Results 11 to 20 of about 27,645,133 (294)

Recombinant human bone morphogenetic protein-2 in the treatment of bone fractures

open access: yesBiologics: Targets & Therapy, 2008
Neil Ghodadra, Kern SinghDepartment of Orthopedic Surgery, Rush University Medical Center, Chicago, Illinois, USAAbstract: Over one million fractures occur per year in the US and are associated with impaired healing increasing patient morbidity, stress ...
Neil Ghodadra, Kern Singh
doaj   +5 more sources

The effect of bone morphogenetic protein-2 on osteosarcoma metastasis. [PDF]

open access: yesPLoS ONE, 2017
PURPOSE:Bone Morphogenetic Protein-2 (BMP-2) may offer the potential to enhance allograft-host osseous union in limb-salvage surgery following osteosarcoma resection.
Jonathan Gill   +11 more
doaj   +4 more sources

Limitations of bone formation in oral implantology: inhibition of osteoblast functions by gingival tissues [PDF]

open access: yes, 2010
PhDClinical observation suggest that bone formation is influenced by the environmental niche where it takes place and specifically that soft connective tissues may inhibit the bone healing process.
Al-Masri, Maher
core   +4 more sources

Bone morphogenetic protein-2 and bone therapy: successes and pitfalls [PDF]

open access: yesJournal of Pharmacy and Pharmacology, 2016
Abstract Objectives Bone morphogenetic proteins (BMPs), more specifically BMP-2, are being increasingly used in orthopaedic surgery due to advanced research into osteoinductive factors that may enhance and improve bone therapy.
Poon, B.   +3 more
openaire   +3 more sources

Novel fluorescent probes for analysis of protein interactions under truly physiological conditions with real medical devices [PDF]

open access: yes, 2012
PhDProtein adsorption under physiological conditions was recognised to be the key step in the modulation of biological responses between materials and an osseous environment.
Mafina, Marc-Krystelle
core   +4 more sources

Bone Morphogenetic Protein-2 Stimulates Runx2 Acetylation [PDF]

open access: yesJournal of Biological Chemistry, 2006
Runx2/Cbfa1/Pebp2aA is a global regulator of osteogenesis and is crucial for regulating the expression of bone-specific genes. Runx2 is a major target of the bone morphogenetic protein (BMP) pathway. Genetic analysis has revealed that Runx2 is degraded through a Smurf-mediated ubiquitination pathway, and its activity is inhibited by HDAC4.
Eun-Joo, Jeon   +13 more
openaire   +2 more sources

Bone morphogenetic protein-2 influence on metabolic activity and proteoglycan synthesis by intervertebral disc cells

open access: yesActa Biomedica Scientifica, 2016
Modern therapeutic strategies for intervertebral disc repair mainly focus on targeting molecular pathways of extracellular matrix degeneration. Anabolic strategies for regeneration are aimed to increase production of major extracellular molecules ...
L. A. Bardonova   +2 more
doaj   +1 more source

USP15 targets ALK3/BMPR1A for deubiquitylation to enhance bone morphogenetic protein signalling [PDF]

open access: yes, 2014
Protein kinase ALK3/BMPR1A mediates bone morphogenetic protein (BMP) signalling through phosphorylation and activation of SMADs 1/5/8. SMAD6, a transcriptional target of BMP, negatively regulates the BMP pathway by recruiting E3 ubiquitin ligases and ...
Bruce, David   +11 more
core   +1 more source

Regulation of Phosphatase Homologue of Tensin Protein Expression by Bone Morphogenetic Proteins in Prostate Epithelial Cells [PDF]

open access: yes, 2010
Phosphatase homologue of tensin (PTEN) is the key endogenous inhibitor of phosphoinositide signaling and is the most commonly mutated gene in human prostate cancer.
Travis Jerde   +4 more
core   +1 more source

Protein associated with SMAD1 (PAWS1/FAM83G) is a substrate for type I bone morphogenetic protein receptors and modulates bone morphogenetic protein signalling [PDF]

open access: yes, 2014
Bone morphogenetic proteins (BMPs) control multiple cellular processes in embryos and adult tissues. BMPs signal through the activation of type I BMP receptor kinases, which then phosphorylate SMADs 1/5/8.
Smith, James C.   +15 more
core   +1 more source

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