Relevant bibliographies by topics / Bone morphogenetic proteins

Academic literature on the topic 'Bone morphogenetic proteins'

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Published: 4 June 2021
Last updated: 30 July 2024

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Journal articles on the topic "Bone morphogenetic proteins"

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Sharma, Anamika, and Himani Sharma. "Bone Morphogenetic Proteins: An Overview." Annals of Applied Bio-Sciences 4, no. 2 (April 10, 2017): R35—R37. http://dx.doi.org/10.21276/aabs.1336.

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Einhorn, Thomas A. "BONE MORPHOGENETIC PROTEINS." Journal of Bone & Joint Surgery 79, no. 2 (February 1997): 318. http://dx.doi.org/10.2106/00004623-199702000-00024.

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Einhorn, Thomas A. "Bone Morphogenetic Proteins." Journal of Bone and Joint Surgery (American Volume) 79, no. 2 (February 1997): 319. http://dx.doi.org/10.2106/00004623-199702000-00026.

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TERMAAT, M. F., F. C. DEN BOER, F. C. BAKKER, P. PATKA, and H. J. TH M. HAARMAN. "BONE MORPHOGENETIC PROTEINS." Journal of Bone and Joint Surgery-American Volume 87, no. 6 (June 2005): 1367–78. http://dx.doi.org/10.2106/00004623-200506000-00027.

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Katagiri, Takenobu, and Tetsuro Watabe. "Bone Morphogenetic Proteins." Cold Spring Harbor Perspectives in Biology 8, no. 6 (June 2016): a021899. http://dx.doi.org/10.1101/cshperspect.a021899.

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&NA;. "Bone Morphogenetic Proteins." Back Letter 25, no. 11 (November 2010): 125–26. http://dx.doi.org/10.1097/01.back.0000390600.95274.20.

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Chen, Di, Ming Zhao, and Gregory R. Mundy. "Bone Morphogenetic Proteins." Growth Factors 22, no. 4 (December 2004): 233–41. http://dx.doi.org/10.1080/08977190412331279890.

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Carreira, A. C., F. H. Lojudice, E. Halcsik, R. D. Navarro, M. C. Sogayar, and J. M. Granjeiro. "Bone Morphogenetic Proteins." Journal of Dental Research 93, no. 4 (January 3, 2014): 335–45. http://dx.doi.org/10.1177/0022034513518561.

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Wozney, John M. "Bone Morphogenetic Proteins." Progress in Growth Factor Research 1, no. 4 (January 1989): 267–80. http://dx.doi.org/10.1016/0955-2235(89)90015-x.

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Azari, Kodi, John S. Doctor, Bruce A. Doll, and Jeffrey O. Hollinger. "Bone morphogenetic proteins." Oral and Maxillofacial Surgery Clinics of North America 14, no. 1 (February 2002): 1–14. http://dx.doi.org/10.1016/s1042-3699(02)00011-0.

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Dissertations / Theses on the topic "Bone morphogenetic proteins"

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Thomas, Nicole. "Bone morphogenetic proteins and hair and wool follicle morphogenesis." Title page, contents and abstract only, 2002. http://web4.library.adelaide.edu.au/theses/09PH/09pht4592.pdf.

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Bibliography: leaves 119-135. A thesis which describes a study to establish the relative roles that the bone morphogenetic proteins BMP-2 and BMP-4 play in initiating hair and derived wool follicles by first establishing their expression patterns by in situ hybridisation and then manipulating them in vitro.
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Christison, Joseph George. "The role of bone morphogenetic proteins in otic specification /." Connect to title online (ProQuest), 2008. http://proquest.umi.com/pqdweb?did=1616787971&sid=1&Fmt=2&clientId=11238&RQT=309&VName=PQD.

