Axys Pharmaceuticals, Inc.

Other

University of California

Arris Pharmaceutical Corporation

Applera Corporation

Discern, Inc.

James M Clark

Thomas E Jenkins

Robert M Stroud

Bradley A Katz

William R Moore

Kyle C Elrod

Robert L Warne

Kevin R Shoemaker

Harry Blount

Dana Guido

Shyr-Jiann Li

Ralph E Cholez

Travis Shanahan

Hong Zhang

A data augmentation machine may form all or part of a data augmentation system that is configured to augment data. The data augmentation machine may be configured (e.g., by one or more software modules) to access data (e.g., by crawling one or more public or private networks), extract metadata based on the data (e.g., from the data and its source), create a link to additional data (e.g., based on the extracted metadata), and augment the extracted metadata (e.g., by storing augmented metadata with the extracted metadata). Such augmented metadata may be presented (e.g., within a user interface), published publicly (e.g., on a webpage), published privately (e.g., in a report available only to premium subscribers of a data augmentation service), or any suitable combination thereof.

Data augmentation based on second-phase metadata

The present invention provides isolated monkey Cathepsin S proteins and isolated nucleic acid molecules such as cDNA molecules that encode these monkey Cathepsin S proteins. The present invention specifically provides, for example, isolated monkey Cathepsin S proteins and encoding nucleic acid molecules, methods of producing the monkey Cathepsin S proteins, methods of identifying and screening modulators of the monkey Cathepsin S proteins, and methods of using these modulators to treat a human disease or disorders associated with an orthologous human Cathepsin S protein.

Isolated monkey cathepsin S proteins, nucleic acid molecules encoding monkey cathepsin S proteins, and uses thereof

The present invention relates to serine protease inhibitors having a P site binding moiety and a divalent cation(s) chelating moiety which are pre-prepared as divalent cation(s) complexes or combined with the serine protease in the presence of divalent cation(s) and methods for identifying and using the inhibitors. The compounds are shown to have high inhibitory activity when complexed to divalent cation(s) and are useful in various processes associated with serine protease isolation and inhibition.

Metal mediated serine protease inhibitors

A method is presented for determining if the inhibition of metal mediated serine proteases can be potentiated by cobalt or zinc ions.

Potentiating metal mediated serine protease inhibitors with cobalt or zinc ions

Serine protease inhibitors are provided comprising compounds having a P site binding moiety and a divalent cation(s) chelating moiety which are pre-prepared as divalent cation(s) complexes or combined with the serine protease in the presence of divalent cation(s). The compounds are shown to have high inhibitory activity when complexed to divalent cation(s) and find use in various processes associated with serine protease isolation and inhibition.

Metal complexed serine protease inhibitors

A highly reliable, versatile and long lasting motorcycle gasket made of a special rubber-covered metal having dual raised silicone beads around the perimeter on both the front and back surfaces of the gasket. The raised silicone beads are provided around the perimeter of both the inner bore and the outer edge of the gasket to provide a double seal. Mirror-images of these same raised beads are provided on both the front and rear surfaces of the gasket further improving its sealing characteristics. A broad silicone layer is provided on both surfaces of the gasket in areas which correspond to known gaps in the metal parts of the engine with which the gasket is to be used.

Bead seal motorcycle gasket

The instant invention is directed to recombinant production of functionally active chymase. 'Functionally active' as used herein refers to the ability to exhibit one or more functional activities of a full-length wild-type chymase protein. In a preferred aspect, a proteolytically inactive chymase fusion protein comprising a functionally active portion of a non-chymase protein joined to the amino-terminus of the chymase protein is produced, which, upon cleavage away of the non-chymase fusion protein portion, becomes proteolytically active. A refolding procedure for increasing yields of proteolytically active recombinant chymase is provided. The invention is further directed to use of the recombinant chymase thus produced for preparing chymase-specific antibodies.

Growing community of inventors

San Mateo, CA, United States of America

James M Clark