The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source doesn’t support the claim as written.
In the citing paper
“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
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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]
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
Experimental — accuracy not yet measured
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
Experimental — accuracy not yet measuredThe source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
Experimental — accuracy not yet measuredThe cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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]
The cited source says what the claim attributes to it.
In the citing paper
“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
The cited source says what the claim attributes to it.
In the citing paper
“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
In the citing paper
“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
In the citing paper
“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
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Pellerin, L., & Magistretti, P. J. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.22.10625 · Cited by 2,927
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
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
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
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
Myelination and the trophic support of long axons
Nave, K.-A. (2010) · Nature Reviews Neuroscience · doi:10.1038/nrn2797 · Cited by 648
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
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
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
Self-citation
Cited by
Sorted by citations
Items 801–900 of 1,000
Pandya, J. D., Leung, L. Y., Hwang, H. M., Yang, X., Deng‐Bryant, Y., & Shear, D. A. (2021) · Journal of Neurotrauma · doi:10.1089/neu.2020.7379 · Cited by 19
Bioenergetic Impairment in the Neuro-Glia-Vascular Unit: An Emerging Physiopathology during Aging
Yuan, M., Wang, Y., Wang, S., Huang, Z., Jin, F., Zou, Q., Li, J., Pu, Y., & Cai, Z. (2021) · Aging and Disease · doi:10.14336/ad.2021.04017 · Cited by 20
Dysfunction of the oligodendrocytes in amyotrophic lateral sclerosis
Gong, Z., Ba, L., & Zhang, M. (2022) · Journal of Biomedical Research · doi:10.7555/jbr.36.20220009 · Cited by 21
Rossi, G., Ordazzo, G., Vanni, N. N., Castoldi, V., Iannielli, A., Silvestre, D. D., Bellini, E. N., Bernardo, L., Giannelli, S. G., Luoni, M., et al. (2023) · eLife · doi:10.7554/elife.81779 · Cited by 19
Moura, R. P., Carvalho, E. D., Martins, C., Rieux, A. D., Pêgo, A. P., & Sarmento, B. F. C. C. (2023) · Journal of Controlled Release · doi:10.1016/j.jconrel.2023.04.034 · Cited by 19
Huang, Z., Xu, P., Hess, D. C., & Zhang, Q. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00457-2 · Cited by 20
Multiple Sclerosis: Basic and Clinical
Buzzard, K. A., Chan, W. H., Kilpatrick, T. J., & Murray, S. S. (2017) · Advances in neurobiology · doi:10.1007/978-3-319-57193-5_8 · Cited by 26
Al‐Khawaga, S., AlRayahi, J., Khan, F., Saraswathi, S., Hasnah, R., Haris, B., Mohammed, I., Abdelalim, E. M., & Hussain, K. (2019) · Frontiers in Pediatrics · doi:10.3389/fped.2019.00299 · Cited by 19
Neuroglia in Psychiatric Disorders
Scuderi, C., Verkhratsky, A., Parpura, V., & Li, B. (2021) · Advances in neurobiology · doi:10.1007/978-3-030-77375-5_1 · Cited by 19
Komin, N., Moein, M., Ellisman, M. H., & Skupin, A. (2015) · Neural Plasticity · doi:10.1155/2015/683490 · Cited by 19
Miller, N. M., Shriver, L. P., Bodiga, V. L., Ray, A., Basu, S., Ahuja, R., Jana, A., Pahan, K., & Dittel, B. N. (2013) · ASN NEURO · doi:10.1042/an20120087 · Cited by 19
Energy metabolism in neuronal/glial induction and in iPSC models of brain disorders
Mlody, B., Lorenz, C., Inak, G., & Prigione, A. (2016) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2016.02.018 · Cited by 20
Astrocyte Sodium Signalling and Panglial Spread of Sodium Signals in Brain White Matter
Moshrefi-Ravasdjani, B., Hammel, E. L., Kafitz, K. W., & Rose, C. R. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2197-9 · Cited by 19
Differentiation of human olfactory bulb‐derived neural stem cells toward oligodendrocyte
