Agouron Pharmaceuticals, Inc.

Other

Michael R Gehring

Michele Ann McTigue

Jesus Ernest Villafranca

Krzysztof Appelt

Chen-Chen Kan

Barbara Mroczkowski

Anna M Tempcyzk-Russell

Chris Pinko

John A Wickersham

Camran V Parast

Richard E Showalter

An outdoor-use heating mat system includes at least one heating mat. At least one heating mat of the system includes a first structural layer, a heating element, a plurality of intermediate strips, a second structural layer, and at least one of a cord and a plug. The first and second structural layers each are both durable and electrically insulating. The first such layer has a plurality of first layer edges associated therewith. The heating element positioned above the first structural layer. The plurality of intermediate strips are mounted upon the first structural layer. Each intermediate strip is positioned proximate at least one of one the first layer edge and the heating element. The second structural layer is mounted to the plurality of intermediate strips opposite the first structural layer.

Outdoor-use heating mat system

A 2.4 &#x212b; crystal structure of a protein construct containing the catalytic kinase domain of vascular endothelial growth factor receptor 2 (VEGFR2/KDR), a key enzyme in angiogenesis, has been determined in an unliganded, phosphorylated state. This protein construct, contains a modified catalytic linker and has comparable in vitro kinase activity to constructs containing the entire KID. The resulting construct retains comparable in vitro kinase activity to that of the wild-type KID, and more importantly, allows complete crystallization of the protein such that it may be characterized by X-ray crystallography. The present invention further discloses the use of the x-ray crystallographic data for identification and construction of possible therapeutic compounds in the treatment of various disease conditions.

Modifications of the VEGF receptor-2 protein and methods of use

A 2.4 &angst; crystal structure of a protein construct containing the catalytic kinase domain of vascular endothelial growth factor receptor 2 (VEGFR2/KDR), a key enzyme in angiogenesis, has been determined in an unliganded, phosphorylated state. This protein construct, contains a modified catalytic linker and has comparable in vitro kinase activity to constructs containing the entire KID. The resulting construct retains comparable in vitro kinase activity to that of the wild-type KID, and more importantly, allows complete crystallization of the protein such that it may be characterized by X-ray crystallography. The present invention further discloses the use of ray crystallographic data for identification and construction of possible therapeutic compounds in the treatment of various disease conditions.

A 2.4 &angst; crystal structure of a protein construct containing the catalytic kinase domain of vascular endothelial growth factor receptor 2 (VEGFR2/KDR), a key enzyme in angiogenesis, has been determined in an unliganded, phosphorylated state. This protein construct, contains a modified catalytic linker and has comparable in vitro kinase activity to constructs containing the entire KID. The resulting construct retains comparable in vitro kinase activity to that of the wild-type KID, and more importantly, allows complete crystallization of the protein such that it may be characterized by X-ray crystallography. The present invention further discloses the use of x-ray crystallographic data for identification and construction of possible therapeutic compounds in the treatment of various disease conditions.

Modifications of the VEGF Receptor-2 Protein and methods of use

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Ramona, CA, United States of America

Michael R Gehring