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BMPR1A and the ubiquitous isoform of BMPR1B differed in mode of translocation into the endoplasmic reticulum; and (ii) BMPR1A was N-glycosylated while BMPR1B was not, resulting in greater efficiency of processing and plasma membrane expression of BMPR1A.
Several germline variants in Hamartomatous Polyposis Syndrome genes were detected, among them three in ENG (show ENG Proteins), two in BMPR1A, one in PTEN, and one in SMAD4 (show SMAD4 Proteins). Although some of the detected variants have been reported previously none could be definitely pathogenic or likely pathogenic.
The present study suggests that HNF-4alpha has a suppressive effect on hepcidin expression by inactivating the BMP pathway, specifically via BMPR1A, in HepG2 cells.
In solid ameloblastoma, positive correlations were observed between the stromal and parenchymal expression of BMP-2 (show BMP2 Proteins) and between the stromal expression of BMP-2 (show BMP2 Proteins) and BMP-4 (show BMP4 Proteins), as well as between the stromal expression of BMPR-II (show BMPR2 Proteins) and BMP-4 (show BMP4 Proteins) and the stromal and parenchymal expression of BMPR-II (show BMPR2 Proteins).
Data show that protein kinase (show CDK7 Proteins) LKB1 (show STK11 Proteins) physically interacts with BMP type I receptors and requires Smad7 (show SMAD7 Proteins) protein to promote downregulation of the receptor.
BMPR1A(+) ASCs show an enhanced ability for adipogenesis in vitro, as shown by gene expression and histological staining.
Duplication of 10q22.3-q23.3 encompassing BMPR1A gene is associated with congenital heart disease, microcephaly, and mild intellectual disability
Authors analyzed human databases from TCGA and survival data from microarrays to confirm BMPR1a tumor promoting functions, and found that high BMPR1a gene expression correlates with decreased survival regardless of molecular breast cancer subtype.
About half of BMPR1A-related polyps displayed loss of heterozygosity, predominantly in the epithelial compartment, compatible with BMPR1A acting as a tumour suppressor gene.
Results support a novel role for miR-885-3p in tumor angiogenesis by targeting BMPR1A, which regulates a proangiogenic factor.
findings suggest that GJA1 may be one of the downstream targets of BMPR1A signaling in osteoclasts that mediates osteoclast-osteoblast communication during bone remodeling.
deletion of BMPR1a in oncogenic astrocytes resulted in decreased proliferation, decreased invasion, decreased migration, and increased expression of stemness markers
different levels of expression and subsequent activation of Smad (show SMAD1 Proteins) signaling differentially contribute each BMP type I receptor to BMP-Smad (show SMAD1 Proteins) signaling and craniofacial development.
BMP signaling mediated by coordination of ALK2/ACVR1 (show ACRV1 Proteins), ALK3/BMPR1A, and BMPR2 (show BMPR2 Proteins) is an essential proangiogenic cue for retinal vessels.
Gonadotrope-specific Bmpr1a knockout animals developed normally and had reproductive organ weights comparable with those of controls. Knockouts were fertile, with normal serum gonadotropins and pituitary gonadotropin subunit mRNA expression. Cre-mediated recombination of the floxed Bmpr1a allele was efficient and specific, as indicated by PCR analysis of diverse tissues and isolated gonadotrope cells.
CK2.1 peptide drives chondrogenesis and cartilage formation without induction of chondrocyte hypertrophy by releasing CK2 (show CSNK2A1 Proteins) from distinct sites at BMPRIa
These results suggest that Pax8 (show PAX8 Proteins) maybe the downstream molecule of ALK3, it mediates the murine heart development via cellular senescence, which may serve as a mechanism that compensates for the cell loss via apoptosis in heart development.
study suggested that Bmpr-Ia and Bmpr-Ib (show BMPR1B Proteins) signaling regulates tooth formation via miR (show MLXIP Proteins)-135a.
integrin alpha1beta1/BMPR IA may block BMP-2 (show BMP2 Proteins)/BMPR IA complex information and interfere with the BMP-2 (show BMP2 Proteins) signalling pathway in cells
signaling via activin-like kinase 3 (ALK3/BMPR1A), a BMP type 1 receptor, is necessary for blastocyst attachment.
Report temporal regulation of BMPR1a mRNA expression in the oocyte, granulosa and theca cells of developing preovulatory follicles in the pig.
ALK3 and ALK6 (show BMPR1B Proteins) both contribute to the gene regulatory network that regulates dorso-ventral patterning.
Data show that USP15 (show USP15 Proteins) enhances BMP-induced phosphorylation of SMAD1 (show SMAD1 Proteins) by interacting with and deubiquitylating ALK3.
The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the activin receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas and activins transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.
, BMP type-1A receptor
, activin A receptor, type II-like kinase 3
, activin receptor-like kinase 3
, bone morphogenetic protein receptor type-1A
, serine/threonine-protein kinase receptor R5
, BMP-2/BMP-4 receptor
, bone morphogenetic protein 4 receptor
, bone morphogenetic protein receptor, type 1A
, BMP receptor 1
, bone morphogenic protein receptor 1
, protein kinase
, bone morphogenetic protein receptor IA
, bone morphogenetic protein receptor, type IA
, bone morphogenetic protein receptor type-1A-like
, BMP receptor
, bone morphogenetic protein receptor type IA