Unknown

Dataset Information

0

A novel HDAC inhibitor with a hydroxy-pyrimidine scaffold.


ABSTRACT: Histone deacetylases (HDACs) are enzymes involved in many important biological functions. They have been linked to a variety of cancers, psychiatric disorders, and other diseases. Since small molecules can serve as probes to study the relevant biological roles of HDACs, novel scaffolds are necessary to develop more efficient, selective drug candidates. Screening libraries of molecules may yield structurally diverse probes that bind these enzymes and modulate their functions in cells. Here we report a small molecule with a novel hydroxy-pyrimidine scaffold that inhibits multiple HDAC enzymes and modulates acetylation levels in cells. Analogs were synthesized in an effort to evaluate structure-activity relationships.

SUBMITTER: Kemp MM 

PROVIDER: S-EPMC3248787 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

A novel HDAC inhibitor with a hydroxy-pyrimidine scaffold.

Kemp Melissa M MM   Wang Qiu Q   Fuller Jason H JH   West Nathan N   Martinez Nicole M NM   Morse Elizabeth M EM   Weïwer Michel M   Schreiber Stuart L SL   Bradner James E JE   Koehler Angela N AN  

Bioorganic & medicinal chemistry letters 20110602 14


Histone deacetylases (HDACs) are enzymes involved in many important biological functions. They have been linked to a variety of cancers, psychiatric disorders, and other diseases. Since small molecules can serve as probes to study the relevant biological roles of HDACs, novel scaffolds are necessary to develop more efficient, selective drug candidates. Screening libraries of molecules may yield structurally diverse probes that bind these enzymes and modulate their functions in cells. Here we rep  ...[more]

Similar Datasets

| S-EPMC9296983 | biostudies-literature
| S-EPMC5820112 | biostudies-literature
| S-EPMC2957683 | biostudies-literature
| S-EPMC7520432 | biostudies-literature
| S-EPMC10250299 | biostudies-literature
| S-EPMC5101637 | biostudies-literature
2020-04-17 | GSE136039 | GEO
| S-EPMC10075517 | biostudies-literature
| S-EPMC5278546 | biostudies-literature
| S-EPMC7894020 | biostudies-literature