Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Inhibiting Aggregation of α-Synuclein with Human Single Chain Antibody Fragments

20 Feb 2004

Abstract excerpt

The alpha-synuclein protein has been strongly correlated with Parkinson's disease (PD) and is a major component of the hallmark Lewy body aggregates associated with PD. Two different mutations in the alpha-synuclein gene as well as increased gene dosage of wild-type alpha-synuclein all associate with early onset cases of PD; and transgenic animal models overexpressing alpha-synuclein develop PD symptoms....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cellular transport and secretion
Share to Neurological disorders and treatments
Share to Parkinson's Disease Mechanisms and Treatments

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 15005622
DOI: 10.1021/bi036281f

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Inhibiting Aggregation of α-Synuclein with Human Single Chain Antibody FragmentsPMID 15005622Read ↗

Detecting Morphologically Distinct Oligomeric Forms of α-SynucleinSemantic proximity Read ↗

Virally encoded single-chain antibody fragments targeting alpha-synuclein protect against motor impairments and neuropathology in a mouse model of synucleinopathySemantic proximity Read ↗

Monoclonal antibodies targeting cytotoxic α-synuclein oligomers: molecular properties and diagnostic potentialSemantic proximity Read ↗

Molecular properties and diagnostic potential of monoclonal antibodies targeting cytotoxic α-synuclein oligomersSemantic proximity Read ↗

Targeted degradation of α-synuclein prevents PFF-induced aggregationSemantic proximity Read ↗

Novel engineered nanobodies specific for N‐terminal region of alpha‐synuclein recognize Lewy‐body pathology and inhibit <i>in‐vitro</i> seeded aggregation and toxicitySemantic proximity Read ↗

Inhibition of α-Synuclein Seeding-Dependent Aggregation by ssDNA Aptamers Specific to C-Terminally Truncated α-Synuclein FibrilsSemantic proximity Read ↗

Expression, purification and characterization of α-synuclein fibrillar specific scFv from inclusion bodiesSemantic proximity Read ↗

Modulating the Amyloidogenesis of α-Synuclein.Semantic proximity Read ↗

An scFv Intrabody against the Nonamyloid Component of α-Synuclein Reduces Intracellular Aggregation and ToxicitySemantic proximity Read ↗

Foldamers Reveal and Validate Novel Therapeutic Targets Associated with Toxic α-Synuclein Self-AssemblySemantic proximity Read ↗

The good and bad of therapeutic strategies that directly target α‐synucleinSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.