Allosteric drugs: thinking outside the active-site box. Journal Article

Overview

abstract

• Recently, a class of small molecules that thermally stabilize the tumor suppressor p53 was selected from a small-molecule library. This, and other recent work, demonstrates the feasibility of taking a lead from nature and selecting new classes of drugs that function by allosteric mechanisms.

CU Boulder Authors

• DeDecker, Brian S

publication date

• May 1, 2000

has subject area

• Allosteric Regulation
• Binding Sites
• Biochemical Phenomena - Peptide Library
• Carrier Proteins - Nitric Oxide Synthase Type II
• Carrier Proteins - Tumor Suppressor Protein p53
• DNA-Binding Proteins - Tumor Suppressor Protein p53
• Gene Library - Peptide Library
• Humans
• Nitric Oxide Synthase
• Nitric Oxide Synthase - Nitric Oxide Synthase Type II
• Nuclear Proteins - Nitric Oxide Synthase Type II
• Nuclear Proteins - Tumor Suppressor Protein p53
• Peptides - Peptide Library
• Phosphoproteins - Tumor Suppressor Protein p53
• Protein Engineering
• Tumor Suppressor Proteins - Tumor Suppressor Protein p53

has restriction

• bronze

Date in CU Experts

• September 4, 2015 2:01 AM

Full Author List

• DeDecker BS

author count

• 1

published in

• Chemistry and Biology  Journal

Other Profiles

International Standard Serial Number (ISSN)

• 1074-5521

Digital Object Identifier (DOI)

• https://doi.org/10.1016/s1074-5521(00)00115-0

Additional Document Info

start page

• R103

end page

• R107

volume

• 7

issue

• 5