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Klaus-Armin Nave

Researcher at Max Planck Society

Publications -  402
Citations -  42271

Klaus-Armin Nave is an academic researcher from Max Planck Society. The author has contributed to research in topics: Myelin & Oligodendrocyte. The author has an hindex of 98, co-authored 387 publications receiving 36847 citations. Previous affiliations of Klaus-Armin Nave include University of Antwerp & University of Glasgow.

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Multiple Sclerosis: An Immune or Neurodegenerative Disorder?

TL;DR: Data that support neurodegeneration as the major cause of irreversible neurological disability in MS patients are reviewed and it is questioned whether inflammatory demyelination is primary or secondary in the disease process.
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Glycolytic oligodendrocytes maintain myelin and long-term axonal integrity

TL;DR: By in vivo magnetic resonance spectroscopy, brain lactate concentrations in mutants were increased compared with controls, but were detectable only in mice exposed to volatile anaesthetics, which indicates that aerobic glycolysis products derived from oligodendrocytes are rapidly metabolized within white matter tracts.
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Disruption of Cnp1 uncouples oligodendroglial functions in axonal support and myelination

TL;DR: It is shown that Cnp1, which encodes 2′,3′-cyclic nucleotide phosphodiesterase in oligodendrocytes, is essential for axonal survival but not for myelin assembly, and the chief function of glia in supporting axonal integrity can thus be completely uncoupled from its function in maintaining compact myelin.
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Myelination and support of axonal integrity by glia

TL;DR: Cell biology and mouse genetics have provided insight into axon–glia signalling and the molecular architecture of the myelin sheath, and glial cells that myelinate axons were found to have a dual role by also supporting the long-term integrity of those axons.
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Axonal neuregulin-1 regulates myelin sheath thickness

TL;DR: This work uses mutant and transgenic mouse lines to show that axonal Neuregulin-1 (Nrg1) signals information about axon size to Schwann cells, and suggests a model by which myelin-forming SchwANN cells integrate axonal Nrg1 signals as a biochemical measure of axonsize.