Physiological and pathological functions of TMEM106B: a gene associated with brain aging and multiple brain disorders
Open accessAbstract
TMEM106B, encoding a lysosome membrane protein, has been recently associated with brain aging, hypomyelinating leukodystrophy and multiple neurodegenerative diseases, such as frontotemporal lobar degeneration (FTLD) and limbic-predominant age-related TDP-43 encephalopathy (LATE). During the past decade, considerable progress has been made towards our understanding of the cellular and physiological functions of TMEM106B. TMEM106B regulates many aspects of lysosomal function, including lysosomal pH, lysosome movement, and lysosome exocytosis. Both an increase and decrease in TMEM106B levels result in lysosomal abnormalities. In mouse models, TMEM106B deficiency leads to lysosome trafficking and myelination defects and FTLD related pathology. In humans, alterations in TMEM106B levels or function are intimately linked to neuronal proportions, brain aging, and brain disorders. Further elucidation of the physiological function of TMEM106B and changes in TMEM106B under pathological conditions will facilitate therapeutic development to treat brain disorders associated with TMEM106B.
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Both GRN and TMEM106B are reported to be involved in defective endosome/lysosome trafficking/function, a defect that is also observed in AD.
“Interestingly, both GRN and TMEM106B are reported to be involved in defective endosome/lysosome trafficking/function49,50, a defect that is also observed in AD.”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [50]
There were no significant changes in TMEM106B and MLKL in AD brains.
“we examined TMEM106B 101-103 and necroptosis effector MLKL 104,105 (Fig. 5c-d), two molecules previously implicated in neurodegeneration of AD, and detected no significant changes.”
From NAD+ hydrolase Sarm1 is a key driver of synapse degeneration and memory loss in Alzheimer’s disease (2025) · cites this paper as [103]
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TMEM106B: a strong FTLD disease modifier
Deming, Y. K., & Cruchaga, C. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1249-3 · Cited by 27 · see citing works
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Cancer-secreted miRNAs regulate amino-acid-induced mTORC1 signaling and fibroblast protein synthesis
Fong, M., Yan, W., Ghassemian, M., Wu, X., Zhou, X., Cao, M., Jiang, L., Wang, J., Liu, X., Zhang, J., et al. (2020) · EMBO Reports · doi:10.15252/embr.202051239 · Cited by 27 · see citing works
Guo, D.-Z., Xiao, L., Liu, Y.-J., Shen, C., Lou, H.-F., Lv, Y., & Pan, S.-Y. (2018) · Experimental & Molecular Medicine · doi:10.1038/emm.2017.291 · Cited by 25 · see citing works
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Self-citationThe Lysosomal Trafficking Transmembrane Protein 106B Is Linked to Cell Death
Suzuki, H., & Matsuoka, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.737171 · Cited by 19 · see citing works
Harding, S. R., Bocchetta, M., Gordón, E., Cash, D. M., Cardoso, M. J., Druyeh, R., Sebastien Ourselin, A., Warren, J. D., Mead, S., & Rohrer, J. D. (2017) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2017-315641 · Cited by 17 · see citing works
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Lysosomal dysfunction in TMEM106B hypomyelinating leukodystrophy
Itō, Y., Hartley, T., Baird, S., Venkateswaran, S., Simons, C., Wolf, N. I., Boycott, K. M., Dyment, D. A., & Kernohan, K. D. (2018) · Neurology Genetics · doi:10.1212/nxg.0000000000000288 · Cited by 15 · see citing works
A recurrent TMEM106B mutation in hypomyelinating leukodystrophy: A rapid diagnostic assay
Ikemoto, S., Hamano, S., Kikuchi, K., Koichihara, R., Hirata, Y., Matsuura, R., Hiraide, T., Nakashima, M., Inoue, K., Kurosawa, K., et al. (2020) · Brain and Development · doi:10.1016/j.braindev.2020.06.002 · Cited by 12 · see citing works
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New insights into the genetic etiology of Alzheimer’s disease and related dementias
Bellenguez, C., Küçükali, F., Jansen, I. E., Kleineidam, L., Moreno-Grau, S., Amin, N., Naj, A. C., Campos-Martin, R., Grenier-Boley, B., Andrade, V., et al. (2022) · Nature Genetics · doi:10.1038/s41588-022-01024-z · Cited by 2,498 · see citing works
Age-dependent formation of TMEM106B amyloid filaments in human brains
