Glycolytic oligodendrocytes maintain myelin and long-term axonal integrity
Open accessAbstract
Oligodendrocytes, the myelin-forming glial cells of the central nervous system, maintain long-term axonal integrity. However, the underlying support mechanisms are not understood. Here we identify a metabolic component of axon-glia interactions by generating conditional Cox10 (protoheme IX farnesyltransferase) mutant mice, in which oligodendrocytes and Schwann cells fail to assemble stable mitochondrial cytochrome c oxidase (COX, also known as mitochondrial complex IV). In the peripheral nervous system, Cox10 conditional mutants exhibit severe neuropathy with dysmyelination, abnormal Remak bundles, muscle atrophy and paralysis. Notably, perturbing mitochondrial respiration did not cause glial cell death. In the adult central nervous system, we found no signs of demyelination, axonal degeneration or secondary inflammation. Unlike cultured oligodendrocytes, which are sensitive to COX inhibitors, post-myelination oligodendrocytes survive well in the absence of COX activity. More importantly, 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. This indicates that aerobic glycolysis products derived from oligodendrocytes are rapidly metabolized within white matter tracts. Because myelinated axons can use lactate when energy-deprived, our findings suggest a model in which axon-glia metabolic coupling serves a physiological function.
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There is so far no experimental approach to the question of whether oligodendrocytes release lactate or pyruvate for the support of axonal energy metabolism.
“However, there is so far no experimental approach to the question of whether oligodendrocytes release lactate or pyruvate (Fünfschilling et al., 2012) for the support of axonal energy metabolism.”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
The paper reports an experimental approach to this question: in vivo magnetic resonance spectroscopy measured increased lactate in Cox10 mutant brains, and the authors interpret the findings as compatible with oligodendroglial lactate release and use by other cells (passage [2], page unavailable). They also report an in vitro test showing that myelinated axons metabolize glial lactate. These experiments do not directly establish whether oligodendrocytes release lactate or pyruvate to support axons, but they contradict the claim that there was no experimental approach to the question. (LLM, conf=0.85)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredRemyelination is a regenerative process of the adult CNS that restores saltatory impulse conduction and trophic support to axons.
“Remyelination is a crucial regenerative process in demyelinating diseases, limiting persisting damage to the CNS. It restores saltatory nerve conduction and ensures trophic support of axons.”
From BCAS1-positive oligodendrocytes enable efficient cortical remyelination in multiple sclerosis (2025) · cites this paper as [3]
The paper’s Abstract describes oligodendrocyte support of long-term axonal integrity and proposes metabolic support from glia to myelinated axons. It discusses remyelination only as an unlikely explanation for its findings in adult mutant mice; it does not show that remyelination restores saltatory conduction or trophic support in demyelinating disease. (LLM, conf=0.83)
Experimental — accuracy not yet measuredOligodendrocytes with impaired oxidative phosphorylation instead boost aerobic glycolysis, as indicated by increased lactate levels.
“Oligodendrocytes with impaired oxidative phosphorylation instead boost aerobic glycolysis, as indicated by increased lactate levels [127].”
From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [127]
The paper reports that Cox10-mutant oligodendrocytes with impaired mitochondrial respiration appear to rely on increased glycolysis, and mutant brains had higher lactate than controls. The cited passage specifies that the lactate increase was detectable only under isoflurane anaesthesia, a condition the claim omits. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThis shift of normal myelin turnover to lipid-based ATP generation allows OLs to share more glucose-derived pyruvate/lactate with axons to support ATP generation and prevent axon degeneration.
“This shift of normal myelin turnover to lipid-based ATP generation allows OLs to share more glucose-derived pyruvate/lactate with the axons to support ATP generation and prevent axon degeneration [278,280].”
From Revisiting the Pathogenesis of X-Linked Adrenoleukodystrophy (2025) · cites this paper as [280]
The Abstract proposes that oligodendrocytes supply glycolysis-derived pyruvate and lactate to energy-deprived axons, and reports no axonal degeneration in adult CNS Cox10 mutants. It does not describe normal myelin turnover being shifted to lipid-based ATP generation, or establish that this shift increases metabolite sharing and prevents degeneration. The metabolic-sharing mechanism is presented as a model, not a demonstrated causal chain. (LLM, conf=0.87)
Experimental — accuracy not yet measuredGlycolytic oligodendrocytes provide direct metabolic support to axons via non-compacted cytoplasmic channels in myelin and monocarboxylate transporters, which preserves functional integrity and axon survival.
“This led to a working model of glycolytic oligodendrocytes providing direct metabolic support to axons via non-compacted cytoplasmic channels in myelin and monocarboxylate transporters, which preserves functional integrity and axon survival (Amaral et al., 2013;Fünfschilling et al., 2012;Lee et al., 2012).”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
The paper proposes a model in which oligodendrocyte glycolysis supplies metabolites to axons, and it identifies MCT1 in myelin and MCT2 in myelinated axons (indexed section labelled Abstract; page unavailable). It also reports maintenance of myelin and axons in adult CNS mutants. Our copy does not describe transport via non-compacted cytoplasmic channels, so that specific route is not supported by this source. (LLM, conf=0.86)
Experimental — accuracy not yet measured
Adult oligodendrocytes become predominantly glycolytic with a reduced rate of oxidative phosphorylation (OXPHOS).
