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Andrew C Braisted

Explore the profile of Andrew C Braisted including associated specialties, affiliations and a list of published articles. Areas
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Recent Articles
1.
He M, Stroustrup Smith A, Oslob J, Flanagan W, Braisted A, Whitty A, et al.
Science . 2005 Nov; 310(5750):1022-5. PMID: 16284179
We have identified a small-molecule inhibitor of tumor necrosis factor alpha (TNF-alpha) that promotes subunit disassembly of this trimeric cytokine family member. The compound inhibits TNF-alpha activity in biochemical and...
2.
Raimundo B, Oslob J, Braisted A, Hyde J, McDowell R, Randal M, et al.
J Med Chem . 2004 May; 47(12):3111-30. PMID: 15163192
Fragment assembly has shown promise for discovering small-molecule antagonists for difficult targets, including protein-protein interactions. Here, we describe a process for identifying a 60 nM inhibitor of the interleukin-2 (IL-2)/IL-2...
3.
Erlanson D, Wells J, Braisted A
Annu Rev Biophys Biomol Struct . 2004 May; 33:199-223. PMID: 15139811
The genomics revolution has provided a deluge of new targets for drug discovery. To facilitate the drug discovery process, many researchers are turning to fragment-based approaches to find lead molecules...
4.
Hyde J, Braisted A, Randal M, Arkin M
Biochemistry . 2003 May; 42(21):6475-83. PMID: 12767230
The cytokine hormone interleukin-2 (IL-2) contains a highly adaptive region that binds small, druglike molecules. The binding properties of this adaptive region have been explored using a "tethering" method that...
5.
Braisted A, Oslob J, DeLano W, Hyde J, McDowell R, Waal N, et al.
J Am Chem Soc . 2003 Mar; 125(13):3714-5. PMID: 12656598
Using a site-directed fragment discovery method called tethering, we have identified a 60 nM small molecule antagonist of a cytokine/receptor interaction (IL-2/IL2Ralpha) with cell-based activity. Starting with a low micromolar...
6.
Arkin M, Randal M, DeLano W, Hyde J, Luong T, Oslob J, et al.
Proc Natl Acad Sci U S A . 2003 Feb; 100(4):1603-8. PMID: 12582206
Understanding binding properties at protein-protein interfaces has been limited to structural and mutational analyses of natural binding partners or small peptides identified by phage display. Here, we present a high-resolution...