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Thesis (Ph. D.)--University of Oregon, 2008.
Typescript. Includes vita and abstract. Includes bibliographical references (leaves 43-47). Also available online in ProQuest, free to University of Oregon users.
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Yin, Huiran. "Expression, purification, and characterization of the extracellular domain of human BMPR-II in solution : a dissertation /." San Antonio : UTHSC, 2007. http://proquest.umi.com/pqdweb?did=1436373301&sid=1&Fmt=2&clientId=70986&RQT=309&VName=PQD.

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Qualtrough, John David. "Bone morphogenetic proteins in human embryonal carcinoma cells." Thesis, University of Sheffield, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.311810.

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Mowbray, Catriona. "Bone morphogenetic proteins and zebrafish inner ear development." Thesis, University of Sheffield, 2002. http://etheses.whiterose.ac.uk/14716/.

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This thesis describes the mRNA expression patterns of the Bone Morphogenetic Proteins (BMPs), downstream members of the BMP signal pathway, BMP antagonists and candidate target genes in the developing inner ear of wild type zebrafish. The crista Bmp expression pattern is conserved between four vertebrate species. However, unlike in chick, mouse and Xenopus laevis none of the hmps examined are macula markers in zebrafish. This thesis identifies sources of Bmp signalling (the cristae, the endolymphatic duct (ED) and the semicircular canals (SCC)) and possible sites of Bmp action (the cristae, posterior macula, SCC and the mesenchyme around the ED). It also provides the first description of the early stages of ED development, a structure only recently described at later stages in the zebrafish (8dpf), and two mRNA markers of this structure (bmp4 and dachA). In analysis of zebrafish mutants with defective cristae, the presence of cristae correlated with the expression of the hmps and msxc, a putative Bmp target. This suggests the Bmps are required to form cristae and express msxc. Gain and loss of function studies have also supported a role for the Bmps in the development of the posterior macula and SCc. Ectopic hBMP4 protein was applied to the otic vesicle via protein-coated beads. This inhibited the development of the posterior macula and SCC. However, these hBMP4 beads were not sufficient to induce the expression of ectopic msxc, generate ectopic cristae or rescue crista development in mutants. Beads coated in a BMP antagonist did not affect the development of endogenous cristae or the expression of endogenous msxc. Rescued swirl (bmp2b) mutant adult zebrafish exhibit a balance defect. Early stages of inner ear development in rescued embryos were found to progress normally up until 7dpf. However, it is not clear when the rescuing mRNA or protein degrades, and work done by others in the lab has shown that Bmp2b is required at later stages to form adult SCc. The ectopic hBMP4 experiments suggest that moderating levels of Bmp signalling may be required for normal development of the SCC at early stages.
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Young, Julia, and n/a. "Bone morphogenetic proteins are involved in controlling mammalian fertility." University of Otago. Department of Biochemistry, 2008. http://adt.otago.ac.nz./public/adt-NZDU20090112.122706.

