Myelin basic protein / / Joan M. Boggs, editor

• Pubblicazione: New York, : Nova Science Publishers, c2008
• Edizione: 1st ed.
• Descrizione fisica: 1 online resource (261 p.)
• Disciplina: 572/.633
• Soggetto topico: Myelin basic protein; Myelin sheath
• Altri autori: BoggsJoan M
• Note generali: "Nova biomedical"--Cover.
• Nota di bibliografia: Includes bibliographical references and index.
• Nota di contenuto: ""MYELIN BASIC PROTEIN""; ""NOTICE TO THE READER""; ""CONTENTS""; ""PREFACE""; ""REFERENCES""; ""THE PROPERTIES AND FUNCTIONS OF THE GOLLI MYELIN BASIC PROTEINS""; ""ABSTRACT""; ""INTRODUCTION""; ""The MBP gene encodes the “classicâ€? and golli family of proteins""; ""Features of the primary and higher ordered structure of the golli-MBPs""; ""Approaches to defining the biological roles of golli proteins in cells""; ""Unique phenotypes of the golli KO and golli overexpressing mice""; ""Emerging relevance of golli expression in pathology and disease""; ""CONCLUSION""; ""ACKNOWLEDGEMENTS"" ; ""REFERENCES""""POSTTRANSLATIONAL MODIFICATIONS OF MYELIN BASIC PROTEINS""; ""ABSTRACT""; ""INTRODUCTION""; ""ACETYLATION""; ""METHYLATION""; ""PHOSPHORYLATION""; ""Deamidation of glutamine at residues 103 and 147""; ""Deimination of arginine residues (citrullination)""; ""CONCLUSION""; ""REFERENCES""; ""DEIMINATION OF MYELIN BASIC PROTEIN BY PAD ENZYMES, AND THEIR ROLE IN MULTIPLE SCLEROSIS""; ""ABSTRACT""; ""INTRODUCTION""; ""MBP CHARGE ISOMERS""; ""CONSEQUENCES OF INCREASED CITRULLINATION OF MBP""; ""A. Proteolysis""; ""B. MBP autocatalysis and neoepitopes"" ; ""THE ROLE OF MYELIN BASIC PROTEIN IN MYELIN COMPACTION""""BILAYER STRUCTURE IN NORMAL APPEARING WHITE MATTER (NAWM) IN MS BRAIN IS NOT “NORMALâ€?""; ""MBP MICROHETEROGENEITY IN MS WHITE MATTER""; ""PEPTIDYL ARGININE DEIMINASES (PADS)""; ""THE PAD2 CPG ISLAND""; ""FUTURE DIRECTIONS AND CONCLUDING REMARKS""; ""ACKNOWLEDGEMENTS""; ""REFERENCES""; ""MYELIN BASIC PROTEIN-MEDIATED IMMUNOPATHOGENESIS IN MULTIPLE SCLEROSIS AND EAE""; ""ABSTRACT""; ""INTRODUCTION""; ""EXPRESSION OF MBP IN THE CNS AND THE IMMUNE SYSTEM""; ""MULTIPLE SCLEROSIS AND EAE"" ; ""MBP PEPTIDE SPECIFICITY OF CD4+ T CELLS IN MS""""FREQUENCY AND PHENOTYPES OF CD4+ T CELLS IN MS PATIENTS""; ""MBP PEPTIDE SPECIFICITY OF CD4+ T CELLS IN EAE""; ""EAE AND MS: TH1 VS. TH17?""; ""MBP-SPECIFIC CD4+ TCR TRANSGENIC MICE""; ""HUMANIZED MBP-SPECIFIC CD4+ TCR TRANSGENIC MICE""; ""MBP-SPECIFIC CD8+ T CELLS INVOLVED IN MS""; ""PATHOGENICITY OF MBP-SPECIFIC CD8+ T CELLS IS DEMONSTRATED IN NEW EAE MODELS""; ""B CELLS INVOLVED IN MS AND EAE""; ""IMMUNE TOLERANCE TO SELF-ANTIGENS""; ""CD4+ T CELL IMMUNE TOLERANCE TO MBP""; ""CD8+ T CELL IMMUNE TOLERANCE TO MBP""; ""CONCLUSION"" ; ""REFERENCES""""A STRUCTURAL PERSPECTIVE OF PEPTIDES FROM MYELIN BASIC PROTEIN""; ""ABSTRACT""; ""ABBREVIATIONS""; ""INTRODUCTION""; ""CRYSTAL STRUCTURE OF HLA-DR2 (DRA*0101, DRB1*1501) COMPLEXED WITH A PEPTIDE FROM HUMAN MYELIN BASIC PROTEIN MBP85-99""; ""Peptide interactions with HLA-DR2A""; ""Peptide interactions with Ob.1A.12 TCR""; ""STRUCTURE OF HUMAN MHC CLASS II COMPLEXED WITH A LONGER EPITOPE PEPTIDE (MBP86-105) FROM HUMAN MYELIN BASIC PROTEIN""; ""Interactions with HLA-DR2a / 2b""; ""Interactions with TCR"" ; ""Structure of a human TCR complexed with a peptide from human MBP89-101 and a MHC class II molecule""
• Sommario/riassunto: The compact myelin sheath formed around nerve axons speeds up nerve conduction and also nurtures the axon. Destruction of this sheath in demyelinating diseases such as multiple sclerosis (MS) results in nerve conduction failure and neurodegeneration. Myelin basic protein (MBP) is the second most abundant protein of central nervous system (CNS) myelin (after the proteolipid protein), representing about 30 % of the total myelin protein and about 10 % of myelin by weight. It is also present in peripheral nervous system (PNS) myelin but as a lower percentage of the total protein. This book addresses the structure, different isoforms, post-translational modifications, immunogenicity, and novel functions of MBP and its possible involvement in MS. MBP is a natively unfolded protein, is conformationally adaptable to different environments, and probably has additional roles in the myelinating cells and in myelin besides its well-established role in adhesion of the cytosolic surfaces of myelin in the CNS.
• Titolo autorizzato: Myelin basic protein
• ISBN: 1-60876-247-5
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Lingua di pubblicazione: Inglese
• Record Nr.: 9910958400303321
• Lo trovi qui: Univ. Federico II
• Serie: Intrinsically disordered proteins.