Wyeth

Genetics Institute, Inc.

American Home Products Corporation

Kodiak Sciences Inc.

Other

Millennium Pharmaceuticals Limited

William Stuart Somers

Mark L Stahl

Lidia Mosyak

Laura Lin

Kevin Delos Parris

Amy Szepui Tam

Jasbir S Seehra

James Bradley Aggen

Stephen A Charles

Wayne To

Tetsuya Ishino

Guang-Yi Xu

Justin Cohen

Zhang Bao Xu

Tatos Akopian

Rayomand Jal Unwalla

Jonathan A Bard

Didier G Benoit

Lori J Fitz

Eric Steven Manas

Daniel Victor Perlroth

Francis Sullivan

D Victor Perlroth

Robert L Powers

Xiaotian Zhong

Stephane Olland

Thomas E McDonagh

Rajiv Chopra

Divya Chaudhary

Chu-Lai Hsiao

James M Wilhelm

Kristine Svenson

Karl Malakian

Zhang-Bao Xu

Laura Long Lin

Brian Dwyer

Andrea Dessen

Hsiang-Ai Yu

Mark Johnson

Jin Hong

Eleonora Presman

Bethany Annis Freeman

Scott Wolfrom

Julie Lee

Didler Benoit

Rita Greco

Wah-Tung Hum

The invention provides a dual VEGF/PDGF antagonist comprising a VEGF antagonist linked to a PDGF antagonist. The VEGF antagonist is an antibody to a VEGF or VEGFR or is a VEGFR extracellular trap segment (i.e., a segment from the extracellular region of one or more VEGFR receptors that inhibits binding of at least one VEGFR to at least one VEGF). The PDGF antagonist is an antibody to a PDGF or PDGFR or is a PDGFR extracellular trap segment (i.e., segment from the extracellular region of one or more PDGFRs, which inhibits binding of at least one PDGFR and at least one PDGF). The dual antagonist is preferably conjugated to a half-life extending moiety, such as a HEMA-PC polymer. The dual antagonist is particularly useful for treating wet aged related macular degeneration.

Dual PDGF/VEGF antagonists

This disclosure relates to LINGO-1 polypeptides, LINGO-1 polypeptide/ligand complexes, crystals of LINGO-1 polypeptides, crystals of LINGO-1 polypeptide/ligand complexes, and related methods and software systems.

Method for identifying or designing a candidate agent that interacts with LINGO-1 polypeptide using a LINGO-1 three-dimensional structure

This invention is directed to the three dimensional crystal structure of Beta-site APP Cleaving Enzyme (BACE), and to the use of this structure in rational drug design methods to identify agents that may interact with active sites of BACE. Such agents may represent new therapeutics in the treatment and/or prevention of Alzheimer's Disease.

Method for identifying agents that interact with beta-site APP cleaving enzyme (BACE)

A three-dimensional structure of human protein kinase C theta (PKC&#x3b8;) can be used in methods of designing an agent that interacts with PKC&#x3b8;. The agent can be an inhibitor of PKC&#x3b8; activity.

Structure of protein kinase C theta

Estrogen receptor ligands, estrogen receptor polypeptide/ligand complexes, crystals of estrogen receptor polypeptide/ligand complexes, and related methods and software systems are disclosed.

Methods for the design of estrogen receptor ligands

This invention is directed to the crystal structure of Estrogen Receptor-&#x3b2; (ER-&#x3b2;) complexed with genistein, and to the use of this structure in rational drug design methods to identify agents that may interact with active sites of ER-&#x3b2;, which may be useful as novel chemotherapeutic agents.

Method using crystal structure of estrogen receptor-&#x3b2; complex

This invention is directed to the crystal structure of Acyl Carrier Protein Synthase (ACPS) complexed with Acyl Carrier Protein (ACP), the solution structure ofACP, and to the use of these structures in rational drug design methods to identify agents that may interact with active sites of ACPS and ACP, and to the testing of these agents to identify agents that may represent novel antibiotics.

Crystals of an acyl carrier protein synthase/acyl carrier protein complex

This invention is directed to Acyl Carrier Protein Synthase (ACPS) crystals and crystals of Acyl Carrier Protein Synthase-Coenzyme A (ACPS-CoA) complex, and to the use of these crystals to determine the three dimensional structure of ACPS. This invention is further directed to the use of rational drug design methods to identify agents that may interact with active sites of ACPS and ACPS-CoA complex, and to the testing of these agents to identify agents that may inhibit ACPS and/or ACPS-CoA complex activity.

Methods for identifying an agent that interacts with an active site of acyl carrier protein synthase or acyl carrier protein synthase complex

The present invention provides for crystalline cPLA2. The crystal structure of cPLA2 has also been solved using such material. Models based upon such crystal structure are also provided. Methods of identifying inhibitors of cPLA2 activity and membrane binding using such models are also disclosed.

Crystal structure of cPLA2 and methods of identifying agonists and antagonists using same

This invention is directed to the crystal structure of Acyl Carrier Protein Synthase (ACPS) complexed with Acyl Carrier Protein (ACP), the solution structure of ACP, and to the use of these structures in rational drug design methods to identify agents that may interact with active sites of ACPS and ACP, and to the testing of these agents to identify agents that may represent novel antibiotics.

Methods for identifying agents that interact with an active site of acyl carrier protein synthase-acyl carrier protein complex

Crystallographic and NMR solution structures of human IL-6 are reported. The invention provides models and systems incorporating such structures which are useful for identifying IL-6/IL-6 receptor interactions and for identification of agonists and antagonists of such interactions. Crystalline human IL-6 is also provided.

Crystalline IL-6 and models of the molecular structure of IL-6

The present invention provides for crystalline GFS. The crystal structure of GFS has also been solved using such material. Models based upon such crystal structure are also provided. Methods of identifying inhibitors of GFS activity using such models are also disclosed.

Crystal structure of E. coli GDP-fucose synthetase (and complexes thereof) and methods of identifying agonists and antagonists using same

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Cambridge, MA, United States of America

William Stuart Somers