“This is compatible with the idea that adult oligodendrocytes become predominantly glycolytic with a reduced rate of oxidative phosphorylation (OXPHOS) (Fünfschilling et al., 2012).”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
The passage labeled Abstract (page not provided) says that after myelination oligodendrocytes may tolerate a partly glycolytic metabolism and that mature wild-type cells have lower COX activity than precursor cells. This is compatible with a shift toward glycolysis, but it does not establish that adult oligodendrocytes are predominantly glycolytic or directly measure a reduced OXPHOS rate. (LLM, conf=0.85)
Experimental — accuracy not yet measuredThe data are compatible with a revised working model in which lactate is preferentially produced in astrocytes close to their gap junctions with neighboring cells, and myelinic channels funnel astroglial lactate and oligodendroglial pyruvate to the periaxonal space of myelinated internodes.
“Our data are thus compatible with a revised working model of Fünfschilling et al. (2012), in which lactate is preferentially produced in astrocytes close to their gap junctions with neighboring cells, and in which myelinic channels funnel astroglial lactate and oligodendroglial pyruvate to the periaxonal space of myelinated internodes.”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
Split into 2 atoms — 0 confirmed, 2 partially supported, 0 disputed, 0 misattributed, 0 unverifiable. Expand the claim to see per-atom verdicts.
Experimental — accuracy not yet measuredOligodendrocytes support axonal energy metabolism and neuronal health.
“As oligodendrocytes support axonal energy metabolism and neuronal health4–7, we hypothesized that loss of myelin integrity could be an upstream risk factor for neuronal amyloid-β (Aβ) deposition, the central neuropathological hallmark of AD.”
From Myelin dysfunction drives amyloid-β deposition in models of Alzheimer’s disease (2023) · cites this paper as [5]
Oligodendrocyte-specific deletion of Cox10 failed to cause demyelination or neurodegeneration even at 14 months of age.
“Oligodendrocyte-specific deletion of Cox10, which encodes a crucial component for cyt c oxidase assembly and is necessary for oxidative phosphorylation, failed to cause demyelination or neurodegeneration even at 14-months of age.”
From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [127]
Impaired mitochondrial metabolism alone does not induce oligodendrocyte death in vivo.
“For example, impaired mitochondrial metabolism alone does not induce oligodendrocyte death in vivo [127].”
From Oligodendrocyte death and myelin loss in the cuprizone model: an updated overview of the intrinsic and extrinsic causes of cuprizone demyelination (2022) · cites this paper as [127]
Mature oligodendrocytes survive well in Cox10-deficient mice, in which oligodendrocytes lack an assembly factor of stable mitochondrial cytochrome c oxidase (COX, mitochondrial complex IV).
“we found that mature oligodendrocytes survive well in Cox10 (protoheme IX farnesyltransferase)-deficient mice, in which oligodendrocytes lack an assembly factor of stable mitochondrial cytochrome c oxidase (COX, mitochondrial complex IV).”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
Glycolytic oligodendrocytes may support electrically active axons primarily by self-made pyruvate.
“This opens the possibility that glycolytic oligodendrocytes, which are suggested to support electrically active axons with an excess of glycolysis products (Fünfschilling et al., 2012;Lee et al., 2012;Saab et al., 2016;Trevisiol et al., 2017) do so primarily by self-made pyruvate.”
From Downregulated expression of lactate dehydrogenase in adult oligodendrocytes and its implication for the transfer of glycolysis products to axons (2024) · cites this paper as Fünfschilling et al., 2012
Axons readily use lactate for ATP generation.
“This confirms that axons readily use lactate for ATP generation”
From Oligodendroglial NMDA receptors regulate glucose import and axonal energy metabolism (2016) · cites this paper as Fünfschilling et al., 2012
Myelin modulates the speed of neural impulse conduction, provides metabolic support to axons, and exhibits adaptive plasticity.
“Myelin modulates the speed of neural impulse conduction (Smith and Koles, 1970; Waxman, 1980), provides metabolic support to axons (Fünfschilling et al., 2012), and exhibits adaptive plasticity (Gibson et al., 2014);”
From Mild respiratory COVID can cause multi-lineage neural cell and myelin dysregulation (2022) · cites this paper as Fünfschilling et al., 2012
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Cites
Estimation of metabolite concentrations from localized in vivo proton NMR spectra
Provencher, S. W. (1993) · Magnetic Resonance in Medicine · doi:10.1002/mrm.1910300604 · Cited by 3,659 · see citing works
Pellerin, L., & Magistretti, P. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10625 · Cited by 2,927 · see citing works
Astrocyte-Neuron Lactate Transport Is Required for Long-Term Memory Formation
Suzuki, A., Stern, S. A., Bozdagi, O., Huntley, G. W., Walker, R. H., Magistretti, P. J., & Alberini, C. M. (2011) · Cell · doi:10.1016/j.cell.2011.02.018 · Cited by 1,711 · see citing works
Disruption of Cnp1 uncouples oligodendroglial functions in axonal support and myelination
Lappe-Siefke, C., Goebbels, S., Gravel, M., Nicksch, E., Lee, J., Braun, P. E., Griffiths, I. R., & Nave, K.-A. (2003) · Nature Genetics · doi:10.1038/ng1095 · Cited by 1,036 · see citing works
Self-citationAxonal Swellings and Degeneration in Mice Lacking the Major Proteolipid of Myelin
