0000000000543255

AUTHOR

Roland Brandt

0000-0003-0101-1257

showing 1 related works from this author

O-glycosylation of the tail domain of neurofilament protein M in human neurons and in spinal cord tissue of a rat model of amyotrophic lateral sclero…

2005

Mammalian neurofilaments (NFs) are modified by post-translational modifications that are thought to regulate NF assembly and organization. Whereas phosphorylation has been intensely studied, the role of another common modification, the attachment of O-linked N-acetylglucosamine (GlcNAc) to individual serine and threonine residues, is hardly understood. We generated a novel monoclonal antibody that specifically recognizes an O-glycosylated epitope in the tail domain of NF-M and allows determination of the glycosylation state at this residue. The antibody displays strong species preference for human NF-M, shows some reactivity with rat but not with mouse or bovine NF-M. By immunohistochemistr…

NeurofilamentGlycosylationGlycosylationMolecular Sequence DataHyperphosphorylationBiologyMitogen-activated protein kinase kinaseBiochemistryAnimals Genetically Modifiedchemistry.chemical_compoundEpitopesMiceWestern blotNeurofilament ProteinsCell Line TumorAcetylglucosaminidasemedicineAnimalsHumansAmino Acid SequenceProtein kinase AMolecular BiologyMitogen-Activated Protein Kinase KinasesNeuronsmedicine.diagnostic_testKinaseAmyotrophic Lateral SclerosisAntibodies MonoclonalCell BiologyAxonsCell biologyProtein Structure TertiaryRatsDisease Models AnimalchemistryBiochemistrySpinal CordNIH 3T3 CellsPhosphorylationCattleThe Journal of biological chemistry
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