A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling.
about
Krüppel-like factor 15 regulates BMPER in endothelial cellsThe role of chordin fragments generated by partial tolloid cleavage in regulating BMP activitySystems control of BMP morphogen flow in vertebrate embryosBinding between Crossveinless-2 and Chordin von Willebrand factor type C domains promotes BMP signaling by blocking Chordin activity.Low-Density Lipoprotein Receptor-Related Protein-1 Signaling in Angiogenesis.BMPER-induced BMP signaling promotes coronary artery remodeling.Bone morphogenetic protein 2: a potential new player in the pathogenesis of diabetic retinopathyBMPER mutation in diaphanospondylodysostosis identified by ancestral autozygosity mapping and targeted high-throughput sequencing.The role of glypicans in Wnt inhibitory factor-1 activity and the structural basis of Wif1's effects on Wnt and Hedgehog signaling.A gene panel, including LRP12, is frequently hypermethylated in major types of B-cell lymphoma.Simultaneous rather than ordered cleavage of two sites within the BMP4 prodomain leads to loss of ligand in miceRegulation of bone morphogenetic protein 9 (BMP9) by redox-dependent proteolysis.Nanoscale structure of the BMP antagonist chordin supports cooperative BMP bindingCrimpy enables discrimination of presynaptic and postsynaptic pools of a BMP at the Drosophila neuromuscular junctionSpemann's organizer and the self-regulation of embryonic fieldsSortilin associates with transforming growth factor-beta family proteins to enhance lysosome-mediated degradation.Bone morphogenetic protein endothelial cell precursor-derived regulator regulates retinal angiogenesis in vivo in a mouse model of oxygen-induced retinopathy.The prodomain of BMP4 is necessary and sufficient to generate stable BMP4/7 heterodimers with enhanced bioactivity in vivoBMPER Promotes Epithelial-Mesenchymal Transition in the Developing Cardiac Cushions.Crossveinless d is a vitellogenin-like lipoprotein that binds BMPs and HSPGs, and is required for normal BMP signaling in the Drosophila wingBone morphogenetic protein modulator BMPER is highly expressed in malignant tumors and controls invasive cell behavior.Osteoblast-like differentiation of cultured human coronary artery smooth muscle cells by bone morphogenetic protein endothelial cell precursor-derived regulator (BMPER)Coevolutionary patterning of teeth and taste budsBmper inhibits endothelial expression of inflammatory adhesion molecules and protects against atherosclerosis.The Pitx2:miR-200c/141:noggin pathway regulates Bmp signaling and ameloblast differentiation.BMPER regulates cardiomyocyte size and vessel density in vivo.Stiffness-dependent cellular internalization of matrix-bound BMP-2 and its relation to Smad and non-Smad signaling.Proteoglycan signaling co-receptors: roles in cell adhesion, migration and invasion.The extracellular regulation of bone morphogenetic protein signaling.Bone Morphogenetic Protein functions as a context-dependent angiogenic cue in vertebrates.BMPs are mediators in tissue crosstalk of the regenerating musculoskeletal system.BMP growth factor signaling in a biomechanical context.The role of BMPs in endothelial cell function and dysfunction.BMPER variants associated with a novel, attenuated subtype of diaphanospondylodysostosis.Trans-system mechanisms against ischemic myocardial injury.Agonists and Antagonists of TGF-β Family Ligands.Bone Morphogenetic Protein-Modulator BMPER Regulates Endothelial Barrier Function.Inhibition of BMP activity protects epithelial barrier function in lung injury.LRP1-dependent endocytic mechanism governs the signaling output of the bmp system in endothelial cells and in angiogenesisOrganism-scale modeling of early Drosophila patterning via bone morphogenetic proteins