Marei, H. E. S., Shouman, Z., Althani, A., Afifi, N. M., Abdelmaksoud, A., Lashen, S., Hasan, A., Caceci, T., Rizzi, R., Cenciarelli, C., et al. (2017) · Journal of Cellular Physiology · doi:10.1002/jcp.26008 · Cited by 19
Reduced apparent fiber density in the white matter of premature-born adults
Menegaux, A., Hedderich, D. M., Bäuml, J., Manoliu, A., Daamen, M., Berg, R., Preibisch, C., Zimmer, C., Boecker, H., Bartmann, P., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-73717-6 · Cited by 20
Fang, M., Lu, L., Lou, J., Ou, J. T., Yu, Q., Tao, X., Zhu, J., & Lin, Z. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04549-y · Cited by 18
Autophagy in alzheimer disease pathogenesis and its therapeutic values
Angst, G., Jia, N., Esqueda, L. T., Fan, Y., Cai, Q., & Wang, C. (2025) · Autophagy Reports · doi:10.1080/27694127.2025.2471677 · Cited by 22
Role of monocarboxylate transporters in cancer immunology and their therapeutic potential
Faghihkhorasani, F., Moosavi, M., Abdulwahid, A. R. R., Kavei, M., Karimi, S., Karimi, M. S., Vezvaei, P., Varkiani, M. M., Aref, A. R., & Ebrahimi, N. (2025) · British Journal of Pharmacology · doi:10.1111/bph.70110 · Cited by 24
Zuroff, L. R., Farkhondeh, V., Bove, R. M., & Green, A. (2025) · Drugs · doi:10.1007/s40265-025-02212-x · Cited by 20
Riboni-Verri, G., McMurran, C. E., Mukherjee, T., Daruwalla, C., Holland, J., Gautam, R., Chen, B. S., Cutting, E., Qian, W., MacManus, D. G., et al. (2025) · Trials · doi:10.1186/s13063-025-09254-2 · Cited by 18
Astrocyte Mitochondria in White-Matter Injury
Nguyen, H., Zerimech, S., & Baltan, S. (2021) · Neurochemical Research · doi:10.1007/s11064-021-03239-8 · Cited by 18
Sensory neurons display cell-type-specific vulnerability to loss of neuron-glia interactions
Elbaz, B., Yang, L., Vardy, M., Isaac, S., Rader, B. L., Kawaguchi, R., Traka, M., Woolf, C. J., Renthal, W. R., & Popko, B. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111130 · Cited by 18
Yadav, V., Mythri, C., & Kumarasamy, M. (2024) · Brain Behavior and Immunity Integrative · doi:10.1016/j.bbii.2024.100048 · Cited by 22
Li, Q., Liu, S., Zheng, T., Li, M., Qi, B., Zhou, L., Liu, B., Ma, D., Zhao, C., & Chen, Z. (2024) · Stem Cell Research & Therapy · doi:10.1186/s13287-024-03651-1 · Cited by 19
Hu, X., Zhu, Q., Lou, T., Hu, Q., Li, H., Xu, Y., Niu, X., He, L., Huang, H., Qiu, M. S., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2405152121 · Cited by 18
Modeling the natural history of Pelizaeus–Merzbacher disease
Mayer, J. A., Griffiths, I. R., Goldman, J. E., Smith, C. M., Cooksey, E., Radcliff, A. B., & Duncan, I. D. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.12.023 · Cited by 18
Why monkeys do not get multiple sclerosis (spontaneously)
Bove, R. M. (2018) · Evolution Medicine and Public Health · doi:10.1093/emph/eoy002 · Cited by 19
Seeing Is Believing: Myelin Dynamics in the Adult CNS
Swire, M., & ffrench‐Constant, C. (2018) · Neuron · doi:10.1016/j.neuron.2018.05.005 · Cited by 18
An in vitro model for studying CNS white matter: functional properties and experimental approaches
Bijland, S., Thomson, G., Euston, M., Michail, K., Thümmler, K., Mücklisch, S., Crawford, C. L., Barnett, S. C., McLaughlin, M., Anderson, T. J., et al. (2019) · F1000Research · doi:10.12688/f1000research.16802.1 · Cited by 17
Self-citationThe Application of Neural Stem/Progenitor Cells for Regenerative Therapy of Spinal Cord Injury
Yu, C., Xia, K., Gong, Z., Ying, L., Shu, J., Zhang, F., Chen, Q., Li, F., & Liang, C. (2019) · Current Stem Cell Research & Therapy · doi:10.2174/1574888x14666190329095638 · Cited by 18
Targeting mitochondria to protect axons in progressive MS
Campbell, G. R., Licht‐Mayer, S., & Mahad, D. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.05.012 · Cited by 18
Self-citationProgressive axonopathy when oligodendrocytes lack the myelin protein CMTM5
Buscham, T. J., Eichel-Vogel, M. A., Steyer, A. M., Jahn, O., Strenzke, N., Dardawal, R., Memhave, T. R., Siems, S. B., Müller, C., Meschkat, M., et al. (2022) · eLife · doi:10.7554/elife.75523 · Cited by 18
Self-citationShakhbazau, A., Schenk, G. J., Hay, C. M., Kawasoe, J. H., Klaver, R., Yong, V. W., Geurts, J. J. G., & van Minnen, J. (2016) · Molecular Biology Reports · doi:10.1007/s11033-016-3990-2 · Cited by 18
Late nonstochastic changes in pig skin after beta irradiation.