Griffiths, I., Klugmann, M., Anderson, T., Yool, D., Thomson, C., Schwab, M. H., Schneider, A., Zimmermann, F., McCulloch, M., Nadon, N., et al. (1998) · Science · doi:10.1126/science.280.5369.1610 · Cited by 889 · see citing works
Self-citationEssential Role for TrkB Receptors in Hippocampus-Mediated Learning
Minichiello, L., Korte, M., Wolfer, D., Kühn, R., Unsicker, K., Cestari, V., Rossi-Arnaud, C., Lipp, H.-P., Bonhoeffer, T., & Klein, R. (1999) · Neuron · doi:10.1016/s0896-6273(00)80853-3 · Cited by 799 · see citing works
Myelination and the trophic support of long axons
Nave, K.-A. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2797 · Cited by 648 · see citing works
Self-citationRegulation of Oligodendrocyte Development and Myelination by Glucose and Lactate
Rinholm, J. E., Hamilton, N. B., Kessaris, N., Richardson, W. D., Bergersen, L. H., & Attwell, D. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.3516-10.2011 · Cited by 383 · see citing works
Mitochondrial potassium transport: the K+ cycle
Garlid, K. D., & Paucek, P. (2003) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(03)00108-7 · Cited by 365 · see citing works
Axonal loss and neuroinflammation caused by peroxisome-deficient oligodendrocytes
Kassmann, C. M., Lappe-Siefke, C., Baes, M., Brügger, B., Mildner, A., Werner, H. B., Natt, O., Michaelis, T., Prinz, M., Frahm, J., et al. (2007) · Nature Genetics · doi:10.1038/ng2070 · Cited by 357 · see citing works
Self-citationThe Turnover of Mitochondria in a Variety of Tissues of Young Adult and Aged Rats
Menzies, R. A., & Gold, P. H. (1971) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)62305-1 · Cited by 336 · see citing works
Goebbels, S., Oltrogge, J., Kemper, R., Heilmann, I., Bormuth, I., Wolfer, S., Wichert, S. P., Möbius, W., Liu, X., Lappe-Siefke, C., et al. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.0219-10.2010 · Cited by 329 · see citing works
Self-citationMiller, R. H., David, S., Patel, R., Abney, E. R., & RAFF, M. C. (1985) · Developmental Biology · doi:10.1016/0012-1606(85)90432-4 · Cited by 316 · see citing works
The POU proteins Brn-2 and Oct-6 share important functions in Schwann cell developmentPreprint
Jaegle, M., Ghazvini, M., Mandemakers, W. J., Piirsoo, M., Driegen, S., Levavasseur, F., Raghoenath, S., Grosveld, F. G., & Meijer, D. (2003) · Genes & Development · doi:10.1101/gad.258203 · Cited by 300 · see citing works
Self-citationLeone, D. P., Genoud, S., Atanasoski, S., Grausenburger, R., Berger, P., METZGER, D., Macklin, W. B., Chambon, P., & Suter, U. (2003) · Molecular and Cellular Neuroscience · doi:10.1016/s1044-7431(03)00029-0 · Cited by 270 · see citing works
Self-citationAntonická, H. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg284 · Cited by 255 · see citing works
Díaz, F., Fukui, H., García, S., & Moraes, C. T. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01767-05 · Cited by 236 · see citing works
Self-citationDevelopmental switch in brain nutrient transporter expression in the rat
Vannucci, S. J., & Simpson, I. A. (2003) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00187.2003 · Cited by 235 · see citing works
Tekkök, S. B., Brown, A. M., Westenbroek, R., Pellerin, L., & Ransom, B. R. (2005) · Journal of Neuroscience Research · doi:10.1002/jnr.20573 · Cited by 224 · see citing works
Notch1 control of oligodendrocyte differentiation in the spinal cord
Genoud, S., Lappe-Siefke, C., Goebbels, S., Radtke, F., Aguet, M., Scherer, S. S., Suter, U., Nave, K.-A., & Mantei, N. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200202002 · Cited by 211 · see citing works
Self-citationViader, A., Golden, J. P., Baloh, R. H., Schmidt, R. E., Hunter, D. A., & Milbrandt, J. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0884-11.2011 · Cited by 197 · see citing works
Fukui, H., Diaz, F., Garcia, S., & Moraes, C. T. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705738104 · Cited by 185 · see citing works
Self-citationDíaz, F., Thomas, C. K., García, S., Hernandez, D., & Moraes, C. T. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi307 · Cited by 179 · see citing works
Self-citationJalil, M. A., Begum, L., Contreras, L., Pardo, B., Iijima, M., Li, M. X., Ramos, M., Mármol, P., Horiuchi, M., Shimotsu, K., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505286200 · Cited by 165 · see citing works
Gandhi, G. K., Cruz, N. F., Ball, K. K., & Dienel, G. A. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06333.x · Cited by 162 · see citing works
Immunocytochemical localization of glycerol-3-phosphate dehydrogenase in rat oligodendrocytes
Leveille, P. J., McGinnis, J. F., Maxwell, D. S., & De Vellis, J. (1980) · Brain Research · doi:10.1016/0006-8993(80)90397-2 · Cited by 135 · see citing works
Enhancing Central Nervous System Remyelination in Multiple Sclerosis
Dubois-Dalcq, M. E., ffrench‐Constant, C., & Franklin, R. J. M. (2005) · Neuron · doi:10.1016/j.neuron.2005.09.004 · Cited by 117 · see citing works
The Turnover of the Protein Components of Mitochondria from Rat Liver, Kidney, and Brain
Beattie, D. S., BASFORD, R. E., & Koritz, S. B. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99496-2 · Cited by 104 · see citing works
Ziabreva, I., Campbell, G. R., Rist, J. M., Zambonin, J. L., Rorbach, J., Wydro, M. M., Lassmann, H., Franklin, R. J. M., & Mahad, D. (2010) · Glia · doi:10.1002/glia.21052 · Cited by 103 · see citing works
Self-citationMetabolic substrates other than glucose support axon function in central white matter
Brown, A. M., Wender, R., & Ransom, B. R. (2001) · Journal of Neuroscience Research · doi:10.1002/jnr.10081 · Cited by 85 · see citing works
Pathophysiology and fate of hepatocytes in a mouse model of mitochondrial hepatopathies
