Receptor linked protein tyrosine phosphatases

Details Receptor linked protein tyrosine phosphatases Receptor linked protein tyrosine phosphatases

2007-05-22

2007-05-22

Kunemund, Robert (Department: 1722)

Single-crystal, oriented-crystal, and epitaxy growth processes;

Processes of growth from liquid or supercritical state

Having growth from a solution comprising a solvent which is...

C117S069000, C117S929000

Reexamination Certificate

active

10385206

ABSTRACT:
The crystal structures of CD45 and LAR, described herein, provide a basis for kinetic and functional studies. Identification of the crystal structures of cellular molecules is important in to determine functional roles in immunity, phosphorylation events, disease initiation mechanism. The isolated crystals and methods for crystallization thereof, are also important in identifying small molecule interactions with cellular molecules for new drug discovery.

REFERENCES:
Jiang et al., “Receptor-like Protein Phosphatase Homodimerizes on the Cell Surface”, Molecular and Cellular Biology Aug. 200 pp. 5917-5929.
Blom et al., “Characterization of a Human Basophil-Like Cell Line”, Scand. J. Immunol. vol. 44 1996 pp. 54-61.
Li et al., “Efficient Total Synthese of Pulchellactam, A CD45 Protein Tyrosine Phosphatase Inhibitor”, J. Org. Chem vol. 67 No. 14. 2002 pp. 4702-4706.
Nam et al., Crystal Structure of the Tandem Phosphatase Domains of RPTP LAR, Cell, vol. 97 May 1999 pp. 449-457.

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