P2860
Q24317601-A593C58F-265C-44D0-9AA8-FDE63FE9DEC0Q26777732-35095A32-6B89-4429-9E6C-B1F3A70B86E6Q27013995-25C4B3DB-7D60-4DF7-AA5C-A5B062F04FD5Q33707750-768DFD09-1B11-47A7-9441-035FE4750498Q33710801-F2B0AF90-0664-4B6B-BAE4-FEA13669345AQ33954831-7D8AD68F-5FBD-49CE-AA44-144FA4099960Q34005734-AEB05B30-C2A1-47A9-9DA6-BBBA158FC24EQ34139959-662F6A08-6DD9-45E7-9970-EF9E57D786EEQ34181382-D6D8CE2B-6795-4BAE-9DB6-28A6A99719B2Q34194620-20C02CF0-F6A4-4D59-98FC-2323977FE147Q34341692-2909162D-9A46-4557-B5C2-4F4009502118Q34467523-032C1E3A-1D59-43D4-982A-9F794799323EQ34583690-23443896-883F-4816-BE88-F810B6583B1CQ34820237-E8F07131-B0B3-4B52-8005-D21524C1896CQ35001381-0CEF0437-94B1-4B38-836D-56FE8003FBACQ35065290-54E518FE-0F07-46B2-A720-D2EF9083435CQ35250759-97670F98-6F65-4B1B-B5EF-184521DBA429Q35590158-9177CC6B-E378-4AEB-B89C-0E6E1FBDF143Q35791889-DF1A13CC-7990-44D1-8D42-A25F0DEFD2BAQ35978899-BB2550C3-57B3-4708-BD5D-6A372B2143D3Q36035290-619B7FB9-DDBF-4F5D-A0C8-A7B55CD6AE9CQ36216361-F0E270A1-B0CD-4C8B-9203-480259E2BA1DQ36268737-203B81F6-70AF-4AA3-AA8D-F5081C9CCC05Q36445238-BD4B5534-B03F-468D-B675-1AF192B3D082Q37080787-EF21D7BE-7172-4EEE-8C77-E5D0AC18DAD2Q37265279-60C3B0FD-ACE5-43B2-A644-E7DC789CE409Q37420513-F42A77A7-1ADB-4FBB-A398-32EE2094AECCQ37475741-0E65C369-2D0F-499B-871B-99C6D13B52E2Q37621158-D78088C1-0F53-4E71-92EF-282406285098Q37947050-D56F456E-99FA-4FF4-9419-F1147DF2E116Q37983414-6346BB68-25C5-4FAF-80F4-F275F17F115EQ38152403-3E6EA655-BBAE-40A5-92D5-C09CB64FF8D0Q38218507-116FDA40-BD46-46E0-9DA8-053AE51C0373Q38295986-915D2EC6-B8BE-4E8B-B509-C3762CBD6B6AQ38318626-543C39D6-1CF5-4CF1-82BF-4975F4AFA21AQ38896053-6C7CC10D-1D1D-4FAF-B3F0-38C56928D937Q39084965-0B6C46F5-C1B2-4430-A275-CF30ADE207F9Q39146360-0F66C5F1-3868-4E11-A0CF-B6094727B25DQ39317513-BCADBFF0-D2D9-489B-97B2-75E5865EAE50Q39870985-34250D9D-05A7-42BE-807F-81CC32E6A8C0
P2860
A concentration-dependent endocytic trap and sink mechanism converts Bmper from an activator to an inhibitor of Bmp signaling.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 16 February 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
A concentration-dependent endo ...... an inhibitor of Bmp signaling.
@en
A concentration-dependent endo ...... an inhibitor of Bmp signaling.
@nl
type
label
A concentration-dependent endo ...... an inhibitor of Bmp signaling.
@en
A concentration-dependent endo ...... an inhibitor of Bmp signaling.
@nl
prefLabel
A concentration-dependent endo ...... an inhibitor of Bmp signaling.
@en
A concentration-dependent endo ...... an inhibitor of Bmp signaling.
@nl
P2093
P2860
P356
P1476
A concentration-dependent endo ...... an inhibitor of Bmp signaling.
@en
P2093
Cam Patterson
Isabel Moreno
Liliana Attisano
Malcolm Ross
Martin Moser
Monika Podkowa
Monte Willis
Rongqin Ren
Rusty Kelley
Xinchun Pi
P2860
P304
P356
10.1083/JCB.200808064
P407
P577
2009-02-16T00:00:00Z