ArticleScientific reports2026
Understanding of the different roles of Noggin in the Noggin-BMP-2 and Noggin-BMP-9 dimer complexes at the molecular level.
Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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1 citing paper in PubMed.
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10 authors.
Funding
Abstract
Bone morphogenetic proteins (BMPs) play crucial roles in tissue development and repair as growth factors. However, the clinical application of some type of BMPs is restricted due to their undefined and uncontrolled complex signaling pathways. This study investigates the interactions of BMPs, particularly BMP-2 and BMP-9, with Noggin, a BMP antagonist crucial for embryonic development. BMPs signal through heterohexameric receptor complexes, activating Smad and non-Smad pathways. Noggin, with its cysteine-knot structure, inhibits BMP signaling by preventing receptor binding. Molecular dynamics simulation studies of structurally similar BMP proteins show higher fluctuations in the Noggin/BMP-9 complex than the Noggin/BMP-2 complex. Surface Plasmon Resonance (SPR) analysis revealed that the equilibrium dissociation constant (K
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