
Myelin Basic Protein.
Başlık:
Myelin Basic Protein.
Yazar:
Boggs, Joan M.
ISBN:
9781608762477
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 online resource (261 pages)
İçerik:
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 "classic" 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 "NORMAL" -- 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 -- STRUCTURAL INTERACTIONS BETWEEN AUTOIMMUNE ANTIGENS OF ACETYLATED N-TERMINAL 9-MER OR 11-MER PEPTIDES OF MYELIN BASIC PROTEIN AND MHC -- Structural Modeling of the AcMBP1-9-I-Au complex -- Structural analysis of the AcMBP1-11-I-Au crystal complex -- Structural analysis of the 172.10 TCR-AcMBP1-11-I-Au crystal complex -- CONFORMATIONAL STUDIES OF LINEAR AND CYCLIC MBP PEPTIDES: NMR AND MOLECULAR MODELING -- ORGANIC COMPOUNDS CAN BLOCK T CELL PRESENTATION OF MYELIN BASIC PROTEIN PEPTIDE MBP152-165 -- FUTURE PROSPECTS -- ACKNOWLEDGEMENTS -- REFERENCES -- INTERACTIONS OF THE 18.5 KDA MYELIN BASIC PROTEIN WITH LIPID BILAYERS: STUDIES BY ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPY AND IMPLICATIONS FOR GENERATION OF AUTOIMMUNITY IN MULTIPLE SCLEROSIS -- ABSTRACT -- ABBREVIATIONS -- INTRODUCTION -- Myelin basic protein - a structural, peripheral membrane protein of the central nervous system.
Deimination of MBP is correlated with early development, and with demyelination and disease severity in multiple sclerosis -- Electron paramagnetic resonance (EPR) spectroscopy to study lipid-reconstituted MBP -- Site-directed spin-labelling (SDSL) and EPR spectroscopy of soluble and membrane-associated proteins -- SDSL/EPR spectroscopy of MBP in a myelin-like membrane environment -- Conformation of an immunodominant epitope of MBP in situ -- Deimination of MBP exposes the central immunodominant epitope -- The SH3-ligand domain of MBP -- Protein-protein interactions -- CONCLUSIONS AND FUTURE DIRECTIONS -- ACKNOWLEDGEMENTS -- REFERENCES -- INSIGHTS INTO THE INTERACTION OF MYELIN BASIC PROTEIN WITH MICROTUBULES -- ABSTRACT -- INTRODUCTION -- Implication of MBP in the signal transduction derived from membrane alterations -- The interaction between myelin basic protein and the cytoskeleton -- Oligodendroglial distribution of microtubules and microfilaments -- Effects of Post-Translational Modifications on Tubulin-MBP interactions -- CONCLUSION -- ACKNOWLEDGEMENTS -- REFERENCES -- MYELIN BASIC PROTEIN INTERACTIONS WITH ACTIN AND TUBULIN IN VITRO: BINDING, ASSEMBLY, AND REGULATION -- ABSTRACT -- INTRODUCTION -- MBP-MEDIATED INTERACTIONS WITH ACTIN AND TUBULIN, AND EFFECT OF POST-TRANSLATIONAL MODIFICATIONS -- MBP-mediated binding of actin to membranes and effect of post-translational modifications -- MBP-cytoskeleton interactions in vivo -- CONCLUSION -- ACKNOWLEDGEMENTS -- REFERENCES -- MOLECULAR MODELLING OF THE INTERACTION OF MYELIN BASIC PROTEIN PEPTIDES WITH SIGNALLING PROTEINS AND EFFECTS OF POST-TRANSLATIONAL MODIFICATIONS -- ABSTRACT -- ABBREVIATIONS -- INTRODUCTION -- WHAT IS EXPERIMENTALLY KNOWN? -- MBP-CaM interaction -- MBP - SH3-domain interaction -- MOLECULAR DOCKING SIMULATION METHODS.
ANALYSIS OF THE STRUCTURAL FEATURES OF THE RECEPTOR AND THE LIGAND: MODEL BUILDING OF MBP FRAGMENTS -- Target identification -- Structural features of the ligand and the receptor -- Modeling of the target -- Choice of the receptor structure -- In silico post-translational modifications of the MBP target peptides -- CaM - MBP COMPLEXES: THE DOCKING RESULTS -- The C-terminal T147-D158 target -- The central P82-P93 target -- The N-terminal R41-R52 target -- SH3-DOMAIN - MBP COMPLEX: THE DOCKING RESULTS -- The T92-R104 proline-rich segment -- EFFECTS OF POST-TRANSLATIONAL MODIFICATIONS -- CaM binding target mMBP(T147-D158) -- SH3-domain binding target -- CONCLUSION -- ACKNOWLEDGEMENTS -- REFERENCES -- STRUCTURE AND DYNAMICS OF THE MYELIN BASIC PROTEIN FAMILY BY SOLUTION AND SOLID-STATE NMR -- ABSTRACT -- ABBREVIATIONS -- INTRODUCTION -- Principles of nuclear magnetic resonance (NMR) spectroscopy -- Solution versus solid-state NMR spectroscopy -- Fundamental measurements and experiments in NMR spectroscopy -- Literature review - NMR of MBP in the 20th century -- Solution NMR spectroscopy of Golli-MBP isoform BG21 - spectral assignment and dynamics -- Solution NMR spectroscopy of the full-length 18.5 kDa classic MBP isoform- assignments under aqueous and membrane-mimetic conditions -- Solid-state NMR spectroscopy of 18.5 kDa MBP reconstituted with lipid vesicles - conformation and dynamics of the protein -- Solid-state NMR spectroscopy of 18.5 kDa MBP reconstituted with lipid vesicles - Effects on the lipid bilayer -- CONCLUSIONS AND FUTURE DIRECTIONS -- ACKNOWLEDGEMENTS -- REFERENCES -- INDEX.
Notlar:
Electronic reproduction. Ann Arbor, Michigan : ProQuest Ebook Central, 2017. Available via World Wide Web. Access may be limited to ProQuest Ebook Central affiliated libraries.
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