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Transforming growth factor beta (TGFβ) superfamily members are involved in controlling mammalian fertility. The largest subset of the TGFβ superfamily are the bone morphogenetic proteins (BMP). BMP ligands signal through the type I and II BMP receptors and utilise the Smads1/5/8 phosphorylation cascade to control gene expression in the cell nucleus. Although BMPs act through the same pathway, they have the ability to activate unique sets of genes dependant on the identity of the ligand. In this study, HEK293T cells were challenged with BMP ligands for four hours and gene expression profiles were compared using microarray technology. The genes upregulated in the presence of BMP2, BMP4, BMP6 and BMP7 play roles in cellular proliferation and differentiation. These functions are critical stages in the successful development of an ovarian follicle whilst undergoing folliculogenesis. All of the BMP ligands investigated in this study were also observed to upregulate the expression of a small group of common genes indicating that a shared regulatory pattern occurs within the BMP pathway. Of these genes, Smad6 and Smad7, inhibitor of DNA binding proteins 1-4 (ID 1-4), and msh homeobox homolog 2 (MSX2) were previously known BMP target genes. However, none of the remaining genes upregulated by all BMPs were previously shown to be BMP targets. The results from the microarray experiment were used as founding data for the in silico mining of novel genes not present on the array that may be differentially expressed in response to these ligands. The expression levels of several of the novel genes identified by in silico mining were then measured in vitro, however the results showed no differential expression in the HEK293T cells. To apply the knowledge of the microarray studies to the tissue of interest, eight genes were selected for assessment in ovine granulosa cells. Four of the genes upregulated in response to BMP6 in HEK293T cells were also differentially expressed in primary ovine granulosa cell cultures in response to BMP6 addition. The identification of several sheep breeds with mutations in TGFβ superfamily members has enabled investigations into the roles that specific TGFβ components play in controlling fertility. The highly fertile Booroola sheep has a substitution mutation in the type IB BMP receptor that results in an additive effect on ovulation rate. The Booroola mutation causes precocious maturation of ovarian follicles with fewer granulosa cells surrounding an enlarged oocyte, and carriers of the mutation have higher levels of circulating follicle stimulating hormone (FSH). BMPs have previously been shown to influence the regulation of FSH synthesis and secretion in the pituitary gland. In this study, primary pituitary cells were harvested and cultured from homozygous Booroola ewes and from wildtype ewes to determine if the mutation caused alterations in FSH secretion in vitro. The cells were collected 24 h following induction of luteolysis and cultured for 72 h prior to being challenged for 24 h with bone morphogenetic proteins (BMP2, BMP4, BMP6), growth and differentiation factor-9 (GDF9), transforming growth factor β1 (TGFβ1), activin-A and gonadotropin releasing hormone (GnRH). The levels of FSH and luteinising hormone (LH) were measured by radioimmunoassay and compared to the untreated controls. Primary pituitary cell cultures from Booroola ewes secreted less FSH than wildtype cells in the presence of BMP2, BMP4 and BMP6. These BMPs did not affect the FSH stores within the cells, or the levels of LH released. GDF9 appeared to act in a BMP-like manner by suppressing FSH secretion. The BMPRIB receptor however, was not found to co-localise with gonadotroph cells in either Booroola or wildtype pituitary tissues. These findings imply that the increased sensitivity of Booroola cells to BMP2, BMP4, BMP6, and GDF9 cannot be due to the direct action of the BMPRIB mutant Booroola receptor in the cells that synthesize FSH. The alternative type I BMP receptor to BMPRIB that can act in BMP signal transduction is BMPRIA. This receptor was also not found in gonadotroph cells of wildtype orBooroola ewes This is in contrast to findings in other flocks which have been shown to express BMPRIA in gonadotroph cells. This study has identified unique sets of differentially regulated genes in response to BMP-2, 4, 6, and 7 as well as TGFβ1 in a human HEK293T cell culture system. Among the differentially expressed genes, a common set of 12 genes were upregulated by all BMP ligands. None of these genes were present in the TGFβ1 set. Selected genes were validated in ovine primary granulosa cell cultures, showing that the human cell culture system functions similarly to cells of biologial relevance in fertility. Within the pituitary gland, BMPs are shown to influence FSH secretion. The presence of the Booroola mutation enhances the BMP effects on gonadotroph cells, however the lack of BMPRIB on gonadotroph cells indicates that the effects are indirect.
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Mace, Peter, and n/a. "Biochemistry of ovine bone and morphogenetic proteins and receptors." University of Otago. Department of Biochemistry, 2006. http://adt.otago.ac.nz./public/adt-NZDU20070508.133410.