Diaz, F., García, S., Hernandez, D., Regev, A., Rebelo, A. P., Oca‐Cossio, J., & Moraes, C. T. (2007) · Gut · doi:10.1136/gut.2006.119180 · Cited by 52 · see citing works
Self-citationEvidence for a higher glycolytic than oxidative metabolic activity in white matter of rat brain
Morland, C., Henjum, S., Iversen, E. G., Skrede, K. K., & Hassel, B. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.01.003 · Cited by 34 · see citing works
Localized proton MRS of animal brain in vivo: Models of human disorders
Michaelis, T., Boretius, S., & Frahm, J. (2008) · Progress in Nuclear Magnetic Resonance Spectroscopy · doi:10.1016/j.pnmrs.2008.11.001 · Cited by 26 · see citing works
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Oligodendroglia metabolically support axons and contribute to neurodegeneration
Lee, Y., Morrison, B. M., Li, Y., Lengacher, S., Farah, M. H., Hoffman, P. N., Liu, Y., Tsingalia, A., Jin, L., Zhang, P.-W., et al. (2012) · Nature · doi:10.1038/nature11314 · Cited by 1,664 · see citing works
Sugar for the brain: the role of glucose in physiological and pathological brain function
Mergenthaler, P., Lindauer, U., Dienel, G. A., & Meisel, A. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.07.001 · Cited by 1,612 · see citing works
Lactate in the brain: from metabolic end-product to signalling molecule
Magistretti, P. J., & Allaman, I. (2018) · Nature Reviews Neuroscience · doi:10.1038/nrn.2018.19 · Cited by 1,298 · see citing works
A Cellular Perspective on Brain Energy Metabolism and Functional Imaging
Magistretti, P. J., & Allaman, I. (2015) · Neuron · doi:10.1016/j.neuron.2015.03.035 · Cited by 1,285 · see citing works
Myelination of the Nervous System: Mechanisms and Functions
Nave, K., & Werner, H. B. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013101 · Cited by 1,000 · see citing works
Self-citationCell transplantation therapy for spinal cord injury
Assinck, P., Duncan, G. J., Hilton, B. J., Plemel, J. R., & Tetzlaff, W. (2017) · Nature Neuroscience · doi:10.1038/nn.4541 · Cited by 941 · see citing works
New Horizons in Diabetic Neuropathy: Mechanisms, Bioenergetics, and Pain
Feldman, E. L., Nave, K.-A., Jensen, T. S., & Bennett, D. L. H. (2017) · Neuron · doi:10.1016/j.neuron.2017.02.005 · Cited by 915 · see citing works
Self-citationThe Biology of Regeneration Failure and Success After Spinal Cord Injury
Tran, A. P., Warren, P. M., & Silver, J. (2018) · Physiological Reviews · doi:10.1152/physrev.00017.2017 · Cited by 883 · see citing works
Neurotransmitter-Triggered Transfer of Exosomes Mediates Oligodendrocyte–Neuron Communication
Frühbeis, C., Fröhlich, D., Kuo, W. P., Amphornrat, J., Thilemann, S., Saab, A. S., Kirchhoff, F., Möbius, W., Goebbels, S., Nave, K.-A., et al. (2013) · PLoS Biology · doi:10.1371/journal.pbio.1001604 · Cited by 812 · see citing works
Self-citationOligodendrocytes: Myelination and Axonal SupportPreprint
Simons, M., & Nave, K. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020479 · Cited by 862 · see citing works
Self-citationMyelin in the Central Nervous System: Structure, Function, and Pathology
Stadelmann, C., Timmler, S., Barrantes‐Freer, A., & Simons, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00031.2018 · Cited by 735 · see citing works
Herculano‐Houzel, S. (2014) · Glia · doi:10.1002/glia.22683 · Cited by 731 · see citing works
Multiple sclerosis progression: time for a new mechanism-driven framework
Kuhlmann, T., Moccia, M., Coetzee, T., Cohen, J. A., Correale, J., Graves, J., Marrie, R. A., Montalban, X., Yong, V. W., Thompson, A. J., et al. (2023) · The Lancet Neurology · doi:10.1016/s1474-4422(22)00289-7 · Cited by 667 · see citing works
Monocarboxylate transporters in cancer
Payen, V. L., Mina, E., Hée, V. F. V., Porporato, P. E., & Sonveaux, P. (2019) · Molecular Metabolism · doi:10.1016/j.molmet.2019.07.006 · Cited by 662 · see citing works
Regenerating CNS myelin — from mechanisms to experimental medicines
Franklin, R. J. M., & ffrench-Constant, C. (2017) · Nature Reviews Neuroscience · doi:10.1038/nrn.2017.136 · Cited by 647 · see citing works
Mechanisms of neurodegeneration and axonal dysfunction in multiple sclerosis
Friese, M. A., Schattling, B., & Fugger, L. (2014) · Nature Reviews Neurology · doi:10.1038/nrneurol.2014.37 · Cited by 628 · see citing works
Oligodendrocytes in development, myelin generation and beyond
Kuhn, S., Gritti, L., Crooks, D., & Dombrowski, Y. (2019) · Cells · doi:10.3390/cells8111424 · Cited by 625 · see citing works
Kang, S. H., Li, Y., Fukaya, M., Lorenzini, I., Cleveland, D. W., Ostrow, L. W., Rothstein, J. D., & Bergles, D. E. (2013) · Nature Neuroscience · doi:10.1038/nn.3357 · Cited by 599 · see citing works
Neuregulin-ERBB Signaling in the Nervous System and Neuropsychiatric Diseases
Mei, L., & Nave, K. (2014) · Neuron · doi:10.1016/j.neuron.2014.06.007 · Cited by 590 · see citing works
Self-citationNeuroinflammation in Alzheimer disease
Heneka, M. T., van der Flier, W. M., Jessen, F., Hoozemanns, J., Thal, D. R., Boche, D., Brosseron, F., Teunissen, C., Zetterberg, H., Jacobs, A. H., et al. (2025) · Nature Reviews Immunology · doi:10.1038/s41577-024-01104-7 · Cited by 638 · see citing works
Self-citationOligodendroglial NMDA receptors regulate glucose import and axonal energy metabolism
Saab, A. S., Tzvetavona, I. D., Trevisiol, A., Baltan, S., Dibaj, P., Kusch, K., Möbius, W., Goetze, B., Jahn, H. M., Huang, W., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.05.016 · Cited by 590 · see citing works
“This confirms that axons readily use lactate for ATP generation (Fünfschilling et al., 2012; Lee et al., 2012; Tekkök et al., 2005; Wyss et al., 2011).”
