The extracellular regulation of bone morphogenetic protein signaling. - Wikidata - wikimedia - TriplyDB

The extracellular regulation of bone morphogenetic protein signaling.

The extracellular regulation of bone morphogenetic protein signaling.

http://www.wikidata.org/entity/Q37621158

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The BMP antagonist follistatin-like 1 is required for skeletal and lung organogenesis BMP signaling components in embryonic transcriptomes of the hover fly Episyrphus balteatus (Syrphidae)Primordial germ cells in mice Making models match measurements: model optimization for morphogen patterning networks Heparan sulfate in skeletal development, growth, and pathology: the case of hereditary multiple exostoses Systems control of BMP morphogen flow in vertebrate embryos Fine-tuned shuttles for bone morphogenetic proteins Promotion of bone morphogenetic protein signaling by tetraspanins and glycosphingolipids Caenorhabditis elegans SMA-10/LRIG is a conserved transmembrane protein that enhances bone morphogenetic protein signaling Anterograde Activin signaling regulates postsynaptic membrane potential and GluRIIA/B abundance at the Drosophila neuromuscular junction In silico Mechano-Chemical Model of Bone Healing for the Regeneration of Critical Defects: The Effect of BMP-2 The role of inflammatory and anti-inflammatory cytokines in the pathogenesis of osteoarthritis.Binding between Crossveinless-2 and Chordin von Willebrand factor type C domains promotes BMP signaling by blocking Chordin activity.Signaling pathways in cartilage repair.CD44 and hyaluronan promote the bone morphogenetic protein 7 signaling response in murine chondrocytes.Efficient reverse-engineering of a developmental gene regulatory network.Inhibition of bone morphogenetic proteins protects against atherosclerosis and vascular calcification.ID family protein expression and regulation in hypoxic pulmonary hypertension.Efficient calculation of steady state probability distribution for stochastic biochemical reaction network.Development of Physiologically Based Pharmacokinetic Model (PBPK) of BMP2 in Mice.Expression and functional study of extracellular BMP antagonists during the morphogenesis of the digits and their associated connective tissues.Notch and PKC are involved in formation of the lateral region of the dorso-ventral axis in Drosophila embryos.Crimpy inhibits the BMP homolog Gbb in motoneurons to enable proper growth control at the Drosophila neuromuscular junction Spatiotemporal delivery of bone morphogenetic protein enhances functional repair of segmental bone defects.Extracellular movement of signaling molecules.Anterior segment alterations and comparative aqueous humor proteomics in the buphthalmic rabbit (an American Ophthalmological Society thesis).Regulation of BMP activity and range in Drosophila wing development Crossveinless d is a vitellogenin-like lipoprotein that binds BMPs and HSPGs, and is required for normal BMP signaling in the Drosophila wing Crossveinless 2 regulates bone morphogenetic protein 9 in human and mouse vascular endothelium.Bone morphogenetic protein modulator BMPER is highly expressed in malignant tumors and controls invasive cell behavior.Multistep molecular mechanism for bone morphogenetic protein extracellular transport in the Drosophila embryo The Gyc76C Receptor Guanylyl Cyclase and the Foraging cGMP-Dependent Kinase Regulate Extracellular Matrix Organization and BMP Signaling in the Developing Wing of Drosophila melanogaster.Bmp2 conditional knockout in osteoblasts and endothelial cells does not impair bone formation after injury or mechanical loading in adult mice.Differential diffusivity of Nodal and Lefty underlies a reaction-diffusion patterning system.Morphogen transport.The role of mathematical models in understanding pattern formation in developmental biology.Pentagone internalises glypicans to fine-tune multiple signalling pathways Extracellular Regulation of Bone Morphogenetic Protein Activity by the Microfibril Component Fibrillin-1.Perichondrium phenotype and border function are regulated by Ext1 and heparan sulfate in developing long bones: a mechanism likely deranged in Hereditary Multiple Exostoses.BMP Antagonist Gremlin 2 Limits Inflammation After Myocardial Infarction.

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P2860

The extracellular regulation of bone morphogenetic protein signaling.

http://www.wikidata.org/entity/Q37621158

description

2009 nî lūn-bûn

@nan

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh

2009年學術文章

@zh-hant

name

The extracellular regulation of bone morphogenetic protein signaling.

@en

The extracellular regulation of bone morphogenetic protein signaling.

@nl

type

label

The extracellular regulation of bone morphogenetic protein signaling.

@en

The extracellular regulation of bone morphogenetic protein signaling.

@nl

prefLabel

The extracellular regulation of bone morphogenetic protein signaling.

@en

The extracellular regulation of bone morphogenetic protein signaling.

@nl

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The extracellular regulation of bone morphogenetic protein signaling.

@en

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David Umulis

http://www.w3.org/2001/XMLSchema#string

Michael B O'Connor

http://www.w3.org/2001/XMLSchema#string

Seth S Blair

http://www.w3.org/2001/XMLSchema#string

P2860

DRAGON, a bone morphogenetic protein co-receptor

Glypican LON-2 is a conserved negative regulator of BMP-like signaling in Caenorhabditis elegans

Bone morphogenetic proteins signal through the transforming growth factor-beta type III receptor

BMPER is an endothelial cell regulator and controls bone morphogenetic protein-4-dependent angiogenesis

Biglycan is a new extracellular component of the Chordin-BMP4 signaling pathway

GDF11 forms a bone morphogenetic protein 1-activated latent complex that can modulate nerve growth factor-induced differentiation of PC12 cells

BMP-2 antagonists emerge from alterations in the low-affinity binding epitope for receptor BMPR-II

A new model for growth factor activation: type II receptors compete with the prodomain for BMP-7

The evolutionarily conserved BMP-binding protein Twisted gastrulation promotes BMP signalling

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3715-3728

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scholarly article

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10.1242/DEV.031534

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22

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136

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38034456

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19855014

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sequestering of BMP from receptor via BMP binding

sequestering of TGFbeta from receptor via TGFbeta binding

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2766339

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