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The transforming growth factor (TGF)-β superfamily mediates a wide range of differentiation and developmental processes across many genera. GDF9 and BMP15 are expressed exclusively in the mammalian ovary and are the only TGF-β ligands that lack the conserved cysteine residue used for dimerisation. As a platform for studying the interactions between GDF9 and BMP15 and their receptors, BMPRII and BMPRIb, a variety of strategies were attempted to produce soluble and active proteins from recombinant systems. Both ligands and receptors showed a tendency to form insoluble aggregates when expressed in prokaryotic systems; however after extensive screening, quantities of biologically active GDF9 were produced using in vitro refolding. When expressed alone, either containing a histidine tag or as an untagged protein, the BMPRII ectodomain was deposited as insoluble inclusion bodies. This protein, subjected to in vitro refolding procedures, exhibited multiple species following anion exchange chromatography and size exclusion chromatography, as visualised on native PAGE. Separation of these species could be achieved using a MonoP matrix. One of these separated fractions, representing about 5% of the starting material, was amenable to crystallisation, and furthermore exhibited activity in a rat granulosa cell thymidine incorporation assay. Two different crystals forms of the extracellular domain of BMPRII were grown from the same protein batch under similar crystallisation conditions. Notably, the tetragonal form that grew more slowly possessed several disordered finger regions, while electron density for the entire molecule was clear in the orthorhombic form. The hydrophobic core of the ligand binding surface of BMPRII , as seen in both structures, resembles that of ActRII bound to BMP2. The A-loop of BMPRII, which is involved in ligand binding, lies in two different conformations in the two structures of BMPRII, mediated by a rearrangement in disulfide Cys94-Cys117. It is proposed here that the tetragonal form represents the ligand-bound receptor structure. Although the majority of the hydrophobic binding surface is shared with ActRII(b), it is likely that His87 and Tyr40 are unique residues that confer specificity in BMPRII ligand binding.
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Wise, Sarah B. "Bone morphogenetic proteins in teleost tooth development and evolution." Connect to online resource, 2007. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3256386.

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Dootson, Gina Elizabeth. "Pro-osteogenic effects of follistatin on bone morphogenetic proteins." Thesis, University of York, 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.437559.

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Al-Hourani, Kinda. "Antiviral functions of bone morphogenetic proteins and the activins." Thesis, University of Oxford, 2015. https://ora.ox.ac.uk/objects/uuid:579bda45-7f98-447d-b2d7-0565a00d8995.

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Previous work in the Drakesmith lab has revealed a novel anti-HCV function of bone morphogenetic protein 6 (BMP6), a TGFβ-superfamily cytokine unrelated to type I IFN. Recombinant BMP6 is antiviral against both replication-competent HCV and a full-length genomic replicon model. Data presented in this thesis demonstrate that an anti-HCV effect extends to multiple BMPs and segregates with ability to ligate the type I BMP receptor. Canonically, the type I BMP receptor signals intracellularly via phosphorylation of SMAD1/5/8 transcription factors. Prior work in the lab shows that BMP6 exerts both type I IFN-dependent and type I IFN-independent antiviral effects. In terms of delineating mechanistic basis for the latter, we have formulated a model whereby BMP6 induces cell cycle arrest in phases characterized by reduced cytosolic nucleotide availability, and which are therefore less permissive to viral replication. A recent report indicates that another TGFβ-type cytokine, activin B, is able to signal through a nonclassical type I BMP receptor dependent mechanism. Activin A and B have multiple established roles in innate immunity and inflammatory responses. However, no direct link between activin A and B and the early response to viral infection has been described. Given their "immune precedent" within the literature, and their high level of structural and phylogenetic homology to the BMPs, both activin A and B represented promising candidates to explore for an antiviral effect. Our data indicate that activin A mRNA, encoded by the INHBA gene, is induced upon activation of RIG-I, MDA5 and TLR7/8 viral nucleic acid sensors in vitro, across multiple cell lines and also in PBMCs. In vitro infection of A549 lung adenocarcinoma-derived cells and Huh7 hepatoma-derived cells with the murine paramyxovirus Sendai Virus also elicits robust INHBA induction. In vitro dengue virus infection also elicits INHBA upregulation by Huh7.5 hepatoma cells. In vivo, infection of mice with influenza A PR8 also elicits induction of activin A message within the lung. Treatment of Huh7 cells with activin A increases transcription of multiple type I IFN transduction elements; moreover, co-incubation of Huh7 cells with IFNa and either activin A or B augments transcriptional induction of key anti-HCV enzymes. This boosting of type I IFN extends to a functional enhancement: activin A elicits a synergistic, dose-dependent enhancement of both type I and type III IFN's antiviral effect against a full-length HCV genomic replicon. In a full-length genomic replicon model of HCV, both activin A and B alone exert a potent, dose-dependent antiviral effect that is contingent upon signalling via type I BMP receptor. A component of the activins' antiviral effect does not require intact type I IFN signalling. A small-molecule inhibitor of signalling downstream of type I IFN receptor blocks the anti-HCV effect of IFNa but does not impair the antiviral effects of activin A. Both BMP6 and activin A exert dose-dependent antiviral effects against Hepatitis B Virus infection in vitro. Of note, SMAD1/5/8-binding sites have been identified in the promoter sequences of multiple antiviral Interferon Stimulated Genes (ISG), providing a possible route for the enhancement of ISG induction by the SMAD1/5/8 axis. Furthermore, strong topological homology exists between of the transactivation domains of the SMADs and Interferon Response Factors (IRF), which postulated to have diverged from a common ancestor in early metazoans. Preliminary bioinformatic analyses reveal striking parallels between the genome-wide binding profiles of activated SMAD1 and IRF1, including proximal to genes encoding antiviral effectors. The observations presented in this study may represent the first characterization of a non-IFN intracellular antiviral response in human cells, with implications for the development of targeted therapies against diverse viral diseases. Moreover, these data reveal a novel facet of activin biology, in addition to in part elucidating the nature of the genomic interactions between BMP-SMAD and IFNIRF signalling.
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Books on the topic "Bone morphogenetic proteins"

