Broad spectrum antiprotozoal agents that inhibit histone deacetylase: structure–activity relationships of apicidin. Part 1-Reference-Cited by-同舟云学术

Broad spectrum antiprotozoal agents that inhibit histone deacetylase: structure–activity relationships of apicidin. Part 1

Published:2001-01 Issue:2 Volume:11 Page:107-111
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Colletti Steven L,Myers Robert W,Darkin-Rattray Sandra J,Gurnett Anne M,Dulski Paula M,Galuska Stefan,Allocco John J,Ayer Michelle B,Li Chunshi,Lim Julie,Crumley Tami M,Cannova Christine,Schmatz Dennis M,Wyvratt Matthew J,Fisher Michael H,Meinke Peter T

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference26 articles.

1. Apicidins: Novel cyclic tetrapeptides as coccidiostats and antimalarial agents from Fusarium pallidoroseum

2. Structures of a histone deacetylase homologue bound to the TSA and SAHA inhibitors

3. Review: Meinke, P. T.; Liberator, P. Curr. Med. Chem. 2000, in press.

4. Review: Strahl, B. D.; Allis, C. D. Nature 2000, 403, 41.

5. HDA1 and RPD3 are members of distinct yeast histone deacetylase complexes that regulate silencing and transcription

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