Peel, D. M., Hopewell, J. W., Wells, J., & Charles, M. W. (1985) · PubMed · Cited by 18
Myelin lipids as nervous system energy reservesPreprint
Asadollahi, E., Trevisiol, A., Saab, A. S., Looser, Z. J., Dibaj, P., Kusch, K., Ruhwedel, T., Möbius, W., Jahn, O., Baes, M. I., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.24.481621 · Cited by 18
Self-citationAnimal Weight Is an Important Variable for Reliable Cuprizone-Induced Demyelination
Leopold, P., Schmitz, C., & Kipp, M. (2019) · Journal of Molecular Neuroscience · doi:10.1007/s12031-019-01312-0 · Cited by 17
What Are the Roles of Oligodendrocyte Precursor Cells in Normal and Pathologic Conditions?
Benarroch, E. E. (2023) · Neurology · doi:10.1212/wnl.0000000000208000 · Cited by 21
Intrinsic organization of the corpus callosum
Barbaresi, P., Fabri, M., Lorenzi, T., Sagrati, A., & Morroni, M. (2024) · Frontiers in Physiology · doi:10.3389/fphys.2024.1393000 · Cited by 20
The immunological role of oligodendrocytes: beyond myelin maintenance
Pasquini, J. M., & Correale, J. D. (2025) · Discovery Immunology · doi:10.1093/discim/kyaf005 · Cited by 16
Oligodendrocytes and myelination: pioneering new frontiers in cognitive neuroscience
Zhang, N., Yi, R., Zhong, F., Lu, Y., Chen, W., Ke, Z., Zhang, Y., Zhou, L., Wang, P., & Wei, L. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1618468 · Cited by 22
González, G. M., Hart, B. A. ‘., Bugiani, M., Plemel, J. R., Schenk, G. J., Kooij, G., & Luchicchi, A. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02923-1 · Cited by 20
Esmael, A., Talaat, M., Egilla, H., & Eltoukhy, K. (2021) · Neurological Research · doi:10.1080/01616412.2021.1893567 · Cited by 17
Neuronal metabolism in learning and memory: The anticipatory activity perspective
Alexandrov, Y. I., & Pletnikov, M. V. (2022) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2022.104664 · Cited by 20
Increased white matter glycolysis in humans with cerebral small vessel disease
Brier, M. R., Blazey, T., Raichle, M. E., Morris, J. C., Benzinger, T. L. S., Vlassenko, A. G., Snyder, A. Z., & Goyal, M. S. (2022) · Nature Aging · doi:10.1038/s43587-022-00303-y · Cited by 16
Forston, M. D., Wei, G. Z., Chariker, J. H., Stephenson, T., Andres, K. R., Glover, C., Rouchka, E. C., Whittemore, S. R., & Hetman, M. (2023) · Scientific Reports · doi:10.1038/s41598-023-48425-6 · Cited by 17
Zhu, T., Wang, H., Liu, P.-M., Gu, H., Pan, W., Zhao, M., Hashimoto, K., & Yang, J. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106375 · Cited by 17
Lineage-specific changes in mitochondrial properties during neural stem cell differentiation
Soares, R., Lourenço, D. M., Mota, I. F., Sebastião, A. M., Xapelli, S., & Morais, V. A. (2024) · Life Science Alliance · doi:10.26508/lsa.202302473 · Cited by 16
Food for thought: Impact of metabolism on neuronal excitability
Katsu-Jiménez, Y., Alves, R. M. P., & Giménez-Cassina, A. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.03.002 · Cited by 18
Embracing oligodendrocyte diversity in the context of perinatal injury
Cunningham, L. A., Newville, J., & Jantzie, L. L. (2017) · Neural Regeneration Research · doi:10.4103/1673-5374.217320 · Cited by 20
Glial Cell Evolution: The Origins of a Lipid Store
Nave, K., Tzvetanova, I. D., & Schirmeier, S. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.10.011 · Cited by 20
