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Publications by A. L. Sieron
The C-Proteinase That Processes Procollagens to Fibrillar Collagens Is Identical to the Protein Previously Identified as Bone Morphogenic Protein-1.
Proceedings of the National Academy of Sciences of the United States of America
Multidisciplinary
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Sphingosine-Dependent Protein Kinase-1, Directed to 14-3-3, Is Identified as the Kinase Domain of Protein Kinase Cδ
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Mammalian Tolloid-Like 1 Binds Procollagen C-Proteinase Enhancer Protein 1 and Differs From Bone Morphogenetic Protein 1 in the Functional Roles of Homologous Protein Domains
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Bone Morphogenic Protein 2 Activates Protein Kinase D to Regulate Histone Deacetylase 7 Localization and Repression of Runx2
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Role of the Bone Morphogenic Protein Pathway in Developmental Haemopoiesis and Leukaemogenesis
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Errata To: “A Current Viewpoint on Structure and Evolution of Collagens. I. Fibrillar Collagens”
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Erratum To: The Effects on Dermal Wound Healing Using Novel Peptide Modified by Bone Morphogenic Protein-2
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Conditional Ablation of the Heparan Sulfate-Synthesizing EnzymeExt1Leads to Dysregulation of Bone Morphogenic Protein Signaling and Severe Skeletal Defects
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Nodal Signaling Regulates the Bone Morphogenic Protein Pluripotency Pathway in Mouse Embryonic Stem Cells
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Extracellular Matrix Protein Mindin Is Required for the Complete Allergic Response to Fungal-Associated Proteinase
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