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[null,"1.","Record Nr.",null,"UNINA9910797425103321"]
[null,null,"Titolo",null,"Bone morphogenic protein / / series editor Gerald Litwack, PhD, Toluca Lake, North Hollywood, California"]
[null,null,"Pubbl/distr/stampa",null,"Waltham, MA : , : Elsevier, , 2015"]
[null,null,"ISBN",null,"0-12-802592-1"]
[null,null,"Edizione",null,"[First edition.]"]
[null,null,"Descrizione fisica",null,"1 online resource (367 p.)"]
[null,null,"Collana",null,"Vitamins and Hormones, , 0083-6729 ; ; volume 99"]
[null,null,"Disciplina",null,"612.75"]
[null,null,"Soggetti",null,"Bone morphogenetic proteins"]
[null,null,"Lingua di pubblicazione",null,"Inglese"]
[null,null,"Formato",null,"Materiale a stampa"]
[null,null,null,"Livello bibliografico","Monografia"]
[null,null,null,"Note generali","Description based upon print version of record."]
[null,null,null,"Nota di bibliografia","Includes bibliographical references and index."]
[null,null,"Nota di contenuto",null,"Front Cover; Bone Morphogenic Protein; Copyright; Former Editors; Contents; Contributors; Preface; Chapter One: Mechanisms of BMP-Receptor Interaction and Activation; 1. Evolutionary Expansion and Diversification of the Transforming Growth Factor β Superfamily; 2. Phylogenetic Analysis Reveals Four Functional Subfamilies for TGFβ Ligands; 3. Expression as Protease-Activated Proproteins and a Cystine-Knot Motif in the C-Terminal Mature Region as Key Features ...; 4. TGFβ Receptor Activation and Its Downstream Signaling Cascade; 5. Too Few Receptors for Too Many Ligands Lead to Promiscuity"]
[{"$nulls":4},"6. Molecular Mechanisms to Ensure Ligand-Receptor Promiscuity and Specificity: The Concept of Multiple Hot Spots of Binding7. Molecular Mechanisms to Ensure Ligand-Receptor Promiscuity and Specificity: The Concept of Structural Adaptability; 8. Consequences of Promiscuity and Specificity in the TGFβ Superfamily: Conclusions; References; Chapter Two: The Bone Morphogenetic Proteins and Their Antagonists; 1. Bone Morphogenetic Proteins; 2. BMP Antagonist Proteins; 2.1. Chordin Family; 2.2. Follistatin and Follistatin-Like Proteins; 2.3. Noggin; 2.4. Twisted Gastrulation"]
[{"$nulls":4},"3. Cerberus and Dan Family BMP Antagonists3.1. Cerberus; 3.2. Coco; 3.3. Dan; 3.4. Gremlin; 3.5. PRDC/Gremlin 2; 3.6. Sclerostin; 3.7. USAG-1/Wise; 4. BMP-Antagonists Binding to Heparin/HS; References; Chapter Three: BMP-7 Signaling and its Critical Roles in Kidney Development, the Responses to Renal Injury, and Chronic K ...; 1. Introduction; 2. The TGF-β/BMP Protein Superfamily; 3. The BMP-7 Protein; 4. TGF-β/BMP Signaling Pathways; 4.1. SMAD-Dependent Mechanisms for TGF-β/BMP Signaling; 4.1.1. Ligand Binding and Receptor Activation; 4.1.2. Activation of SMAD Transcription Factors"]
[{"$nulls":4},"4.1.3. Heterodimerization and Nuclear Translocation of SMAD Transcription Factors4.1.4. SMAD-Dependent Regulation of Transcription; 4.2. SMAD-Independent Mechanisms for TGF-β/BMP Signaling; 4.3. Key Regulatory Steps in TGF-β/BMP Signaling; 4.3.1. Ligand Expression; 4.3.2. Ligand Availability; 4.3.3. Receptor Activation; 4.3.4. SMAD Activation; 4.3.5. Formation of Transcription Factor Complexes; 5. The Role of BMP-7 in Kidney Development; 5.1. Effects of BMP-7 Genetic Ablation on Development; 5.2. Functions of BMP-7 in the Metanephric Mesenchyme; 5.3. Functions of BMP-7 in the Ureteric Bud"]
[{"$nulls":4},"5.4. Functions of BMP-7 in Stromal Cell Populations6. BMP-7, Congenital Renal Abnormalities, and Pediatric Kidney Disease; 7. The Role of BMP-7 in the Pathogenesis of CKD; 7.1. Therapeutic Effects of Recombinant BMP-7 in Models of CKD; 7.2. Renal Protective Mechanisms of Recombinant BMP-7; 7.2.1. Inhibition of Renal Fibrosis; 7.2.2. Other Important Renal Protective Mechanisms; 8. A Model for the Role of Endogenous BMP-7 in Regulating the Responses to Renal Injury; 9. Clinical Implications for BMP-7 in Patients with CKD; Acknowledgments; References"]
[{"$nulls":4},"Chapter Four: The Role of BMP Signaling and NF-κB Signaling on Osteoblastic Differentiation, Cancer Development, and Vasc..."]