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Winkler, F., Venkatesh, H. S., Amit, M., Batchelor, T. T., Demir, İ. E., Deneen, B., Gutmann, D. H., Hervey‐Jumper, S. L., Kuner, T., Mabbott, D., et al. (2023) · Cell · doi:10.1016/j.cell.2023.02.002 · Cited by 578 · see citing works
In vivo evidence for a lactate gradient from astrocytes to neurons
Mächler, P., Wyss, M. T., Elsayed, M., Stobart, J., Gutierrez, R., von Faber-Castell, A., Kaelin, V., Zuend, M., San Martín, A., Romero-Gómez, I., et al. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2015.10.010 · Cited by 571 · see citing works
Myelin remodeling through experience-dependent oligodendrogenesis in the adult somatosensory cortex
Hughes, E. G., Orthmann-Murphy, J. L., Langseth, A. J., & Bergles, D. E. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0121-5 · Cited by 540 · see citing works
Liu, L., MacKenzie, K. R., Putluri, N., Maletić-Savatić, M., & Bellen, H. J. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.08.024 · Cited by 556 · see citing works
Regulatory T cells promote myelin regeneration in the central nervous system
Dombrowski, Y., O'Hagan, T., Dittmer, M., Penalva, R., Mayoral, S. R., Bankhead, P., Fleville, S., Eleftheriadis, G., Zhao, C., Naughton, M., et al. (2017) · Nature Neuroscience · doi:10.1038/nn.4528 · Cited by 533 · see citing works
Mild respiratory COVID can cause multi-lineage neural cell and myelin dysregulation
Fernández-Castañeda, A., Lu, P., Geraghty, A. C., Song, E., Lee, M.-H., Wood, J., O’Dea, M. R., Dutton, S., Shamardani, K., Nwangwu, K., et al. (2022) · Cell · doi:10.1016/j.cell.2022.06.008 · Cited by 521 · see citing works
Rapid production of new oligodendrocytes is required in the earliest stages of motor-skill learning
Xiao, L., Ohayon, D., McKenzie, I. A., Sinclair-Wilson, A., Wright, J. L., Fudge, A. D., Emery, B., Li, H., & Richardson, W. D. (2016) · Nature Neuroscience · doi:10.1038/nn.4351 · Cited by 507 · see citing works
Oligodendrocyte precursors migrate along vasculature in the developing nervous system
Tsai, H.-H., Niu, J., Munji, R., Davalos, D., Chang, J., Zhang, H., Tien, A.-C., Kuo, C. J., Chan, J. R., Daneman, R., et al. (2016) · Science · doi:10.1126/science.aad3839 · Cited by 483 · see citing works
Myelin dysfunction drives amyloid-β deposition in models of Alzheimer’s disease
Depp, C., Sun, T., Sasmita, A. O., Spieth, L., Berghoff, S. A., Nazarenko, T., Overhoff, K., Steixner-Kumar, A. A., Subramanian, S., Arinrad, S., et al. (2023) · Nature · doi:10.1038/s41586-023-06120-6 · Cited by 476 · see citing works
Self-citationMyelin Membrane Wrapping of CNS Axons by PI(3,4,5)P3-Dependent Polarized Growth at the Inner Tongue
Snaidero, N., Möbius, W., Czopka, T., Hekking, L. H. P., Mathisen, C., Verkleij, D., Goebbels, S., Edgar, J. M., Merkler, D., Lyons, D. A., et al. (2014) · Cell · doi:10.1016/j.cell.2013.11.044 · Cited by 451 · see citing works
Self-citationWhite matter and cognition: making the connection
Filley, C. M., & Fields, R. D. (2016) · Journal of Neurophysiology · doi:10.1152/jn.00221.2016 · Cited by 445 · see citing works
Oligodendrocyte‐microglia cross‐talk in the central nervous system
Peferoen, L., Kipp, M., van der Valk, P., van Noort, J. M., & Amor, S. (2014) · Immunology · doi:10.1111/imm.12163 · Cited by 438 · see citing works
Oligodendrocyte, Astrocyte, and Microglia Crosstalk in Myelin Development, Damage, and Repair
Domingues, H. S., Portugal, C. C., Socodato, R., & Relvas, J. B. (2016) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2016.00071 · Cited by 438 · see citing works
The restless brain: How intrinsic activity organizes brain function
Raichle, M. E. (2015) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2014.0172 · Cited by 433 · see citing works
Oligodendrocyte-Encoded HIF Function Couples Postnatal Myelination and White Matter Angiogenesis
Yuen, T. J., Silbereis, J. C., Griveau, A., Chang, S. M., Daneman, R., Fancy, S. P. J., Zahed, H., Maltepe, E., & Rowitch, D. H. (2014) · Cell · doi:10.1016/j.cell.2014.04.052 · Cited by 433 · see citing works
Sadick, J. S., O’Dea, M. R., Hasel, P., Dykstra, T., Faustin, A., & Liddelow, S. A. (2022) · Neuron · doi:10.1016/j.neuron.2022.03.008 · Cited by 415 · see citing works
The neurobiology of long COVID
Monje, M., & Iwasaki, A. (2022) · Neuron · doi:10.1016/j.neuron.2022.10.006 · Cited by 415 · see citing works
Monocarboxylate transporters in the brain and in cancer
