I don't see buying much of anything right this minute, as I see Mr. Market taking a breather. Frankly amazed the damage today is so small given the consumer confidence number.
However, on weakness that might take it into the 4s, I like RIGL. T/FIF-like enough? Dunno, you're the judge.
From 3rd Q PR:
>>"Rigel continues to make great strides on all fronts as we advance from a pure discovery company to a development stage company. For example, we believe our progress should enable us to file several IND's over the next couple of years, with the first one expected in the summer of 2002," said James M. Gower, Chairman of the Board and Chief Executive Officer. "In addition, we are particularly excited about the work we are doing in establishing an exciting new class of small molecule oncology targets -- ubiquitin ligase inhibitors -- and you will continue to hear more from us in this area."
Ubiquitin ligases are enzymes involved in many important cellular functions, including cell division and the progression of certain cancers. These enzymes represent a promising new class of anti-cancer targets for which Rigel is developing inhibitors to work selectively against these targets at the molecular level.<<
I found another hint in PubMed (emphasis mine):
>>J Exp Med 2001 Nov 5;194(9):1263-76
Functional Cloning of Src-like Adapter Protein-2 (SLAP-2), a Novel Inhibitor of Antigen Receptor Signaling.
Holland SJ, Liao XC, Mendenhall MK, Zhou X, Pardo J, Chu P, Spencer C, Fu A, Sheng N, Yu P, Pali E, Nagin A, Shen M, Yu S, Chan E, Wu X, Li C, Woisetschlager M, Aversa G, Kolbinger F, Bennett MK, Molineaux S, Luo Y, Payan DG, Mancebo HS, Wu J.
Rigel, Incorporated, South San Francisco, CA 94080. Novartis Forschungsinstitut GmbH, A-1235 Vienna, Austria. Novartis Pharma AG, CH-4002 Basel, Switzerland.
In an effort to identify novel therapeutic targets for autoimmunity and transplant rejection, we developed and performed a large-scale retroviral-based functional screen to select for proteins that inhibit antigen receptor-mediated activation of lymphocytes. In addition to known regulators of antigen receptor signaling, we identified a novel adaptor protein, SLAP-2 which shares 36% sequence similarity with the known Src-like adaptor protein, SLAP. Similar to SLAP, SLAP-2 is predominantly expressed in hematopoietic cells. Overexpression of SLAP-2 in B and T cell lines specifically impaired antigen receptor-mediated signaling events, including CD69 surface marker upregulation, nuclear factor of activated T cells (NFAT) promoter activation and calcium influx. Signaling induced by phorbol myristate acetate (PMA) and ionomycin was not significantly reduced, suggesting SLAP-2 functions proximally in the antigen receptor signaling cascade. The SLAP-2 protein contains an NH(2)-terminal myristoylation consensus sequence and SH3 and SH2 Src homology domains, but lacks a tyrosine kinase domain. In antigen receptor-stimulated cells, SLAP-2 associated with several tyrosine phosphorylated proteins, including the ubiquitin ligase Cbl. Deletion of the COOH terminus of SLAP-2 blocked function and abrogated its association with Cbl. Mutation of the putative myristoylation site of SLAP-2 compromised its inhibitory activity and impaired its localization to the membrane compartment. Our identification of the negative regulator SLAP-2 demonstrates that a retroviral-based screening strategy may be an efficient way to identify and characterize the function of key components of many signal transduction systems.<<
snip
Cheers, Tuck |
