Bristol-myers Squibb Compnay

Roberto Weinmann

John S Tokarski

Mark E Salvati

Stanley Richard Krystek, Jr

Ricardo Attar

John S Sack

Chihuei Wang

Howard M Einspahr

Marco Gottardis

Matthew V Lorenzi

Thomas Spires

Dan You

The first crystal structure of the androgen receptor ligand binding domain has been determined to 2.0 angstrom resolution. Disclosed are the coordinates for the crystal structure, and methods for determining agonists, partial agonists, antagonists, partial antagonists and selective androgen receptors modulators (SARMs) of the androgen receptor.

Crystallographic structure of the androgen receptor ligand binding domain

Methods for determining whether a test agent inhibits a 17&#x3b2;-HSD3, the methods comprising: obtaining a recombinant host cell that expresses the 17&#x3b2;-HSD3; obtaining a reaction mixture comprising the 17&#x3b2;-HSD3, androstenedione, and the test agent; measuring the amount of testosterone in the reaction mixture by a scintillation proximity assay (SPA) using SPA beads conjugated with a testosterone-specific antibody, wherein when the amount of testosterone is lower in the presence of a test agent than in the absence of the test agent, the test agent is identified as an inhibitor of the 17&#x3b2;-HSD3.

Methods for identifying or screening for agents that modulate 17&#x3b2;-HSD3

The present invention provides a nucleic acid and amino acid sequence of a human Pif-1 type helicase. The invention also provides methods of screening for compounds that modulate the activity of human Pif-1 type helicase, as well as methods for affecting viability of a cell by contacting the cell with a human Pif-1 helicase modulator. Such contacting specifically increases or decreases the specific activity of the human helicase in the cell, and may affect its viability, by affecting telomere length regulatory processes.

Human homologue of yeast helicase and uses thereof

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Lawrenceville, NJ, United States of America

Roberto Weinmann