Pérez‐Escuredo, J., Hée, V. F. V., Sboarina, M., Falces, J., Payen, V. L., Pellerin, L., & Sonveaux, P. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.03.013 · Cited by 407 · see citing works
van der Knaap, M. S., & Bugiani, M. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1739-1 · Cited by 403 · see citing works
Myelin Fat Facts: An Overview of Lipids and Fatty Acid Metabolism
Poitelon, Y., Kopec, A. M., & Belin, S. (2020) · Cells · doi:10.3390/cells9040812 · Cited by 394 · see citing works
Extracellular vesicles as mediators of neuron-glia communication
Frühbeis, C., Fröhlich, D., Kuo, W. P., & Krämer‐Albers, E. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00182 · Cited by 383 · see citing works
San Martín, A., Ceballo, S., Ruminot, I., Lerchundi, R., Frommer, W. B., & Barros, L. F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057712 · Cited by 361 · see citing works
Preservation of a remote fear memory requires new myelin formation
Pan, S., Mayoral, S. R., Choi, H. S., Chan, J. R., & Kheirbek, M. A. (2020) · Nature Neuroscience · doi:10.1038/s41593-019-0582-1 · Cited by 366 · see citing works
Mancusi, R. A., & Monje, M. (2023) · Nature · doi:10.1038/s41586-023-05968-y · Cited by 370 · see citing works
Schwann Cell MyelinationPreprint
Salzer, J. L. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a020529 · Cited by 365 · see citing works
Differentiation and maturation of oligodendrocytes in human three-dimensional neural cultures
Marton, R. M., Miura, Y., Sloan, S. A., Li, Q., Revah, O., Levy, R. J., Huguenard, J. R., & Pașca, S. P. (2019) · Nature Neuroscience · doi:10.1038/s41593-018-0316-9 · Cited by 362 · see citing works
Sankowski, R., Mader, S., & Valdés-Ferrer, S. I. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00028 · Cited by 351 · see citing works
Remyelination in multiple sclerosis: From basic science to clinical translation
Lubetzki, C., Zalc, B., Williams, A., Stadelmann, C., & Stankoff, B. (2020) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30140-x · Cited by 350 · see citing works
Enhancing myelin renewal reverses cognitive dysfunction in a murine model of Alzheimer’s disease
Chen, J.-F., Liu, K., Hu, B., Li, R.-R., Xin, W., Chen, H., Wang, F., Chen, L., Li, R.-X., Ren, S.-Y., et al. (2021) · Neuron · doi:10.1016/j.neuron.2021.05.012 · Cited by 346 · see citing works
Oligodendroglia: metabolic supporters of neurons
Philips, T., & Rothstein, J. D. (2017) · Journal of Clinical Investigation · doi:10.1172/jci90610 · Cited by 346 · see citing works
Individual Oligodendrocytes Have Only a Few Hours in which to Generate New Myelin Sheaths In Vivo
Czopka, T., ffrench‐Constant, C., & Lyons, D. A. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.013 · Cited by 332 · see citing works
Traumatic Brain Injury: Mechanistic Insight on Pathophysiology and Potential Therapeutic Targets
Thapa, K., Khan, H., Singh, T. G., & Kaur, A. (2021) · Journal of Molecular Neuroscience · doi:10.1007/s12031-021-01841-7 · Cited by 341 · see citing works
Glial glycolysis is essential for neuronal survival in Drosophila
Volkenhoff, A., Weiler, A., Letzel, M., Stehling, M., Klämbt, C., & Schirmeier, S. (2015) · Cell Metabolism · doi:10.1016/j.cmet.2015.07.006 · Cited by 339 · see citing works
The role of myelin and oligodendrocytes in axonal energy metabolism
Saab, A. S., Tzvetanova, I. D., & Nave, K. (2013) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2013.09.008 · Cited by 339 · see citing works
Self-citationMyelin plasticity: sculpting circuits in learning and memory
Xin, W., & Chan, J. R. (2020) · Nature Reviews Neuroscience · doi:10.1038/s41583-020-00379-8 · Cited by 329 · see citing works
Metabolic signaling by lactate in the brain
Barros, L. F. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.04.002 · Cited by 326 · see citing works
Mei, F., Lehmann‐Horn, K., Shen, Y. A., Rankin, K. A., Stebbins, K. J., Lorrain, D. S., Pekarek, K. L., Sagan, S. A., Xiao, L., Teuscher, C., et al. (2016) · eLife · doi:10.7554/elife.18246 · Cited by 323 · see citing works
Dynamics and Mechanisms of CNS Myelination
Bercury, K. K., & Macklin, W. B. (2015) · Developmental Cell · doi:10.1016/j.devcel.2015.01.016 · Cited by 320 · see citing works
Motor learning promotes remyelination via new and surviving oligodendrocytes
Bacmeister, C. M., Barr, H. J., McClain, C. R., Thornton, M. A., Nettles, D., Welle, C. G., & Hughes, E. G. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0637-3 · Cited by 310 · see citing works
The Therapeutic Potential of Metformin in Neurodegenerative Diseases
