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Matthew James Hilton

Professor in Orthopaedic Surgery
Orthopaedic Surgery
450 Research Drive, LSRC B321C, DUMC 91009, Durham, NC 27710
91009, Durham, NC 27710

Overview


A long-term interest of the Hilton lab is to uncover the molecular circuitry regulating lineage commitment, proliferation, and differentiation of skeletal stem cells, chondrocytes, and osteoblasts. My laboratory uses genetic mouse models and primary cell culture techniques coupled with biochemistry to answer questions regarding skeletal stem cell self-renewal/differentiation, chondrogenesis, and osteoblastogenesis. Recently my lab has generated novel data from a variety of Notch gain and loss-of-function mutant mice demonstrating the importance of Notch signaling in each of these processes. We are currently investigating the exact Notch signaling mechanisms at play during skeletal development, disease, and repair. Additional studies are also focused on identifying and understanding the molecular mechanisms underlying various congenital skeletal pathologies, including Multiple Herediatry Exostoses (MHE) and Preaxial Polydactyly (PPD).

Current Duke Appointments & Affiliations


Professor in Orthopaedic Surgery · 2024 - Present Orthopaedic Surgery, Clinical Science Departments
Affiliate of the Duke Regeneration Center · 2021 - Present Duke Regeneration Center, Basic Science Departments

Recent Scholarly Works


Characterizing histological fatty accumulation, muscle atrophy, and fibrosis in relation to re-tear and revision after primary rotator cuff repair: a mean 3-year follow-up study.

Journal article JSES Rev Rep Tech · May 2026 BACKGROUND: The failure rate following primary arthroscopic rotator cuff repair (RCR) is high. There is little existing literature reporting on failure rates in the context of the histological degree of fatty accumulation, fibrosis, and atrophy of the rota ... Full text Link to item Cite

MESH1 functions as a metazoan PAPS phosphatase to regulate sulfation.

Journal article Nat Chem Biol · April 10, 2026 Biological sulfation reactions require 3'-phosphoadenosine-5'-phosphosulfate (PAPS) as the universal sulfate donor. While the biosynthetic pathway of PAPS has been well characterized, the phosphatase degrading PAPS remains unidentified. Here, we discover M ... Full text Open Access Link to item Cite
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Recent Grants


Genetics and Genomics Training Grant

Inst. Training Prgm or CMEMentor · Awarded by National Institutes of Health · 2026 - 2031

Cell and Molecular Biology Training Program

Inst. Training Prgm or CMEMentor · Awarded by National Institute of General Medical Sciences · 2026 - 2031

JAK Specific Signaling in PTOA-associated Joint Degeneration and Pain

ResearchPrincipal Investigator · Awarded by National Institutes of Health · 2025 - 2030

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Education


University of Houston · 2004 Ph.D.