Self-citationPrefrontal cortex NG2 glia undergo a developmental switch in their responsiveness to exercise
Tomlinson, L., Huang, P. H., & Colognato, H. (2018) · Developmental Neurobiology · doi:10.1002/dneu.22590 · Cited by 19
Maintenance mechanisms of circuit-integrated axons
Mariano, V., Domıńguez-Iturza, N., Neukomm, L. J., & Bagni, C. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.08.007 · Cited by 18
Yakimov, V., Schweiger, F., Zhan, J., Behrangi, N., Horn, A., Schmitz, C., Hochstrasser, T., & Kipp, M. (2019) · Histochemistry and Cell Biology · doi:10.1007/s00418-019-01786-4 · Cited by 17
Role of Brain Glycogen During Ischemia, Aging and Cell-to-Cell Interactions
Bastian, C., Quinn, J. P., Doherty, C. M., Franke, C., Faris, A. E. R., Brunet, S., & Baltan, S. (2019) · Advances in neurobiology · doi:10.1007/978-3-030-27480-1_12 · Cited by 18
Spinal Cord Injury — Healing from Within
Monje, M. (2021) · New England Journal of Medicine · doi:10.1056/nejmcibr2030836 · Cited by 17
White, N., & Sakiyama‐Elbert, S. E. (2018) · Developmental Dynamics · doi:10.1002/dvdy.24680 · Cited by 17
An overview of the human brain myelin proteome and differences associated with schizophrenia
Martins‐de‐Souza, D., Guest, P. C., Reis‐de‐Oliveira, G., Schmitt, A., Falkai, P., & Turck, C. W. (2020) · The World Journal of Biological Psychiatry · doi:10.1080/15622975.2020.1789217 · Cited by 17
Djannatian, M., Weikert, U., Safaiyan, S., Wrede, C., Deichsel, C., Kislinger, G., Ruhwedel, T., Campbell, D. S., van Ham, T. J., Schmid, B., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.02.02.429485 · Cited by 17
Self-citationBCAS1-positive oligodendrocytes enable efficient cortical remyelination in multiple sclerosis
Bergner, C. G., van der Meer, F., Franz, J., Vakrakou, A., Würfel, T., Nessler, S., Schäfer, L., Nau-Gietz, C., Winkler, A., Lagumersindez-Denis, N., et al. (2025) · Brain · doi:10.1093/brain/awae293 · Cited by 16
Neuroinflammation: An Oligodendrocentric View
Festa, L. K., Jordan‐Sciutto, K. L., & Grinspan, J. B. (2025) · Glia · doi:10.1002/glia.70007 · Cited by 18
Martins‐de‐Souza, D., Carvalho, P. C., Schmitt, A., Junqueira, M., Nogueira, F. C. S., Turck, C. W., & Domont, G. B. (2013) · Journal of Proteome Research · doi:10.1021/pr4009157 · Cited by 16
PAM (PIK3/AKT/mTOR) signaling in glia: potential contributions to brain tumors in aging
Duggan, M. R., Weaver, M. W., & Khalili, K. (2021) · Aging · doi:10.18632/aging.202459 · Cited by 16
Blocking mitochondrial calcium release in Schwann cells prevents demyelinating neuropathies
Gonzalez, S., Berthelot, J., Jiner, J., Perrin-Tricaud, C., Fernando, R. N., Chrast, R., Lenaers, G., & Tricaud, N. (2016) · Journal of Clinical Investigation · doi:10.1172/jci84505 · Cited by 16
RetractedHörner, M., Groh, J., Klein, D., Ilg, W., Schöls, L. J., Santos, S. D., Bergmann, A., Klebe, S., Cauhapé, M., Branchu, J., et al. (2022) · Experimental Neurology · doi:10.1016/j.expneurol.2022.114119 · Cited by 15
Li, T., Wang, J., Wang, H., Yang, Y., Wang, S., Huang, N., Wang, F., Gao, X., Niu, J., Li, Z., et al. (2018) · Glia · doi:10.1002/glia.23450 · Cited by 16
Falkai, P., Raabe, F. J., Bogerts, B., Schneider-Axmann, T., Malchow, B., Tatsch, L., Huber, V., Slapakova, L., Dobrowolny, H., Schmitz, C., et al. (2019) · European Archives of Psychiatry and Clinical Neuroscience · doi:10.1007/s00406-019-01067-0 · Cited by 16