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Rogers, Melissa B., ed. Bone Morphogenetic Proteins. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-8904-1.

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Vukicevic, Slobodan, and Kuber T. Sampath, eds. Bone Morphogenetic Proteins. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8121-0.

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Vukicevic, Slobodan, and Kuber T. Sampath, eds. Bone Morphogenetic Proteins: Systems Biology Regulators. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-47507-3.

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Vukicevic, Slobodan, and Kuber T. Sampath, eds. Bone Morphogenetic Proteins: Regeneration of Bone and Beyond. Basel: Birkhäuser Basel, 2004. http://dx.doi.org/10.1007/978-3-0348-7857-9.

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Sam, Lindholm T., ed. Advances in skeletal reconstruction using bone morphogenetic proteins. River Edge, NJ: World Scientific, 2002.

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1951-, Vukicevic Slobodan, and Sampath Kuber T, eds. Bone morphogenetic proteins: From local to systemic therapeutics. Basel: Birkhäuser, 2008.

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Vukicevic, Slobodan, and Kuber T. Sampath, eds. Bone Morphogenetic Proteins: From Local to Systemic Therapeutics. Basel: Birkhäuser Basel, 2008. http://dx.doi.org/10.1007/978-3-7643-8552-1.

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Sam, Lindholm T., ed. Bone morphogenetic proteins: Biology, biochemistry and reconstructive surgery. San Diego, Calif: Academic Press, 1996.

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name, No. Advances in skeletal reconstruction using bone morphogenetic proteins. Singapore: World Scientific, 2003.

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McKay, William F. The rhBMP-2 reference guide. St. Louis, Mo: Quality Medical Pub., 2002.

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Book chapters on the topic "Bone morphogenetic proteins"

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Wozney, J. M., and V. Rosen. "Bone Morphogenetic Proteins." In Physiology and Pharmacology of Bone, 725–48. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77991-6_20.

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Bomback, David A., and Jonathan N. Grauer. "Bone Morphogenetic Proteins." In Progress in Neurological Surgery, 52–64. Basel: KARGER, 2005. http://dx.doi.org/10.1159/000084423.

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Brazil, Derek P. "Bone Morphogenetic Proteins." In Encyclopedia of Molecular Pharmacology, 1–9. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-21573-6_5292-1.

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Brazil, Derek P. "Bone Morphogenetic Proteins." In Encyclopedia of Molecular Pharmacology, 346–53. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-57401-7_5292.