Rotermund, C., Machetanz, G., & Fitzgerald, J. C. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00400 · Cited by 310 · see citing works
van Tilborg, E., de Theije, C. G. M., van Hal, M., Wagenaar, N., de Vries, L. S., Benders, M. J. N. L., Rowitch, D. H., & Nijboer, C. H. A. (2017) · Glia · doi:10.1002/glia.23256 · Cited by 292 · see citing works
Mitochondrial Dysfunction and Multiple Sclerosis
de Barcelos, I. P., Troxell, R., & Graves, J. S. (2019) · Biology · doi:10.3390/biology8020037 · Cited by 243 · see citing works
Boyd, A. L., Zhang, H., & Williams, A. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1112-y · Cited by 284 · see citing works
Remyelination therapies: a new direction and challenge in multiple sclerosis
Plemel, J. R., Liu, W., & Yong, V. W. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.115 · Cited by 281 · see citing works
A large fraction of neocortical myelin ensheathes axons of local inhibitory neurons
Micheva, K. D., Wolman, D. N., Mensh, B. D., Pax, E., Buchanan, J., Smith, S. J., & Bock, D. D. (2016) · eLife · doi:10.7554/elife.15784 · Cited by 271 · see citing works
Neuroprotection and repair in multiple sclerosis
Franklin, R. J. M., ffrench‐Constant, C., Edgar, J. M., & Smith, K. J. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.200 · Cited by 274 · see citing works
Self-citationLactate as a Metabolite and a Regulator in the Central Nervous System
Proia, P., Liegro, C. M. D., Schiera, G., Fricano, A., & Liegro, I. D. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17091450 · Cited by 280 · see citing works
Myelin plasticity and nervous system function
Monje, M. (2018) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-080317-061853 · Cited by 274 · see citing works
Viader, A., Sasaki, Y., Kim, S., Strickland, A. M., Workman, C. S., Yang, K., Gross, R. W., & Milbrandt, J. (2013) · Neuron · doi:10.1016/j.neuron.2013.01.012 · Cited by 270 · see citing works
Xiang, X., Wind, K., Wiedemann, T., Blume, T., Shi, Y., Briel, N., Beyer, L., Biechele, G., Eckenweber, F., Zatcepin, A., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe5640 · Cited by 268 · see citing works
White matter involvement after TBI: clues to axon and myelin repair capacity
Armstrong, R. C., Mierzwa, A. J., Marion, C. M., & Sullivan, G. M. (2016) · Experimental Neurology · doi:10.1016/j.expneurol.2015.02.011 · Cited by 262 · see citing works
Energy metabolism in ALS: an underappreciated opportunity?
Vandoorne, T., Bock, K. D., & Bosch, L. V. D. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1835-x · Cited by 260 · see citing works
New perspectives in diabetic neuropathy
Eid, S., Rumora, A. E., Beirowski, B., Bennett, D., Hur, J., Savelieff, M. G., & Feldman, E. L. (2023) · Neuron · doi:10.1016/j.neuron.2023.05.003 · Cited by 276 · see citing works
Pleiotropic Mitochondria: The Influence of Mitochondria on Neuronal Development and Disease
Rangaraju, V., Lewis, T. L., Hirabayashi, Y., Bergami, M., Motori, E., Cartoni, R., Kwon, S., & Courchet, J. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1157-19.2019 · Cited by 257 · see citing works
Myelin dynamics: protecting and shaping neuronal functions
Saab, A. S., & Nave, K. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.09.013 · Cited by 259 · see citing works
Self-citationNew insights on schwann cell development
Monk, K. R., Feltri, M. L., & Taveggia, C. (2015) · Glia · doi:10.1002/glia.22852 · Cited by 256 · see citing works
Oligodendroglia: metabolic supporters of axons
Morrison, B. M., Lee, Y., & Rothstein, J. D. (2013) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.07.007 · Cited by 252 · see citing works
Glial cells in amyotrophic lateral sclerosis
Philips, T., & Rothstein, J. D. (2014) · Experimental Neurology · doi:10.1016/j.expneurol.2014.05.015 · Cited by 255 · see citing works
Programming axonal mitochondrial maintenance and bioenergetics in neurodegeneration and regeneration
Cheng, X., Huang, N., & Sheng, Z. (2022) · Neuron · doi:10.1016/j.neuron.2022.03.015 · Cited by 253 · see citing works
Bergersen, L. H. (2014) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1038/jcbfm.2014.206 · Cited by 255 · see citing works
Wrapped to Adapt: Experience-Dependent Myelination
Mount, C., & Monje, M. (2017) · Neuron · doi:10.1016/j.neuron.2017.07.009 · Cited by 251 · see citing works
Marton, R. M., & Pașca, S. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.11.004 · Cited by 202 · see citing works
Mechanisms regulating the development of oligodendrocytes and central nervous system myelin.
