Gal Bitan

Building Units for N-Backbone Cyclic Peptides. 3. Synthesis of Protected N(alpha)-(omega-Aminoalkyl)amino Acids and N(alpha)-(omega-Carboxyalkyl)amino Acids.

Paradigm shifts in Alzheimer's disease and other neurodegenerative disorders: the emerging role of oligomeric assemblies.

Polyglutamine repeat length-dependent proteolysis of huntingtin.

Amyloid beta -protein (Abeta) assembly: Abeta 40 and Abeta 42 oligomerize through distinct pathways.

Elucidation of primary structure elements controlling early amyloid beta-protein oligomerization.

Increased T cell reactivity to amyloid beta protein in older humans and patients with Alzheimer disease.

A molecular switch in amyloid assembly: Met35 and amyloid beta-protein oligomerization.

Rapid photochemical cross-linking--a new tool for studies of metastable, amyloidogenic protein assemblies.

Amyloid beta-protein: monomer structure and early aggregation states of Abeta42 and its Pro19 alloform.

Preparation of aggregate-free, low molecular weight amyloid-beta for assembly and toxicity assays.

Determination of Peptide oligomerization state using rapid photochemical crosslinking.

Neurotoxic protein oligomers--what you see is not always what you get.

En route to early diagnosis of Alzheimer's disease--are we there yet?

Amyloid beta-protein monomer structure: a computational and experimental study.

Dendrimeric Abeta1-15 is an effective immunogen in wildtype and APP-tg mice.

Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach.

Early diagnostics and therapeutics for Alzheimer's disease--how early can we get there?

Structural study of metastable amyloidogenic protein oligomers by photo-induced cross-linking of unmodified proteins.

C-terminal peptides coassemble into Abeta42 oligomers and protect neurons against Abeta42-induced neurotoxicity.

The structure of Abeta42 C-terminal fragments probed by a combined experimental and theoretical study.

Amino acid position-specific contributions to amyloid beta-protein oligomerization.

RNA aptamers generated against oligomeric Abeta40 recognize common amyloid aptatopes with low specificity but high sensitivity.

Biophysical characterization of Abeta42 C-terminal fragments: inhibitors of Abeta42 neurotoxicity.

Despite its role in assembly, methionine 35 is not necessary for amyloid beta-protein toxicity.

Mechanistic investigation of the inhibition of Abeta42 assembly and neurotoxicity by Abeta42 C-terminal fragments.

Amyloid-β protein oligomerization and the importance of tetramers and dodecamers in the aetiology of Alzheimer's disease.

Surprising toxicity and assembly behaviour of amyloid β-protein oxidized to sulfone.

Rational design of β-sheet ligands against Aβ42-induced toxicity.

Lysine-specific molecular tweezers are broad-spectrum inhibitors of assembly and toxicity of amyloid proteins.

Induction of methionine-sulfoxide reductases protects neurons from amyloid β-protein insults in vitro and in vivo.

C-terminal tetrapeptides inhibit Aβ42-induced neurotoxicity primarily through specific interaction at the N-terminus of Aβ42.

Aβ(39-42) modulates aβ oligomerization but not fibril formation.

A Two-Step Strategy for Structure-Activity Relationship Studies of N-Methylated Aβ42 C-Terminal Fragments as Aβ42 Toxicity Inhibitors.

Modulating Self-Assembly of Amyloidogenic Proteins as a Therapeutic Approach for Neurodegenerative Diseases: Strategies and Mechanisms.