Phenomix Corporation

Rqx Pharmaceuticals, Inc.

Janux Therapeutics, Inc.

Afraxis Holdings, Inc.

Activx Biosciences, Inc.

Forest Laboratories Holdings Limited (bm)

Afraxis, Inc.

David Alan Campbell

David T Winn

Juan Manuel Betancort

Warren Stanfield Wade

Benedikt K Vollrath

Robert Higuchi

Peter Andrew Smith

Tucker Curran Roberts

Thomas R DiRaimondo

Prasuna Paraselli

Sergio G Duron

Sergio G Durón

Ramesh Bhatt

Min Wu

Anna Katrin Szardenings

Zhen-Ping Wu

Marek Liyanage

Julie M Cherrington

Provided herein are multispecific antibodies that selectively bind to EGFR and effector cell antigens such as CD3, pharmaceutical compositions thereof, as well as nucleic acids, and methods for making and discovering the same.

Compositions and methods related to tumor activated antibodies targeting EGFR and effector cell antigens

Provided herein are multispecific antibodies for redirecting T cells to cancers, that rely on binding of one antigen interacting portion of the antibody to a tumor-associated antigen or marker, such as epidermal growth factor receptor (EGFR), while a second antigen interacting portion can bind to an effector cell antigen on a T cell, such as CD3, pharmaceutical compositions thereof, as well as nucleic acids, and methods for making and discovering the same.

Provided herein are multispecific antibodies that selectively bind to PSMA and effector cell antigens such as CD3, pharmaceutical compositions thereof, as well as nucleic acids, and methods for making and discovering the same.

Compositions and methods related to tumor activated antibodies targeting PSMA and effector cell antigens

Provided herein are cleavable linkers, pharmaceutical compositions thereof, as well as nucleic acids, and methods for making and discovering the same. The cleavable linkers described herein have improved efficacy and safety.

Cleavable linker compositions and methods

Provided herein are analogs of the natural product arylomycin for the treatment of microbial infections. In some embodiments, the compounds described herein have broad spectrum bioactivity. The compounds provided herein can in other embodiments overcome the resistance conferred by single amino acid mutations at defined positions of bacterial Signal Peptidases (SPases) and in other embodiments provide for a broader spectrum of antibiotic bioactivity compared to the natural product. Pharmaceutical compositions and methods for treatment using the compounds described herein are also provided.

Broad spectrum antibiotics

Provided herein are antibacterial compounds, wherein the compounds in some embodiments have broad spectrum bioactivity. The compounds provided herein can in other embodiments overcome the resistance conferred by single amino acid mutations at defined positions of bacterial Signal Peptidases (SPases) and in other embodiments provide for a broad spectrum of antibiotic bioactivity. Pharmaceutical compositions and methods for treatment using the compounds described herein are also provided.

Linear peptide antibiotics

Provided herein are antibacterial compounds, wherein the compounds in some embodiments have broad spectrum bioactivity. In various embodiments, the compounds act by inhibition of bacterial type 1 signal peptidase (SpsB), an essential protein in bacteria. Pharmaceutical compositions and methods for treatment using the compounds described herein are also provided.

Macrocyclic broad spectrum antibiotics

Provided herein are PAK inhibitors and methods of utilizing PAK inhibitors for the treatment of CNS disorders such as neuropsychiatric disorders.

6-(sulfonylaryl)pyrido[2,3-D]pyrimidin-7(8H)-ones for the treatment of CNS disorders

Provided herein are PAK inhibitors and methods of utilizing PAK inhibitors for the treatment of CNS disorders.

6-(ethynyl)pyrido[2,3-D]pyrimidin-7(8H)-ones for the treatment of CNS disorders

Provided herein are pyrido[2,3-D]pyrimidin-7(8H)-one compounds and compositions useful as PAK inhibitors. Also provided herein are methods of utilizing these compounds for the treatment of neuropsychiatric conditions. The compounds modulate dendritic spine morphology and/or synaptic function.

Compounds for treating neuropsychiatric conditions

Dipeptidyl peptidase IV (DPP-IV)-inhibiting compounds are provided that have formula I: wherein n is 1 to 3; X is CHS; O; CFor C(CH); Z is H; halogen; hydroxyl; (C)alkoxy; (C)alkyl; (C)cycloalkyl; phenyl; or heteroaryl; where the phenyl and heteroaryl groups are optionally mono- or independently plurisubstituted with R7; optionally, X together with an adjacent ring carbon and Z form a fused cyclopropyl; and optionally, one of the bonds in the ring containing X is a double bond; and CrR, R, R, R, Rand Rare as described herein. Methods for preparing these compounds, and methods for treating diabetes, especially Type II diabetes, and other related diseases are described using the compounds of formula I in pharmaceutical compositions which contain these compounds. Pharmaceutical compositions which contain combinations of these compounds with other antidiabetic agents are also described herein. 

Heterocyclic boronic acid compounds

8-ethyl-6-(aryl)pyrido[2,3-D]pyrimidin-7(8H)-ones for the treatment of CNS disorders

This invention relates to DPP-IV inhibitory citrate or tartrate salts of pyrrolidinylaminoacetyl pyrrolidine boronic acid compounds that are physically and chemically stable, substantially non-deliquescent solids under ambient conditions.

Solid tartrate salts of DPP-IV inhibitors

The present invention provides compositions and methods for assessing profiles of catalytically active enzymes in compositions containing a plurality of proteins. In preferred embodiments, the enzyme is a hydrolase, most preferably a cysteine protease. The methods described herein use activity based probes ('ABPs') that have an affinity moiety for directing the binding of the ABP to one or more catalytically active target enzymes, a reactive group for forming a covalent bond at an active site of the target enzyme(s), and a TAG (e.g., a detectable label, preferably a fluorophore). One or more ABPs may be combined with a protein-containing sample under conditions for binding and reaction of the ABP(s) with target enzyme(s) that are present in the sample. The resulting products may then be used to assess the active enzyme profile of the sample, and can be correlated to the presence, amount, or activity of one or more target enzyme(s) present in the original complex protein mixture. 

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Sand Diego, CA, United States of America

David Alan Campbell