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

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

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

http://www.wikidata.org/entity/Q24653867

about

Latent myostatin has significant activity and this activity is controlled more efficiently by WFIKKN1 than by WFIKKN2 Fibrillin-1 and -2 differentially modulate endogenous TGF-β and BMP bioavailability during bone formation The pro-form of BMP-2 interferes with BMP-2 signalling by competing with BMP-2 for IA receptor binding Genetic and functional linkage between ADAMTS superfamily proteins and fibrillin-1: a novel mechanism influencing microfibril assembly and function Fine-tuned shuttles for bone morphogenetic proteins Abnormal Activation of BMP Signaling Causes Myopathy in Fbn2 Null Mice Structure of bone morphogenetic protein 9 procomplex Processing of anti-mullerian hormone regulates receptor activation by a mechanism distinct from TGF-beta.Biogenesis and function of fibrillin assemblies.Bone matrix to growth factors: location, location, location Two distinct regions of latency-associated peptide coordinate stability of the latent transforming growth factor-beta1 complex.Fibrillin assemblies: extracellular determinants of tissue formation and fibrosis Prodomains of transforming growth factor beta (TGFbeta) superfamily members specify different functions: extracellular matrix interactions and growth factor bioavailability.Loss of BMPR2 leads to high bone mass due to increased osteoblast activity The prodomain of BMP4 is necessary and sufficient to generate stable BMP4/7 heterodimers with enhanced bioactivity in vivo Fibrillin-containing microfibrils are key signal relay stations for cell function.Rapid Activation of Bone Morphogenic Protein 9 by Receptor-mediated Displacement of Pro-domains.A large bioactive BMP ligand with distinct signaling properties is produced by alternative proconvertase processing.Extracellular Regulation of Bone Morphogenetic Protein Activity by the Microfibril Component Fibrillin-1.Extracellular microfibrils in vertebrate development and disease processes.Extracellular microfibrils: contextual platforms for TGFbeta and BMP signaling.The extracellular regulation of bone morphogenetic protein signaling.Stromal Modulators of TGF-β in Cancer.The Prodomain-bound Form of Bone Morphogenetic Protein 10 Is Biologically Active on Endothelial Cells.Regulation of the Bioavailability of TGF-β and TGF-β-Related Proteins.Structural Biology and Evolution of the TGF-β Family Conditional deletion of BMP7 from the limb skeleton does not affect bone formation or fracture repair.Different requirements for proteolytic processing of bone morphogenetic protein 5/6/7/8 ligands in Drosophila melanogaster Activin A binds to perlecan through its pro-region that has heparin/heparan sulfate binding activity.A common biosynthetic pathway governs the dimerization and secretion of inhibin and related transforming growth factor beta (TGFbeta) ligands In vitro evaluation of TAT-OP1 osteogenic properties and prospects for in vivo applications.The cartilage-specific lectin C-type lectin domain family 3 member A (CLEC3A) enhances tissue plasminogen activator-mediated plasminogen activation.Alternative cleavage of the bone morphogenetic protein (BMP), Gbb, produces ligands with distinct developmental functions and receptor preferences.Tolloid cleavage activates latent GDF8 by priming the pro-complex for dissociation.You're going to need a bigger (glass bottom) boat.

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P2860

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

http://www.wikidata.org/entity/Q24653867

description

2008 nî lūn-bûn

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2008 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

A new model for growth factor ...... e with the prodomain for BMP-7

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A new model for growth factor ...... e with the prodomain for BMP-7

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A new model for growth factor ...... e with the prodomain for BMP-7

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type

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A new model for growth factor ...... e with the prodomain for BMP-7

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A new model for growth factor ...... e with the prodomain for BMP-7

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A new model for growth factor ...... e with the prodomain for BMP-7

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A new model for growth factor ...... e with the prodomain for BMP-7

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A new model for growth factor ...... e with the prodomain for BMP-7

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A new model for growth factor ...... e with the prodomain for BMP-7

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J.JMB.2008.06.074

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Journal of Molecular Biology

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A new model for growth factor ...... e with the prodomain for BMP-7

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Gerhard Sengle

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Karen M Lyons

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Lynn Y Sakai

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Robert N Ono

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P2860

Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis

Latent transforming growth factor beta-binding protein 1 interacts with fibrillin and is a microfibril-associated protein

Regulation of myostatin activity and muscle growth

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

Proteolytic activation of latent transforming growth factor-beta from fibroblast-conditioned medium

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly

Type I receptor binding of bone morphogenetic protein 6 is dependent on N-glycosylation of the ligand

Targeting of bone morphogenetic protein growth factor complexes to fibrillin

The integrin alpha v beta 6 binds and activates latent TGF beta 1: a mechanism for regulating pulmonary inflammation and fibrosis

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Hans Peter Bächinger

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