The Structural Combination of SIL and MODAG Scaffolds Fails to Enhance Binding to α-Synuclein but Re...
The Structural Combination of SIL and MODAG Scaffolds Fails to Enhance Binding to α-Synuclein but Reveals Promising Affinity to Amyloid β
About this item
Full title
Author / Creator
Publisher
Switzerland: MDPI AG
Journal title
Language
English
Formats
Publication information
Publisher
Switzerland: MDPI AG
Subjects
More information
Scope and Contents
Contents
A technique to image α-synuclein (αSYN) fibrils in vivo is an unmet scientific and clinical need that would represent a transformative tool in the understanding, diagnosis, and treatment of various neurodegenerative diseases. Several classes of compounds have shown promising results as potential PET tracers, but no candidate has yet exhibited the a...
Alternative Titles
Full title
The Structural Combination of SIL and MODAG Scaffolds Fails to Enhance Binding to α-Synuclein but Reveals Promising Affinity to Amyloid β
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_576ea8a4e6754caea2b9a7ee3231ccb0
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_576ea8a4e6754caea2b9a7ee3231ccb0
Other Identifiers
ISSN
1420-3049
E-ISSN
1420-3049
DOI
10.3390/molecules28104001