Neuronal Maturation: Challenges and Opportunities in a Nascent Field
Bradke, F., Giovanni, S. D., & Fawcett, J. W. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.02.005 · Cited by 16
Oligodendroglial Epigenetics, from Lineage Specification to Activity-Dependent Myelination
Pruvost, M., & Moyon, S. (2021) · Life · doi:10.3390/life11010062 · Cited by 18
Clinical Applications of Myelin Plasticity for Remyelinating Therapies in Multiple Sclerosis
Pan, S., & Chan, J. R. (2021) · Annals of Neurology · doi:10.1002/ana.26196 · Cited by 17
Normal lactate concentration range in the neonatal brain
Tomiyasu, M., Aida, N., Shibasaki, J., Tachibana, Y., Endo, M., Nozawa, K., Shimizu, E., Tsuji, H., & Obata, T. (2016) · Magnetic Resonance Imaging · doi:10.1016/j.mri.2016.07.006 · Cited by 16
Cre‐inducible site‐specific recombination in zebrafish oligodendrocytes
Pinzon‐Olejua, A., Welte, C., Chekuru, A., Bosak, V., Brand, M., Hans, S., & Stuermer, C. A. O. (2016) · Developmental Dynamics · doi:10.1002/dvdy.24458 · Cited by 13
Joseph, S., Vingill, S., Jahn, O., Fledrich, R., Werner, H. B., Katona, I., Möbius, W., Mitkovski, M., Huang, Y., Weis, J., et al. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.3094-18.2019 · Cited by 15
Self-citationZhu, X., Chen, W., Pinho, R. A., & Thirupathi, A. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1598419 · Cited by 18
Excitable Axonal Domains Adapt to Sensory Deprivation in the Olfactory System
George, N. M., Polese, A. G., Merle, L., Macklin, W. B., & Restrepo, D. (2022) · Journal of Neuroscience · doi:10.1523/jneurosci.0305-21.2021 · Cited by 16
Resistance Mechanisms of the Metastatic Tumor Microenvironment to Anti-Angiogenic Therapy
Schiffmann, L. M., Bruns, C. J., & Schmidt, T. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.897927 · Cited by 15
Ragupathy, H., Vukku, M., & Barodia, S. K. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241914421 · Cited by 16
RNA-binding proteins as versatile metabolic regulators
Koletsou, E., & Huppertz, I. (2025) · npj Metabolic Health and Disease · doi:10.1038/s44324-024-00044-z · Cited by 17
The Role of Mammalian Glial Cells in Circadian Rhythm Regulation
Chi-Castañeda, D., & Ortega, A. (2017) · Neural Plasticity · doi:10.1155/2017/8140737 · Cited by 15
Lee, S. W., Park, J. B., Kim, H. J., Kim, H. Y., Lee, S. Y., Chung, W. T., Shin, Y. K., Park, H. T., Rho, J. H., & Yoo, Y. H. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.07.034 · Cited by 15
Mitchell, R., Campbell, G. R., Mikolajczak, M., McGill, K., Mahad, D., & Fleetwood‐Walker, S. (2019) · Molecular Neurobiology · doi:10.1007/s12035-018-1455-4 · Cited by 16
Self-citationBergaglio, T., Luchicchi, A., & Schenk, G. J. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.610295 · Cited by 16
Reassessing associations between white matter and behaviour with multimodal microstructural imaging
Lazari, A., Salvan, P., Cottaar, M., Papp, D., van der Werf, O. J., Johnstone, A., Sanders, Z., Sampaio‐Baptista, C., Eichert, N., Miyamoto, K., et al. (2021) · Cortex · doi:10.1016/j.cortex.2021.08.017 · Cited by 15
SARM1 Depletion Slows Axon Degeneration in a CNS Model of Neurotropic Viral Infection
Crawford, C. L., Antoniou, C., Komarek, L., Schultz, V., Donald, C. L., Montague, P., Barnett, S. C., Linington, C., Willison, H. J., Kohl, A., et al. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.860410 · Cited by 15
