Boston University

Dana-farber-cancer Institute Inc.

Universita Di Perugia

Aaron Beaty Beeler

John A Porco, Jr

Oscar Ingham

James Elliott Bradner

Lauren E Brown

Emiliano Biasini

Nunzio Iraci

David A Harris

Ichun Anderson Chen

Brian R Fluharty

Nathaniel Ryan Hendrick

Jason Michael Lenihan

Richard V Trilles

Maria Letizia Barreca

Andrew Emili

The disclosure provides probes comprising dipyrromethane-BFderivatives which exhibits different fluorescent spectral properties when conjugated to the amino acids, compositions and kits comprising same. The disclosure also provides methods for detecting/identifying amino acids and sequencing polypeptide molecules by conjugating a dipyrromethane-BF2 derivative which exhibits different fluorescent spectral properties when conjugated to the amino acids.

BODIPY-based dyes for digital spatial proteomics

Herein are described apparatus and processes for the preparation of cannabinoids, such as cannabidiol (CBD) and derivatives thereof. The apparatus and processes described can be used for the one-step, flow-mediated synthesis of cannabidiol and derivatives with improved overall yield, material throughput, and product purity relative to batch processes.

One-step flow-mediated synthesis of cannabidiol (CBD) and derivatives

The invention provides compositions and methods for treatment of neurodegenerative diseases or disorders, particularly neurodegenerative diseases and disorders associated with protein aggregation. The present invention is based on the discovery of binding regions on the surface of PrPc, referred to as PrPc Binding Domains (PBD). In particular, the inventors have identified six different binding regions on PrPc, referred to herein as PrP-binding domain-1 (PBD-1), PrP-binding domain-2 (PBD-2), PrP-binding domain-3 (PBD-3), PrP-binding domain-4 (PBD-4), PrP-binding domain-5 (PBD-5), and PrP-binding domain-6 (PBD-6), herein. The PBD-1 to PBD-6 are each defined by a cluster of amino acids located in the globular domain of the protein, e.g., in the C-terminal half of the protein (i.e., in residues 120-230). One embodiment uses residues 127-226.

Prion protein ligands as therapeutic agents for neurodegenerative disorders

Described herein are compounds and pharmaceutical compositions containing such compounds, which inhibit the activity of histone deacetylase 8 (HDAC8). Also described herein are methods of using such HDAC8 inhibitors, alone and in combination with other compounds, for treating diseases or conditions that benefit from inhibition of HDAC8 activity.

Selective histone deacetylase 8 inhibitors

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Cambridge, MA, United States of America

Aaron Beaty Beeler