Michael R. Sierks

Degradation of beta-amyloid by proteolytic antibody light chains.

Residues 17-20 and 30-35 of beta-amyloid play critical roles in aggregation.

Inhibiting aggregation of alpha-synuclein with human single chain antibody fragments.

Single chain variable fragments against beta-amyloid (Abeta) can inhibit Abeta aggregation and prevent abeta-induced neurotoxicity.

Proteolytic antibody light chains alter beta-amyloid aggregation and prevent cytotoxicity.

A human single-chain Fv intrabody blocks aberrant cellular effects of overexpressed alpha-synuclein.

Trehalose differentially inhibits aggregation and neurotoxicity of beta-amyloid 40 and 42.

Quantification of cytokines involved in wound healing using surface plasmon resonance.

Identification and repair of positive binding antibodies containing randomly generated amber codons from synthetic phage display libraries.

Single chain Fv antibodies against the 25-35 Abeta fragment inhibit aggregation and toxicity of Abeta42.

Isolating recombinant antibodies against specific protein morphologies using atomic force microscopy and phage display technologies.

Insights into the mechanisms of action of anti-Abeta antibodies in Alzheimer's disease mouse models.

Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity.

Single-molecule selection and recovery of structure-specific antibodies using atomic force microscopy.

Characterization of an antibody scFv that recognizes fibrillar insulin and beta-amyloid using atomic force microscopy.

Anti-oligomeric single chain variable domain antibody differentially affects huntingtin and alpha-synuclein aggregates.

Anti-oligomeric Abeta single-chain variable domain antibody blocks Abeta-induced toxicity against human neuroblastoma cells.

Characterizing antibody specificity to different protein morphologies by AFM.

Detecting morphologically distinct oligomeric forms of alpha-synuclein.

Intracellular targeting and clearance of oligomeric alpha-synuclein alleviates toxicity in mammalian cells.

Conformational targeting of fibrillar polyglutamine proteins in live cells escalates aggregation and cytotoxicity.

Cyclodextrins promote protein aggregation posing risks for therapeutic applications.

Antifibrillizing agents catalyze the formation of unstable intermediate aggregates of beta-amyloid.

Physico-chemical determinants of soluble intrabody expression in mammalian cell cytoplasm.

Engineered proteolytic nanobodies reduce Abeta burden and ameliorate Abeta-induced cytotoxicity.

Curcumin reduces alpha-synuclein induced cytotoxicity in Parkinson's disease cell model.

Nanobody specific for oligomeric β-amyloid stabilizes nontoxic form.

Inhibiting β-secretase activity in Alzheimer's disease cell models with single-chain antibodies specifically targeting APP.

CSF levels of oligomeric alpha-synuclein and beta-amyloid as biomarkers for neurodegenerative disease.

Bispecific tandem single chain antibody simultaneously inhibits β-secretase and promotes α-secretase processing of AβPP.

Isolation and characterization of antibody fragments selective for specific protein morphologies from nanogram antigen samples.

Human α4β2 nicotinic acetylcholine receptor as a novel target of oligomeric α-synuclein.

A Sensitive phage-based capture ELISA for sub-femtomolar detection of protein variants directly from biological samples.

Isolation and characterization of antibody fragments selective for toxic oligomeric tau.