Self-citationSuo, N., He, B., Cui, S.-H., Yang, Y., Wang, M., Yuan, Q., & Xie, X. (2022) · Glia · doi:10.1002/glia.24233 · Cited by 15
Prognosis in substance abuse-related acute toxic leukoencephalopathy: A scoping review
Macchi, Z. A., Carlisle, T. C., & Filley, C. M. (2022) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2022.120420 · Cited by 17
Deng, J., Gu, J., Zhao, X., Yan, B., Wang, L., Ji, G., & Huang, C. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.123356 · Cited by 15
Perinatal Asphyxia in Rat Alters Expression of Novel Schizophrenia Risk Genes
Paparelli, A., Iwata, K., Wakuda, T., Iyegbe, C. O., Murray, R. M., & Takei, N. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00341 · Cited by 15
Tackling mitochondrial diversity in brain function: from animal models to human brain organoids
Menacho, C., & Prigione, A. (2020) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2020.105760 · Cited by 15
Gotoh, H., Nomura, T., & Ono, K. (2016) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1177/0271678x16665380 · Cited by 15
Exploring Autophagy Inducing Molecules: Targeting Diverse Pathways in Alzheimer's Disease Management
Singh, B., Mahajan, S., Abdella, S., Khan, R., & Garg, S. (2025) · Medicinal Research Reviews · doi:10.1002/med.70013 · Cited by 16
Signaling roles for astrocytic lipid metabolism in brain function
Bolaños, J. P., & Almeida, Á. (2026) · EMBO Reports · doi:10.1038/s44319-025-00683-3 · Cited by 16
Cannabinoids as Glial Cell Modulators in Ischemic Stroke: Implications for Neuroprotection
Vicente-Acosta, A., Ceprián, M., Sobrino, P., Pazos, M. R., & Loría, F. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.888222 · Cited by 15
Recruitment of endogenous CNS stem cells for regeneration in demyelinating disease
Murphy, N. A., & Franklin, R. J. M. (2017) · Progress in brain research · doi:10.1016/bs.pbr.2016.12.013 · Cited by 14
Oligodendrocyte differentiation
Mathews, E. S., & Appel, B. (2016) · Methods in cell biology · doi:10.1016/bs.mcb.2015.12.004 · Cited by 13
Efficacy of exogenous pyruvate in TremblerJ mouse model of Charcot‐Marie‐Tooth neuropathy
Sahenk, Z., YALVAÇ, M. E., Amornvit, J., Arnold, W. D., Chen, L., Shontz, K. M., & Lewis, S. (2018) · Brain and Behavior · doi:10.1002/brb3.1118 · Cited by 14
Could an Impairment in Local Translation of mRNAs in Glia be Contributing to Pathogenesis in ALS?
Barton, S. K., Gregory, J. M., Chandran, S., & Turner, B. J. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00124 · Cited by 18
Sutiwisesak, R., Burns, T. C., Rodriguez, M., & Warrington, A. E. (2021) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2021.1942840 · Cited by 14
Involvement of GPR17 in Neuronal Fibre Outgrowth
Braune, M., Scherf, N., Heine, C., Sygnecka, K., Pillaiyar, T., Parravicini, C., Heimrich, B., Abbracchio, M. P., Müller, C. E., & Franke, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222111683 · Cited by 14
Tricaud, N., Gautier, B., Hameren, G. V., Berthelot, J., Gonzalez, S., & Chrast, R. (2022) · Biomedicines · doi:10.3390/biomedicines10061447 · Cited by 17
Chew, L., DeBoy, C. A., & Senatorov, V. V. (2014) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2014.08.017 · Cited by 13
Metadata
- 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 › Clinical Neurology › 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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
