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Biotech / Medical : Ligand (LGND) Breakout! -- Ignore unavailable to you. Want to Upgrade?

To: Henry Niman who wrote (20997)	5/17/1998 6:55:00 PM
From: Machaon	Read Replies (1) \| Respond to of 32384

Henry, I never realized that tonyt and fugazi had such big hearts, and such a high level of ethics. <VBG> Perhaps we have been wrong about them!? Maybe they have been contributing, all this time, to this thread, in the spirit of friendship and fellowship? Maybe, when they write insulting PMS type of nasty notes, they are actually saying how much they love us! We have been sooooo wrong, Henry. (sniff!) My little heart is broken. (Head is now hanging low, tears dripping off my face and cascading downwards towards the floor, splattering badly, as if the shame is too much to bare.) (sniff!) But, there is hope. (sniff!) Even though the ASCO might've ok'ed Physicians Assisted Suicide (PASS), for those with terminal PMS syndrome, some day they might find a cure. Oh well, you win some, you lose some. <g> By the way: GO LGND!!! Regards, Bob

To: Henry Niman who wrote (20997)	5/17/1998 9:31:00 PM
From: squetch	Read Replies (1) \| Respond to of 32384

Looks like one less ORPHAN in the world. Genes Dev 1998 May 1;12(9):1269-1277 BXR, an embryonic orphan nuclear receptor activated by a novel class of endogenous benzoate metabolites. Blumberg B, Kang H, Bolado J Jr, Chen H, Craig AG, Moreno TA, Umesono K, Perlmann T, De Robertis EM, Evans RM Gene Expression Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037 USA. [Record supplied by publisher] Nuclear receptors are ligand-modulated transcription factors that respond to steroids, retinoids, and thyroid hormones to control development and body physiology. Orphan nuclear receptors, which lack identified ligands, provide a unique, and largely untapped, resource to discover new principles of physiologic homeostasis. We describe the isolation and characterization of the vertebrate orphan receptor, BXR, which heterodimerizes with RXR and binds high-affinity DNA sites composed of a variant thyroid hormone response element. A bioactivity-guided screen of embryonic extracts revealed that BXR is activatable by low-molecular-weight molecules with spectral patterns distinct from known nuclear receptor ligands. Mass spectrometry and 1H NMR analysis identified alkyl esters of amino and hydroxy benzoic acids as potent, stereoselective activators. In vitro cofactor association studies, along with competable binding of radiolabeled compounds, establish these molecules as bona fide ligands. Benzoates comprise a new molecular class of nuclear receptor ligand and their activity suggests that BXR may control a previously unsuspected vertebrate signaling pathway. ncbi.nlm.nih.gov