid formation., The
Self-assembled arrays of peptide nanotubes by vapour deposition.
Self-assembled Fmoc-peptides as a platform for the formation of nanostructures and hydrogels.
Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization.
Self-assembled peptide nanotubes are uniquely rigid bioinspired supramolecular structures.
Self-assembly of phenylalanine oligopeptides: insights from experiments and simulations.
Self assembly of short aromatic peptides into amyloid fibrils and related nanostructures.
Stability and DNA Binding of the Phd Protein of the Phage P1 Plasmid Addiction System
Strong piezoelectricity in bioinspired peptide nanotubes.
Structural and functional characterization of the alpha 5 segment of Bacillus thuringiensis delta -endotoxin.
Structural and Thermodynamic Characterization of the Escherichia coli RelBE Toxin-Antitoxin System: Indication for a Functional Role of Differential Stability
structural basis of amyloid formation., The
Structural characterization, membrane interaction, and specific assembly within phospholipid membranes of hydrophobic segments from Bacillus thuringiensis var. israelensis cytolytic toxin.
Structural transition in peptide nanotubes.
Structure and orientation of the mammalian antibacterial peptide cecropin P1 within phospholipid membranes
Targeting insulin amyloid assembly by small aromatic molecules: toward rational design of aggregation inhibitors.
Thermal and chemical stability of diphenylalanine peptide nanotubes: implications for nanotechnological applications.
Use of biomolecular templates for the fabrication of metal nanowires:
von Hippel-Lindau tumor suppressor protein is a molten globule under native conditions: implications for its physiological activities., The
YefM antitoxin defines a family of natively unfolded proteins: implications as a novel antibacterial target., The
yefM-yoeB Toxin-Antitoxin Systems of Escherichia coli and Streptococcus pneumoniae: Functional and Structural Correlation, The
YoeB toxin is a folded protein that forms a physical complex with the unfolded YefM antitoxin. Implications for a structural-based differential stability of toxin-antitoxin systems., The
Contributed to or performed: 
ANGEWANDTE CHEMIE -INTERNATIONAL EDITION IN ENGLISH-
BIOCHEMISTRY -PENNSYLVANIA THEN WASHINGTON-
BIOINFORMATICS -OXFORD-
CHEMICAL SOCIETY REVIEWS
CURRENT MEDICINAL CHEMISTRY
FASEB JOURNAL
FEBS JOURNAL
NATURE NANOTECHNOLOGY
PRION
Notes: 
Sources: 
BOWKER
NTA
ZETO