| Nota di contenuto |
Intro -- Preface -- Contents -- About the Editor -- 1: Proteins Drug Targeting and Its Therapeutics -- 1.1 Introduction -- 1.2 Therapeutic Proteins Fabrication and Decontamination -- 1.3 Therapeutic Polypeptides Formulation -- 1.4 Therapeutic Proteins Pharmacokinetics -- 1.5 Therapeutic Proteins Metabolism -- 1.6 Therapeutic Proteins Exclusion -- 1.7 Therapeutic Proteins Transference -- 1.8 Protein Nanomaterials as Drug Delivery Carters -- 1.9 Preparation of Protein Nanoparticles Approaches -- 1.10 Therapeutic Immunoglobulin -- 1.11 Therapeutic Proteins for Cancer Treatment -- 1.12 Proteins Involved in Cell Cycle Regulations -- 1.13 Therapeutic Proteins Contests -- 1.14 Conclusion -- References -- 2: Interferons -- 2.1 History -- 2.2 What Are Interferons (IFNs)? -- 2.3 Chemical and Biological Features of IF -- 2.4 Structure of Interferons -- 2.4.1 Types of Interferons -- 2.4.1.1 Interferon Type I -- 2.4.1.2 Interferon Type II (IFN- in Humans) -- 2.4.1.3 Interferon Type III -- 2.4.2 Interferon Downstream Signalling -- 2.4.3 How Does Interferon Protect Cells Against Virus Infection? -- 2.4.4 How Do Viruses Escape Interferon Activity? -- 2.5 Therapeutic Uses of Interferon -- 2.5.1 Treatment of Multiple Sclerosis (MS) -- 2.5.2 Suppression of Cell Growth -- 2.5.3 Prevention of Angiogenesis -- 2.5.4 Interferon Alpha in COVID-19 -- 2.5.5 Interferon in Chronic Infection with Hepatitis B Virus -- 2.5.6 Interferon in Chronic Infection with Hepatitis C Virus -- 2.5.7 Interferon Against Malignant Diseases -- 2.6 Current Research -- 3: Epidermal Growth Factor (EGF) in Wound Repair -- 3.1 Introduction -- 3.2 Epidermal Growth Factor (EGF) -- 3.3 Functions of EGF -- 3.4 Mechanism of Action of EGF -- 3.5 Skin and Wound -- 3.6 Physiology of Wound Repair -- 3.7 Role of Neutrophils in Wound Repair -- 3.8 Role of Macrophages in Wound Repair.
3.9 Regulation of Angiogenesis in Wound Repair by Chemokines and Growth Factors -- 3.9.1 Role of Keratinocytes in Wound Repair -- 3.9.2 Chronic Wound -- 3.9.3 Diabetic Wound -- 3.9.4 Growth Factors in Wound Repair -- 3.9.5 Role of EGF in Diabetic Wound -- 3.9.6 Role of EGF in Burn Injury -- 3.9.7 Role of Salivary EGF in Wound Repair -- 3.9.8 EGF in Psoriasis -- 3.9.9 EGF in Healing of Gastric Ulcer -- 3.9.10 Role of EGF in Colonic Ulcer Repair -- 3.9.11 Drug Delivery Systems (DDS) with EGF -- 3.9.11.1 Particulate Systems -- 3.9.11.2 Hydrogels -- 3.9.11.3 Scaffolds -- 3.9.11.4 Miscellaneous Systems -- 3.9.12 Applications of EGF in Humans -- 3.9.13 Limitations -- 3.10 Future Directions -- References -- 4: Therapeutic Protein Against Autoimmune Disorders: Intracellular and Extracellular Properties -- 4.1 Introduction -- 4.2 Treatment for Autoimmune Disorders -- 4.3 Autoantibodies Against Intracellular Proteins -- 4.4 Autoantibody Against Extracellular Proteins -- 4.5 Heat Shock Proteins (HSP) -- 4.6 HSP as Molecular Proteases -- 4.7 HSP´s Immunosuppressive Properties -- 4.8 Anti-HSP Autoantibody-Autoimmune Disorders -- 4.9 Clinical Research Outcome of HSP -- 4.10 Conclusion -- References -- 5: Prions as Therapeutic Proteins and their Prospect as Drug Delivery Agent -- 5.1 Introduction -- 5.2 Prion Proteins and Diseases -- 5.2.1 Features of Prion Protein -- 5.2.2 Protein-Only Theory of Prion Diseases -- 5.3 Therapeutic Potentials of Prion -- 5.3.1 Prions as Antimicrobial Peptides -- 5.3.2 Prions as Mediator of Immunomodulatory Activities Antiviral Agent -- 5.3.3 Heterologous Prions as Therapy to Prion Disease -- 5.4 Prion Protein as a Drug Delivery Agent, Future Perspective -- 5.5 Conclusion -- References -- 6: Interleukin-2 -- 6.1 Introduction -- 6.2 Discovery of IL-2 -- 6.3 Interleukin-2 Receptor -- 6.4 Soluble IL-2R.
