The abstract directly reports human BMP2 dimer complexed with two BMPR1A ectodomains; receptor ectodomains do not contact one another in this structure.

The abstract describes TGFBRAP1 as a SMAD4 chaperone. The specific BMPR1A interaction experiment underlying the source annotation remains unresolved.

Selected primary Results/Discussion use soluble BMPR-IA-Fc to inhibit BMP5-induced dendrites; endogenous neuronal receptor binding remains an explicit limitation.

The abstract includes BMP-receptor comparators and indexed publisher Methods identify activated human ALK3. Full construct-specific ATP/SMAD assays were not retrieved; the ALK4/5/7 title does not establish a wrong-gene citation.

Conditional mouse mesenchymal deletion supports Bmpr1a participation in AMH-dependent Müllerian-duct regression, not a direct human purified-ligand binding experiment.

The abstract describes structural/mutational evidence for the BMP2–BRIA interface, with ligand L51P specifically disrupting type I receptor binding.

The abstract supports BRIa localization in caveolin-associated domains. Caveolin isoforms and BRII immunoprecipitation conclusions must be distinguished from BMPR1A-specific results.

The abstract compares GDF5 wild-type and disease-variant binding to BMPR1A/BMPR1B ectodomains; variants can decrease or increase BMPR1A affinity.

The abstract describes BMP2/type I/type II receptor ectodomain assembly with distinct ligand-binding surfaces and no direct contact between receptor ectodomains.

The abstract reports candidate polymorphism/bacteremia associations in sickle-cell anemia; the direct immune-response role of BMPR1A remains unresolved.

The abstract focuses on the type III BMP co-receptor. The existing BMPR1A/BMP2 binding assertion is retained with curator deference and independent receptor-structure support.

The canonical abstract supports HJV signaling through selected BMP receptors. Selected archived full text identifies ALK3-dependent reporter/hepcidin-promoter responses in cell-specific settings; this is signaling-dependent transcription, not BMPR1A DNA binding.

Selected canonical Methods/Results distinguish human mesenchymal-cell receptor RNAi from full-length human receptor BRET experiments in HEK-293 cells and from ligand-induced mineralization. BMPR1A preferentially mediates BMP2/4 responses in that mesenchymal-cell system.

Selected canonical primary passages distinguish SM22alpha-Cre mouse developmental phenotypes from human pulmonary smooth-muscle RNAi. Loss of BMPR1A increases basal migration but impairs PDGF-BB-directed migration; early myocardial proliferation defects occur without enhanced apoptosis in the tested model.

The abstract explains higher-affinity GDF5 recognition by BMPR1B through a receptor-loop conformation; this does not establish absence of lower-affinity BMPR1A binding.

The abstract distinguishes TGFBR3-dependent ALK3 surface retention from ALK6 internalization and downstream trafficking differences.

The abstract directly reports proBMP2 binding to BMPR1A ectodomain and cell-surface receptor without mature-BMP2-like osteogenic activity.

Selected publisher Results, Figure 8 caption and SPR Methods were read. They directly examine BMP2/BMP4 interactions with soluble BMPR1A and FSTL1. The local cache remains abstract-only.

Publisher Figure 3, Results and Methods identify human BMPR1A ectodomain expressed in Pichia and direct BMP2/BMP4 SPR assays. The local cache remains abstract-only.

Selected primary Methods/Results describe crystallization of human BRIA ectodomain with engineered high-affinity GDF5 R57A. The construct is not a natural receptor isoform.

The accessible abstract emphasizes TSC22D1 regulation of TGF-beta signaling; UniProt explicitly cites it for the target BMPR1A–TSC22D1 interaction. Complete target-assay detail remains unread.

The accessible abstract emphasizes GDF5 S94N, noggin resistance and receptor specificity. The exact assays behind the BMPR1A/GDF5 and BMPR1A/BMPR2 source rows remain unresolved.

Selected primary Results/Methods compare wild-type GDF5 with W414R binding to BMPR1A ectodomain; both ligand identity and altered affinity must be retained.

The abstract connects BMPR1A perturbation to BMP/SMAD/ID1 signaling and angiogenesis in a colon-cancer xenograft context.

The abstract supports HFE–ALK3 association, receptor stabilization and surface accumulation. Indexed primary Discussion proposes a larger HFE/TFR2/HJV/ALK3 assembly; its full assembly and supplemental evidence were not independently established.

Selected primary Results and Methods directly measure human BMPR1A ectodomain binding to BMP2 by SPR. RGM bridging and soluble-receptor ligand interception are distinct mechanisms.

The abstract and target-specific UniProt annotation support SCUBE3-dependent BMP signaling and BMPR1A association; SCUBE3 scaffold/co-receptor activity must not be assigned to BMPR1A.

The abstract includes human as well as Drosophila signaling; indexed primary Discussion identifies human Alk3 QD. The exact ligand-specific TGF-beta pathway interpretation remains unresolved.

The abstract reports cloning of human ALK3 and predicts its single-pass receptor kinase topology; TGF-beta-superfamily membership alone does not establish a specific TGF-beta ligand pathway.

The abstract directly establishes BMP type I receptor phosphorylation of the SMAD1 C-terminal motif. Construct-specific full text was not independently retrieved; repeated human BMPR1A GO-CAM assignments provide curator evidence.

Selected canonical Methods explicitly use activated BMPR-IA(Q233D) and BMP4. Receptor-activated SMAD transcriptional mechanisms are distinct from receptor kinase activity.

Type II receptor phosphorylation activates the type I receptor.

BMP receptors transduce ligand binding through SMAD signaling.

The event title names BMP R-SMAD1/5/8 dissociation, while the cached summary describes TGF-beta/SMAD2/3. Plasma-membrane location has independent support; this source mismatch is not silently corrected.

BMP2 engages the receptor complex.

I-SMAD competes with R-SMAD access to type I receptor.

Activated type I receptors phosphorylate R-SMAD1/5/8.

Endofin recruits R-SMADs to the receptor.

I-SMAD/Smurf regulation promotes receptor inhibition/degradation; the receptor is a substrate, not the E3 ligase.

Heteromeric BMP receptor complexes may be preformed or ligand induced.

Human P36894 is a 532-residue single-pass receptor with extracellular ligand recognition and intracellular serine/threonine kinase activity. The source record documents BMP-family and regulatory interactions; its mature chain is not a newly established splice isoform.