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Rueger, David C. "Biochemistry of bone morphogenetic proteins." In Bone Morphogenetic Proteins, 1–18. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8121-0_1.

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Giltaij, Lex R., Andrew Shimmin, and Gary E. Friedlaender. "Osteogenic protein-1 (OP-1) in the repair of bone defects and fractures of long bones: clinical experience." In Bone Morphogenetic Proteins, 193–205. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8121-0_10.

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Patel, Tushar Ch, Jonathan N. Grauer, and Jonathan S. Erulkar. "Evaluation of OP-1 in a rabbit model of lumbar fusions." In Bone Morphogenetic Proteins, 207–22. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8121-0_11.

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Luyten, Frank P., Rik Lories, Dirk De Valck, Cosimo De Bari, and Francesco Dell’Accio. "Bone morphogenetic proteins and the synovial joints." In Bone Morphogenetic Proteins, 223–48. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8121-0_12.

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Jelic, Mislav, Marko Pecina, Miroslav Haspl, Anton Brkic, and Slobodan Vukicevic. "BMPs in articular cartilage repair." In Bone Morphogenetic Proteins, 249–62. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8121-0_13.

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Borovecki, Fran, Nikolina Basic, Mislav Jelic, Dunja Rogic, Haimanti Dorai, Ana Stavljenic-Rukavina, Kuber T. Sampath, and Slobodan Vukicevic. "The role of bone morphogenetic proteins in kidney development and repair." In Bone Morphogenetic Proteins, 263–88. Basel: Birkhäuser Basel, 2002. http://dx.doi.org/10.1007/978-3-0348-8121-0_14.

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Conference papers on the topic "Bone morphogenetic proteins"

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Jonigk, Danny, Kais Hussein, Katharina Theophile, Marlene Merk, Lavinia Maegel, Jens Gottlieb, Stefan Fischer, et al. "Aberrant Expression Of Bone Morphogenetic Proteins In Fibrotic Airway Remodelling." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2083.

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Clausen, Kathryn A., Xiumin Di, Frank M. Torti, and Suzy V. Torti. "Abstract 3253: Bone morphogenetic proteins increase hepcidin in breast cancer cells." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3253.

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Owens, Philip, Hannah Polikowsky, Michael W. Pickup, Lauren A. Matise, Agnes E. Gorska, Aubie K. Shaw, Sergey V. Novitskiy, Mary E. Aakre, Charles C. Hong, and Harold L. Moses. "Abstract 1500: Bone morphogenetic proteins stimulate mammary fibroblasts to promote mammary tumorigenesis." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-1500.

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Chung, Eunna, and Marissa Nichole Rylander. "Effects of Growth Factors and Stress Conditioning on the Induction of Heat Shock Proteins and Osteogenesis." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206662.

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Tissue engineering is an emerging field that focuses on development of methods for repairing and regenerating damaged or diseased tissue. Successful development of engineered tissues is often limited by insufficient cellular proliferation and insufficient formation of extracellular matrix. To induce effective bone regeneration, many research groups have investigated the cellular response and capability for tissue regeneration associated with bioreactor conditions and addition of growth factors [1]. Bioreactors in tissue engineering have been developed to expose cells to a similar stress environment as found within the body or induce elevated stress levels for potential induction of specific cellular responses associated with tissue regeneration. Native bone encounters a diverse array of dynamic stresses such as shear, tensile, and compression daily. Stress conditioning protocols in the form of thermal or tensile stress have been shown to induce up-regulation of molecular chaperones called heat shock proteins (HSPs) and bone-related proteins like MMP13 (matrix metallopeptidase 13) [2] and OPG (osteoprotegerin) [3, 4]. HSPs have important roles in enhancing cell proliferation and collagen synthesis. Osteogenic growth factors such as TGF-β1 (transforming growth factor beta 1) and BMP-2 (bone morphogenetic protein 2) are related to bone remodeling and osteogenesis as well as HSP induction [5]. Therefore, identification of effective preconditioning using growth factors and stress protocols that enhance HSP expression could substantially advance development of bone regeneration. The purpose of this research was to identify preconditioning protocols using osteogenic growth factors and tensile stress applied through a bioreactor system to enhance expression of HSPs and bone-related proteins while minimizing cellular injury for ultimate use for bone regeneration.
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Holtzhausen, Alisha, Tam How, Bradley C. Gersh, and Gerard C. Blobe. "Abstract 3035: Bone morphogenetic proteins signal through Smad2 and Smad3 to regulate cell migration and proliferation." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3035.

