Abstract: The present invention provides methods for improving or accelerating wound healing in a subject comprising administering to a wound of the subject in need thereof an agent that suppresses expression of a clock gene, wherein the clock gene is neuronal PAS domain protein 2 (Npas2). This invention also relates to methods for regenerating alveolar bone, regenerating connective tissue at a wound site, and for decreasing wound area size comprising administering to a bone loss site or a wound site, in particular, an open wound site, of a subject an agent that suppresses expression of Npas2.

Abstract: Disclosed herein are methods and compositions for removing or displacing bisphosphonates in skeletal tissue.

Abstract: In certain embodiments osteoadsorptive fluorogenic substrates of cathepsin K (or other proteases) are provided. Utilizing a bisphosphonate targeting moiety, the fluorogenic substrates provide effective bone-targeted protease sensor(s). In certain embodiments the “probes” comprise cleavable fluorophore-quencher pair linked by a cathepsin K (or other protease) peptide substrate and tethered to a bisphosphonate. Unlike existing probes that are cleared within a few days in vivo, the probes described herein (e.g., OFS-1) allow for monitoring resorption over the course of longer time periods with a single dose.

Abstract: Methods for enhancing or accelerating osseointegration of an implant into bone marrow of a subject, the methods comprising increasing expression of peripheral clock neuronal PAS domain protein 2 (NPAS2) in the bone marrow, are provided. Expression of NPAS2 is increased by administration of a Npas2 modulating compound to the subject.

Abstract: Disclosed herein are methods and compositions for removing or displacing bisphosphonates in skeletal tissue.

Abstract: Disclosed herein are methods and compositions for removing or displacing bisphosphonates in skeletal tissue.

Abstract: In certain embodiments osteoadsorptive fluorogenic substrates of cathepsin K (or other proteases) are provided. Utilizing a bisphosphonate targeting moiety, the fluorogenic substrates provide effective bone-targeted protease sensor(s). In certain embodiments the “probes” comprise cleavable fluorophore-quencher pair linked by a cathepsin K (or other protease) peptide substrate and tethered to a bisphosphonate. Unlike existing probes that are cleared within a few days in vivo, the probes described herein (e.g., OFS-1) allow for monitoring resorption over the course of longer time periods with a single dose.

Abstract: Disclosed herein are methods and compositions for removing or displacing bisphosphonates in skeletal tissue.

Abstract: Provided herein are compositions comprising aligned peptide amphiphile biomaterials, methods of generating such alignment, and their use in nerve repair applications. In particular, peptide amphiphile nanofibers are aligned using a screen extrusion method, and find use in the repair of peripheral nerve injuries.