6.5 Interleukin-2 Signaling Pathway -- 6.6 Interleukin-2 as a Biomarker -- 6.7 Application of IL-2 in Cancer Immunotherapy -- 6.8 Limitations -- 6.9 Efficacy of IL-2 Immunotherapy -- 6.10 Future Direction -- 7: Bioinformatics Resources, Tools, and Strategies in Designing Therapeutic Proteins -- 7.1 Background -- 7.2 Databases -- 7.2.1 Protein Data Bank (PDB) -- 7.2.2 InterPro -- 7.2.3 Pfam -- 7.2.4 PIRSF -- 7.2.5 PROSITE -- 7.2.6 neXtProt -- 7.2.7 IntAct -- 7.2.8 PeptideAtlas -- 7.2.9 PRIDE -- 7.2.10 DEPOD -- 7.2.11 PhosPhAt -- 7.2.12 Phospho.ELM -- 7.2.13 PhosphoGrid -- 7.2.14 UniCarbKB -- 7.2.15 MEROPS -- 7.3 Tools and Softwares -- 7.3.1 Protein-Ligand and Protein-Protein Interactions -- 7.3.1.1 CAPRI -- 7.3.1.2 STRING -- 7.3.2 Molecular Dynamic (MD) Simulation -- 7.3.2.1 Desmond -- 7.3.2.2 GROMOS -- 7.3.2.3 GROMACS -- 7.3.2.4 NAMD -- 7.3.2.5 UCSF Chimera -- 7.3.3 Molecular Docking -- 7.3.3.1 ArgusLab -- 7.3.3.2 AutoDock -- 7.3.3.3 DockThor -- 7.3.3.4 Glide -- 7.3.3.5 HADDOCK -- 7.3.3.6 SwissDock -- 7.3.4 Structure Prediction -- 7.3.4.1 CASTp -- 7.3.4.2 HHpred -- 7.3.4.3 MAESTRO -- 7.3.4.4 PocketPicker -- 7.3.4.5 SiteEngine -- 7.3.5 Sequence Alignment -- 7.3.5.1 BLASTO -- 7.3.5.2 DELTA BLAST -- 7.3.5.3 CLUSTALW -- 7.3.6 Molecular Modeling -- 7.3.6.1 Cn3D -- 7.3.6.2 CONFOLD -- 7.3.6.3 MODELLER -- 7.3.7 Molecular Visualization -- 7.3.7.1 DeltaProt -- 7.3.7.2 MOLMOL -- 7.3.7.3 RasMol -- 7.3.7.4 PyMOL -- 7.3.8 Antibody Numbering -- 7.3.8.1 AbRSA -- 7.3.8.2 ANARCI -- 7.3.8.3 IMGT/V-QUEST -- 7.3.9 Antibody Modeling -- 7.3.9.1 BIOVIA -- 7.3.9.2 RosettaAntibody -- 7.3.9.3 BepiPred -- 7.3.9.4 AgAbDb -- 7.3.10 Antibody Design -- 7.3.10.1 AbDesign -- 7.3.10.2 OptCDR -- 7.3.10.3 OptMAVEn -- 7.3.10.4 RosettaAntibodyDesign -- 7.4 Strategies for Designing Therapeutic Proteins -- 7.4.1 Target Structure Preparation -- 7.4.2 Comparative Modeling.
7.4.3 Binding Site Analysis -- 7.4.4 Representing Ligands and Target for Docking -- 7.4.5 Sampling Algorithms for Protein-Ligand Docking -- 7.4.6 Scoring Functions for Complex Evaluation -- 7.4.7 Atomic Level or High-Resolution Docking -- 7.4.8 Molecular Fingerprint and Similarity -- 7.4.9 ADMET Profile -- 7.4.10 Antibody Design -- 7.5 Conclusion -- References -- 8: Therapeutic Proteins Used in Human Pancreatic Disease -- 8.1 Introduction -- 8.2 Therapeutic Proteins -- 8.3 Hormones as TPs -- 8.4 Fc-Fusion Proteins -- 8.5 Monoclonal Antibodies against Pancreatic Diseases -- 8.6 Blood Components -- 8.7 Enzymes -- 8.8 Protein Based Diet -- 8.9 Adverse Effects of TP -- 8.10 Future Challenges -- 8.11 Scope -- 8.12 Conclusion -- References -- 9: Therapeutic Role of Soybean-Derived Lunasin Peptide in Colon Cancer Treatment: A Recent Updates from Literature -- 9.1 Introduction -- 9.2 Bioavailability of Lunasin Peptide -- 9.3 The Chemistry Associated with the Lunasin Peptide -- 9.4 Factors Associated with the Concentration of Lunasin Peptide -- 9.5 An Outline of the Therapeutic Properties of Lunasin Peptide -- 9.5.1 Antioxidant and Anti-inflammatory Properties -- 9.5.2 Chemopreventive Properties of Lunasin Peptide in Colon Cancer -- 9.5.3 Lunasin Peptide Works by an Epigenetic Mechanism -- 9.6 The Combination Strategy of Lunasin Peptide for Therapeutic Approach -- 9.7 Conclusion and Future Perspective -- References -- 10: Therapeutic Peptides in Skin and Hair Disorders -- 10.1 Introduction -- 10.2 Inquisition of the Production, Delivery, and Elimination of Protein Therapeutics -- 10.2.1 Production of Therapeutic Proteins and Peptides -- 10.2.2 Delivering Therapeutic Peptides to Target Organs -- 10.2.3 Elimination of Protein Therapeutics from the Body -- 10.2.4 Therapeutic Peptides Against Skin Disorders -- 10.2.5 Antimicrobial Peptides -- 10.2.6 Psoriasis.
10.2.7 Wound Healing -- 10.2.8 Cancer -- 10.2.9 Peptides as Cosmeceuticals -- 10.2.10 Stem Cells as Therapeutics -- 10.2.11 Therapeutic Peptides in Hair Disorders -- 10.3 Why Use Therapeutic Peptides? -- 10.4 Summary -- References.
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Molecular Mechanisms of Steroid Hormone Biosynthesis and Action / / edited by Jacques J. Tremblay
