Expression and properties of the recombinant murine Golli-Myelin basic protein isoform J37

Journal of Neuroscience Research

Volumn 71, Issue 6, 2003, Pages 777-784

  Kaur, Jaspreet ^a   Libich, David S ^a   Campagnoni, Celia W ^b   Wood, D Denise ^c   Moscarello, Mario A ^c   Campagnoni, Anthony T ^b   Harauz, George ^a  

^a UNIVERSITY OF GUELPH   (Canada)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c HOSPITAL FOR SICK CHILDREN   (Canada)

Author keywords

Calmodulin; Circular dichroism; Fluorescence spectroscopy; Genes of oligodendrocyte lineage (Golli); J37; Lipid aggregation; Mass spectrometry; MBP; Myelin basic protein

Indexed keywords

ACRYLAMIDE; CALCIUM ION; CALMODULIN; GANGLIOSIDE GM1; ISOPROTEIN; MONOSIALOGANGLIOSIDE; MONOSIALOGANGLIOSIDE GM1; MURINE GOLLI MYELIN BASIC PROTEIN; MYELIN; MYELIN BASIC PROTEIN; PHOSPHATIDYLINOSITOL 4 PHOSPHATE; PROTEIN; PROTEIN BG21; PROTEIN J37; PROTEIN TP8; RECOMBINANT MURINE GOLLI MYELIN BASIC PROTEIN J37; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID ANALYSIS; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; ARTICLE; BETA SHEET; BINDING AFFINITY; BINDING SITE; CENTRAL NERVOUS SYSTEM; CIRCULAR DICHROISM; DISSOCIATION CONSTANT; FLUORESCENCE SPECTROSCOPY; LIGAND BINDING; LIPID AGGREGATION; LIPID VESICLE; LIPID VESICLE AGGREGATION; MOLECULAR MECHANICS; MYELIN SHEATH; MYELINATION; NONPHOTOCHEMICAL QUENCHING; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN ISOLATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; STEADY STATE;

ANIMALS; BINDING SITES; CALMODULIN; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; MASS SPECTROMETRY; MICE; MYELIN BASIC PROTEINS; NERVE TISSUE PROTEINS; PROTEIN BINDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP; TRANSCRIPTION FACTORS;

EID: 0037443597     PISSN: 03604012     EISSN: None     Source Type: Journal    
DOI: 10.1002/jnr.10547     Document Type: Article

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