Genetics Institute, Inc.

Wyeth

Other

Lih-Ling Lin

James R Graham

Jennifer Chen

Andrea R Schievella

Jean-Baptiste Telliez

Guang-Yi Xu

Ariamala Gopalsamy

Neelu Kaila

Neal Green

Steve Yikkai Tam

Dennis William Powell

Lori Krim Gavrin

Thomas E McDonagh

Yonghan Hu

Yongchang Qiu

Joseph Lawrence Wooters

John William Cuozzo

Jun Kuai

Kristin Marie Janz

Jennifer R Thomason

Steven F Sukits

Yvonne M Yannoni

Elliott Nickbarg

Desiree H H Tsao

Sang Hsu

A Karl Malakian

Polynucleotides encoding DADD protein are also disclosed, along with vectors, host cells, and methods of making DADD protein. Methods of identifying inhibitors of DADD death domain binding and inhibitors identified by such methods are also disclosed.

DADD, death activator death domain protein

The present invention relates to the three dimensional solution structure of the N-terminal domain of TNFR-1 associated death domain protein ('N-TRADD'), as well as the identification and characterization of a C-TRAF2 binding active site of N-TRADD. Also provided for by the present invention are methods of utilizing the three dimensional structures for the design and selection of potent and selective inhibitors of TNF signaling pathways.

N-TRADD active site and uses thereof

The present invention provides compounds of formula (I): and pharmaceutically acceptable salts thereof, wherein R, R, R, R, Rr, m and n are defined as described herein. The invention also provides methods of making the compounds of formula (I), and methods of treating inflammatory diseases, such as rheumatoid arthritis, in a mammal comprising administering a therapeutically effective amount of a compound of formula (I) to the mammal.

4,6-diamino-[1,7]naphthyridine-3-carbonitrile inhibitors of Tpl2 kinase and methods of making and using the same

The present invention relates to the three dimensional solution structure of receptor interacting protein dead domain (RIP DD), as well as the identification and characterization of various binding active sites of RIP DD. Also provided for by the present invention are methods of utilizing the three dimensional structure for the design and selection of potent and selective inhibitors of TNF signaling pathways.

Solution structure of RIP DD and uses thereof

The present invention relates to uses of proteins that bind MK2 to modulate inflammation. More particularly, the invention relates to uses of proteins that bind MK2 for treating condition that are related to inflammation. The invention is useful for treating inflammatory conditions, particularly those in which a decrease in inflammation would be therapeutically beneficial.

MK2 interacting proteins

The invention relates to compositions and methods comprising lymphotoxin-beta receptor (LT&#x3b2;R) modulators, which activate or inhibit LT&#x3b2;R signaling. LT&#x3b2;R modulators are useful for treating lymphocyte mediated immunological diseases and cancer, and more particularly, for regulating mitochondrial-mediated apoptosis. This invention relates to soluble forms of the LT&#x3b2;R complex proteins that act as LT&#x3b2;R activating or inhibiting agents. This invention also relates to the use of soluble molecules, directed against either the LT&#x3b2;R, its ligands, LIGHT and LT&#x3b2;1&#x3b1;2, or its intracellular binding partners, that function to regulate LT&#x3b2;R signaling. A novel screening method for selecting soluble receptors, antibodies and other agents that modulate LT&#x3b2;R signaling is provided.

Method of identifying a modulator of a LT&#x3b2;R complex signaling pathway

Novel TNF receptor death domain ('TNF-R1-DD') ligand proteins are disclosed. Polynucleotides encoding the TNF-R1-DD ligand protein are also disclosed, along with vectors, host cells, and methods of making the TNF-R1-DD ligand protein. Pharmaceutical compositions containing the TNF-R1-DD ligand protein, methods of treating inflammatory conditions, and methods of inhibiting TNF-R death domain binding are also disclosed. Methods of identifying inhibitors of TNF-R death domain binding and inhibitors identified by such methods are also disclosed.

TNF receptor death domain ligand proteins and inhibitors of ligand binding

Antibodies to IL-1-R intracellular ligand proteins are disclosed. The antibodies arc useful for inhibiting the binding between IL-1-R and IL-1-R intracellular ligand proteins.

Antibodies to interleukin-1 receptor intracellular ligand proteins

Novel TNF receptor death domain (&ldquo;TNF-R1-DD&rdquo;) ligand proteins are disclosed. Polynucleotides encoding the TNF-R1-DD ligand protein are also disclosed, along with vectors, host cells, and methods of making the TNF-R1-DD ligand protein. Pharmaceutical compositions containing the TNF-R1-DD ligand protein, methods of treating inflammatory conditions, and methods of inhibiting TNF-R death domain binding are also disclosed. Methods of identifying inhibitors of TNF-R death domain binding and inhibitors identified by such methods are also disclosed.

Novel IL-1-R intracellular ligand proteins are disclosed. Polynucleotides encoding the IL-1-R intracellular ligand protein are also disclosed, along with vectors, host cells, and methods of making the IL-1-R intracellular ligand protein. Pharmaceutical compositions containing the IL-1-R intracellular ligand protein, methods of treating inflammatory conditions, and methods of inhibiting IL-1-R intracellular domain binding are also disclosed. Methods of identifying inhibitors of IL-1-R intracellular domain binding and inhibitors identified by such methods are also disclosed.

Method of identification of inhibitors of IL-1 receptor intracellular domain binding

Interleukin-1 receptor intracellular ligand proteins

TNF receptor death domain ligand proteins

TNF receptor death ligand proteins and inhibitors of ligand binding

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Concord, MA, United States of America

Lih-Ling Lin