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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Bone morphogenetic protein 3

BMP-3, bone morphogenetic protein-3, Osteogenin
BMP3 belongs to the transforming growth factor-beta (TGFB) superfamily. Bone morphogenic protein, also known as osteogenin, induces bone formation. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, TGF-beta, BMP-7, BMP4, ACID
Papers on BMP-3
Wisp1 mediates Bmp3-stimulated mesenchymal stem cell proliferation.
Yang et al., London, Canada. In J Mol Endocrinol, Jan 2016
Previously, we demonstrated that bone morphogenetic protein 3 (Bmp3), the expression of which was upregulated in our rat model of hyperplasic visceral adiposity, potently stimulated MSC proliferation.
Identification of plasma microRNA expression profile in radiographic axial spondyloarthritis-a pilot study.
Haseeb et al., Cleveland, United States. In Clin Rheumatol, Jan 2016
miR-34a, which was overexpressed in patients with rad-axial SpA, was predicted to target BMP-3 mRNA by TargetscanS and PicTar miRNA target algorithms.
The role of the BMP signaling cascade in regulation of stem cell activity following massive small bowel resection in a rat.
Coran et al., Haifa, Israel. In Pediatr Surg Int, Nov 2015
From these genes, five genes were found to be up-regulated in jejunum (BMP1-10 %, BMP2-twofold increase, BMP3-10 %, BMP2R-12 % and STAT3-28 %) and four genes to be up-regulated in ileum (BMP1-16 %, BMP2-27 %, BMP3-10 %, and STAT3-20 %) in SBS vs sham animals with a relative change in gene expression level of 10 % or more.
Stool DNA methylation assays in colorectal cancer screening.
Nossikoff et al., Sofia, Bulgaria. In World J Gastroenterol, Oct 2015
In this paper, we describe the recent advances in non-invasive CRC screening and more specifically in molecular assays for aberrantly methylated BMP3 and NDRG4 promoter regions.
Palmieri et al., Monza, Italy. In J Biol Regul Homeost Agents, Jul 2015
After 24 h, significant up-regulated genes (Fold change > 2) in DPSCs were the Bone Morphogenetic Proteins BMP3, BMP4 and their receptor BMPR1A.
[Fecal Biomarker for Colorectal Cancer Diagnosis].
Matsumura et al., In Rinsho Byori, Mar 2015
DNA mutation of APC, KRAS, and TP53 genes and DNA methylation of VIM, TFPI2, BMP3, NDRG4, and SFRP2 genes were reported as fecal DNA biomarkers.
BMP3 Alone and Together with TGF-β Promote the Differentiation of Human Mesenchymal Stem Cells into a Nucleus Pulposus-Like Phenotype.
Chen et al., Hangzhou, China. In Int J Mol Sci, 2014
Thus far, the effects of bone morphogenetic protein 3 (BMP3) and the cocktail effects of BMP3 and transforming growth factor (TGF)-β on MSC proliferation and differentiation remain obscure.
The Functions of BMP3 in Rabbit Articular Cartilage Repair.
Zhang et al., Beijing, China. In Int J Mol Sci, 2014
As BMP2/4 show a clearly positive effect for cartilage repair, we investigated the functions of BMP3 in rabbit articular cartilage repair.
Multitarget stool DNA testing for colorectal-cancer screening.
Berger et al., Framingham, United States. In N Engl J Med, 2014
The DNA test includes quantitative molecular assays for KRAS mutations, aberrant NDRG4 and BMP3 methylation, and β-actin, plus a hemoglobin immunoassay.
Growth and differentiation factors for periodontal regeneration: a review on factors with clinical testing.
Wikesjö et al., Århus, Denmark. In J Periodontal Res, 2012
RESULTS: Growth and differentiation factor technologies intended for periodontal wound healing/regeneration and evaluated clinically included platelet-derived growth factor, insulin-like growth factor-I and -II, basic fibroblast growth factor, bone morphogenetic protein-3 and growth differentiation factor-5; platelet-derived growth factor was the only Food and Drug Administration-approved commercially available growth and differentiation factor technology.
BMP3 suppresses osteoblast differentiation of bone marrow stromal cells via interaction with Acvr2b.
Rosen et al., Boston, United States. In Mol Endocrinol, 2012
findings best fit a model in which BMP3, produced by mature bone cells, acts to reduce BMP signaling through Acvr2b in skeletal progenitor cells, limiting their differentiation to mature osteoblasts
Bone morphogenetic protein 3 controls insulin gene expression and is down-regulated in INS-1 cells inducibly expressing a hepatocyte nuclear factor 1A-maturity-onset diabetes of the young mutation.
Prehn et al., Dublin, Ireland. In J Biol Chem, 2011
a critical link between HNF1A-MODY-induced alterations in Bmp-3 expression and insulin gene levels
Circulating bone morphogenetic protein 1-3 isoform increases renal fibrosis.
Vukicevic et al., Zagreb, Croatia. In J Am Soc Nephrol, 2011
Circulating bone morphogenetic protein 1-3 isoform increases renal fibrosis.
8.6Mb interstitial deletion of chromosome 4q13.3q21.23 in a boy with cognitive impairment, short stature, hearing loss, skeletal abnormalities and facial dysmorphism.
Limon et al., Gdańsk, Poland. In Genet Couns, 2010
As an addition to PRKG2 and RASGEFIB genes, we propose to include BMP3 gene as the principal determinant of the observed common phenotype.
Evidence for positive selection on the Osteogenin (BMP3) gene in human populations.
Zhang et al., Kunming, China. In Plos One, 2009
Features supportive of positive selection in the BMP3 gene were found including the presence of an excess of nonsynonymous mutations in modern humans, and a significantly lower genetic diversity that deviates from neutrality
BMP and BMP inhibitors in bone.
Rosen, Boston, United States. In Ann N Y Acad Sci, 2006
To date, inhibin and BMP-3 have been identified as BMP receptor antagonists that can block BMP signaling in bone.
Bone morphogenetic proteins.
Mundy et al., Rochester, United States. In Growth Factors, 2004
The activity of BMPs was first identified in the 1960s (Urist, M.R. (1965) "Bone formation by autoinduction", Science 150, 893-899), but the proteins responsible for bone induction remained unknown until the purification and sequence of bovine BMP-3 (osteogenin) and cloning of human BMP-2 and 4 in the late 1980s (Wozney, J.M. et al. (1988) "Novel regulators of bone formation: molecular clones and activities", Science 242, 1528-1534; Luyten, F.P. et al. (1989) "Purification and partial amino acid sequence of osteogenin, a protein initiating bone differentiation", J. Biol.
Bone morphogenetic protein-3 is a negative regulator of bone density.
Lyons et al., Los Angeles, United States. In Nat Genet, 2001
BMP3 was originally purified from bone as osteogenin, which induces osteogenic differentiation.
Novel regulators of bone formation: molecular clones and activities.
Wang et al., Cambridge, United States. In Science, 1989
Each of the three (BMP-1, BMP-2A, and BMP-3) appears to be independently capable of inducing the formation of cartilage in vivo.
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