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Owens, Philip, Agniesszka E. Gorska, Mary E. Aakre, and Harold L. Moses. "Abstract 3840: Bone morphogenetic proteins require the type II TGFβ receptor for growth arrest in mammary tumor cells." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3840.

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Pinheiro, Antonio Luiz B., Gilberth T. S. Aciole, Luiz G. P. Soares, Neandder A. Correia, and Jean N. dos Santos. "Effects of LED phototherapy on bone defects grafted with MTA, bone morphogenetic proteins, and guided bone regeneration in a rodent model: a description of the bone repair by light microscopy." In SPIE BiOS, edited by Michael R. Hamblin, Ronald W. Waynant, and Juanita Anders. SPIE, 2011. http://dx.doi.org/10.1117/12.875836.

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Kosacka, Monika, Monika Chaszczewska, Elzbieta Wisniewska, Katarzyna Bogunia-Kubik, and Anna Brzecka. "Late Breaking Abstract - Decreased thrombospondin-1 and bone morphogenetic protein-4 serum levels in non-small-cell lung cancer and the relationship of these proteins with the stage of the disease." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa4196.

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Drexler, S., C. Chai, H. Gaitantzi, M. Ebert, and K. Breitkopf-Heinlein. "Fettlebererkrankung: protektive Rolle von Bone Morphogenetic Protein (BMP)-9?" In Viszeralmedizin 2019. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1695352.

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Liang, Kun, Xiaocheng Li, and Beng Kang Tay. "Large diameter TiO2 nanotube fabrication for bone morphogenetic protein delivery." In 2011 IEEE 4th International Nanoelectronics Conference (INEC). IEEE, 2011. http://dx.doi.org/10.1109/inec.2011.5991774.

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Reports on the topic "Bone morphogenetic proteins"

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Reddi, A. H. Bone Morphogenetic Proteins, Antagonists and Receptors in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, January 2005. http://dx.doi.org/10.21236/ada433874.

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Kim, Isaac. Neuroendocrine Differentiation in Prostate Cancer: Role of Bone Morphogenetic Protein-6 and Macrophages. Fort Belvoir, VA: Defense Technical Information Center, July 2011. http://dx.doi.org/10.21236/ada555480.

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López-Valverde, Nansi, Javier Aragoneses, Antonio López-Valverde, Cinthia Rodríguez, and Juan Manuel Aragoneses. Role in the osseointegration of titanium dental implants, of bioactive surfaces based on biomolecules: A systematic review and meta-analysis of in vivo studies. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, June 2022. http://dx.doi.org/10.37766/inplasy2022.6.0076.

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Abstract:
Review question / Objective: Does the bioactive surface of titanium dental implants, based on biomolecules, influence osseointegration?. The aim of our study was to evaluate the role and efficacy of bioactive surfaces in osseointegration. Our review study limited the research interest to titanium dental implants coated with a biomolecule, i.e., an organic molecule produced by a living organism. Condition being studied: In recent years, much attention has been paid to topographical modifications of dental implant surfaces, as well as to their coating with biologically active substances.a bioactive surface is one capable of achieving faster and higher quality osseointegration, shortening waiting times and solving situations of poor bone quality. Molecules that can be applied for bioactive purposes include bioceramics, ions and biomolecules. Collagen and bone morphogenetic protein have been suggested as bone stimulating agents. Biofunctionalization of the implant surface with a biomimetic active peptide has also been shown to result in a significant increase in bone-to-implant ratios and an increase in peri-implant bone density.
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