Mitew, S., Hay, C., Peckham, H., Xiao, J., Koenning, M., & Emery, B. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2013.11.029 · Cited by 259 · see citing works
The Axon-Myelin Unit in Development and Degenerative Disease
Stassart, R. M., Möbius, W., Nave, K.-A., & Edgar, J. M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00467 · Cited by 246 · see citing works
Self-citationSchwann cell functions in peripheral nerve development and repair
Bosch-Queralt, M., Fledrich, R., & Stassart, R. M. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105952 · Cited by 244 · see citing works
Oxidative stress and its impact on neurons and glia in multiple sclerosis lesions
Lassmann, H., & van Horssen, J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.09.018 · Cited by 240 · see citing works
Peroxisome proliferator-activated receptor γ (PPARγ): A master gatekeeper in CNS injury and repair
Cai, W., Yang, T., Liu, H., Han, L., Zhang, K., Hu, X., Zhang, X., Yin, K., Gao, Y., Bennett, M. V. L., et al. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.10.002 · Cited by 238 · see citing works
Oxidative Stress‐Related Mechanisms in Schizophrenia Pathogenesis and New Treatment Perspectives
Ermakov, E. A., Dmitrieva, E. M., Parshukova, D. A., Kazantseva, D. V., Vasilieva, A. R., & Smirnova, L. P. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/8881770 · Cited by 252 · see citing works
MEG3 activates necroptosis in human neuron xenografts modeling Alzheimer’s disease
Balusu, S., Horré, K., Thrupp, N., Craessaerts, K., Snellinx, A., Serneels, L., T’Syen, D., Chrysidou, I., Arranz, A. M., Sierksma, A. S. R., et al. (2023) · Science · doi:10.1126/science.abp9556 · Cited by 234 · see citing works
Zirngibl, M., Assinck, P., Sizov, A., Caprariello, A. V., & Plemel, J. R. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00538-8 · Cited by 233 · see citing works
Misu, T., Höftberger, R., Fujihara, K., Wimmer, I., Takai, Y., Nishiyama, S., Nakashima, I., Konno, H., Bradl, M., Garzuly, F., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1116-7 · Cited by 233 · see citing works
Myelin damage and repair in pathologic CNS: challenges and prospects
Alizadeh, A., Dyck, S. M., & Karimi‐Abdolrezaee, S. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00035 · Cited by 230 · see citing works
Rajeev, V., Chai, Y. L., Poh, L., Selvaraji, S., Fann, D. Y., Jo, D., Silva, T. M. D., Drummond, G. R., Sobey, C. G., Arumugam, T. V., et al. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01590-1 · Cited by 237 · see citing works
Non‐signalling energy use in the brain
Engl, E., & Attwell, D. (2015) · The Journal of Physiology · doi:10.1113/jphysiol.2014.282517 · Cited by 230 · see citing works
Glial Cells Shape Pathology and Repair After Spinal Cord Injury
Gaudet, A. D., & Fonken, L. K. (2018) · Neurotherapeutics · doi:10.1007/s13311-018-0630-7 · Cited by 232 · see citing works
Disease-associated oligodendrocyte responses across neurodegenerative diseases
Pandey, S., Shen, K., Lee, S.-H., Shen, Y.-A. A., Wang, Y., Otero-García, M., Kotova, N., Vito, S. T., Laufer, B. I., Newton, D. F., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111189 · Cited by 227 · see citing works
Multiple sclerosis animal models: a clinical and histopathological perspective
Kipp, M., Nyamoya, S., Hochstrasser, T., & Amor, S. (2017) · Brain Pathology · doi:10.1111/bpa.12454 · Cited by 226 · see citing works
On Myelinated Axon Plasticity and Neuronal Circuit Formation and Function
Almeida, R. G., & Lyons, D. A. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.3185-16.2017 · Cited by 221 · see citing works
Mechanisms of lysophosphatidylcholine‐induced demyelination: A primary lipid disrupting myelinopathy
Plemel, J. R., Michaels, N. J., Weishaupt, N., Caprariello, A. V., Keough, M. B., Rogers, J. A., Yukseloglu, A., Lim, J., Patel, V. V., Rawji, K. S., et al. (2018) · Glia · doi:10.1002/glia.23245 · Cited by 220 · see citing works
- Authors
- Fünfschilling, U., Supplie, L. M., Mahad, D., Boretius, S., Saab, A. S., Edgar, J., Brinkmann, B. G., Kassmann, C. M., Tzvetanova, I. D., Möbius, W., Diaz, F., Meijer, D., Suter, U., Hamprecht, B., Sereda, M. W., Moraes, C. T., Frahm, J., Goebbels, S., & Nave, K.-A.
- Affiliations
- Max Planck Institute of Experimental Medicine (DE)
- Max Planck Society (DE)
- Newcastle University (GB)
- Erasmus MC (NL)
- ETH Zurich (CH)
- University of Miami (US)
- Corresponding author
- Nave, Klaus-Armin
- ORCID
- Venue
- Nature
- Published
- 2012-04-29
- Volume
- 485
- Issue
- 7399
- Pages
- 517-521
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC3613737
- OpenAlex
- W2085029391
- Cited by
- 1,523
- References
- 33
- Citations by year
- 2026: 121 · 2025: 120 · 2024: 127 · 2023: 107 · 2022: 125 · 2021: 142 · 2020: 121 · 2019: 107 · 2018: 91 · 2017: 128 · 2016: 95 · 2015: 93 · 2014: 64 · 2013: 65 · 2012: 13
- FWCI
- 25.34
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- EUR Research Repository (Erasmus University Rotterdam) (submittedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- ENLIGHTEN (Jurnal Bimbingan dan Konseling Islam) (submittedVersion)
- GRO (submittedVersion, cc-by)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Wellcome Trust (078415)
- Topics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Health Sciences › Medicine › Pathology and Forensic Medicine › Multiple Sclerosis Research Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- oligodendrocytes, myelination, aerobic glycolysis, lactate, mitochondrial cytochrome c oxidase, COX10, axonal integrity, demyelination, Schwann cells, white matter, brain lactate, mitochondrial respiration
- MeSH terms
- Action Potentials, Animals, Axons, Brain, Cell Survival, Electron Transport Complex IV, Demyelinating Diseases, Glycolysis, Membrane Proteins, Mitochondria, Myelin Sheath, Magnetic Resonance Spectroscopy, Oligodendroglia, Protons, Schwann Cells, Time Factors, Cell Respiration, Lactic Acid, Alkyl and Aryl Transferases, Mutant Proteins, Mice
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