Schweighauser, M., Arseni, D., Bacioglu, M., Huang, M., Lövestam, S., Shi, Y., Yang, Y., Zhang, W., Kotecha, A., Garringer, H. J., et al. (2022) · Nature · doi:10.1038/s41586-022-04650-z · Cited by 194 · see citing works
TMEM106B is a receptor mediating ACE2-independent SARS-CoV-2 cell entry
Baggen, J., Jacquemyn, M., Persoons, L., Vanstreels, E., Pye, V. E., Wrobel, A. G., Calvaresi, V., Martin, S. R., Roustan, C., Cronin, N., et al. (2023) · Cell · doi:10.1016/j.cell.2023.06.005 · Cited by 153 · see citing works
Homotypic fibrillization of TMEM106B across diverse neurodegenerative diseases
Chang, A., Xiang, X., Wang, J., Lee, C., Arakhamia, T., Simjanoska, M., Wang, C., Carlomagno, Y., Zhang, G., Dhingra, S., et al. (2022) · Cell · doi:10.1016/j.cell.2022.02.026 · Cited by 150 · see citing works
Step by step: towards a better understanding of the genetic architecture of Alzheimer’s disease
Lambert, J.-C., Ramirez, A., Grenier-Boley, B., & Bellenguez, C. (2023) · Molecular Psychiatry · doi:10.1038/s41380-023-02076-1 · Cited by 87 · see citing works
Fan, Y., Zhao, Q., Xia, W., Tao, Y., Yu, W., Chen, M., Liu, Y., Zhao, J., Shen, Y., Sun, Y., et al. (2022) · Cell Research · doi:10.1038/s41422-022-00665-3 · Cited by 67 · see citing works
Accumulation of TMEM106B C-terminal fragments in neurodegenerative disease and aging
Perneel, J., Neumann, M., Heeman, B., Cheung, S., den Broeck, M. V., Wynants, S., Baker, M. C., Vicente, C. T., Faura, J., Rademakers, R., et al. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02531-3 · Cited by 65 · see citing works
Lee, J. Y., Harney, D., Teo, J. D., Kwok, J. B., Sutherland, G. T., Larance, M., & Don, A. S. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00650-3 · Cited by 45 · see citing works
T. Vicente, C., Perneel, J., Wynants, S., Heeman, B., Van den Broeck, M., Baker, M., Cheung, S., Faura, J., Mackenzie, I. R. A., & Rademakers, R. (2023) · Brain · doi:10.1093/brain/awad133 · Cited by 38 · see citing works
Comprehensive Overview of Alzheimer’s Disease: Etiological Insights and Degradation Strategies
Singh, M. K., Shin, Y., Ju, S., Han, S., Kim, S. S., & Kang, I. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25136901 · Cited by 41 · see citing works
Perneel, J., & Rademakers, R. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02486-5 · Cited by 35 · see citing works
The role of lysosomal membrane proteins in autophagy and related diseases
Xu, J., Gu, J., Pei, W., Zhang, Y., Wang, L., & Gao, J. (2023) · FEBS Journal · doi:10.1111/febs.16820 · Cited by 37 · see citing works
Valori, C. F., Sulmona, C., Brambilla, L., & Rossi, D. (2023) · Cells · doi:10.3390/cells12111450 · Cited by 30 · see citing works
TMEM106B deficiency impairs cerebellar myelination and synaptic integrity with Purkinje cell loss
Feng, T., Luan, L., Katz, I. I., Ullah, M., Deerlin, V. M. V., Trojanowski, J. Q., Lee, E. B., & Hu, F. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01334-7 · Cited by 29 · see citing works
Self-citationRunning, L. S., Cristobal, J. R., Karageorgiou, C., Camdzic, M., Aguilar, J. M. N., Gökçümen, Ö., Aga, D. S., & Atilla‐Gokcumen, G. E. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00652 · Cited by 25 · see citing works
Neumann, M., Perneel, J., Cheung, S., den Broeck, M. V., Nygaard, H. B., Hsiung, G. R., Wynants, S., Heeman, B., Rademakers, R., & Mackenzie, I. R. (2023) · Acta Neuropathologica · doi:10.1007/s00401-023-02580-2 · Cited by 24 · see citing works
TMEM106B regulates microglial proliferation and survival in response to demyelination
Zhang, T., Pang, W., Feng, T., Guo, J. D., Wu, K., Santos, M. N., Arthanarisami, A., Nana, A. L., Nguyen, Q., Kim, P. J., et al. (2023) · Science Advances · doi:10.1126/sciadv.add2676 · Cited by 22 · see citing works
Self-citationProgranulin deficiency in the brain: the interplay between neuronal and non-neuronal cells
Gawęda-Walerych, K., Aragona, V., Lodato, S., Sitek, E. J., Narożańska, E., & Buratti, E. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00475-8 · Cited by 22 · see citing works
Nies, S. H., Takahashi, H., Herber, C. S., Huttner, A. J., Chase, A., & Strittmatter, S. M. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.101159 · Cited by 23 · see citing works
Lu, J., Florio, D. N. D., Boya, P., Maday, S., Springer, W., & Chu, C. T. (2025) · Autophagy · doi:10.1080/15548627.2025.2581217 · Cited by 21 · see citing works
Loss of TMEM106B exacerbates Tau pathology and neurodegeneration in PS19 mice
Feng, T., Du, H., Yang, C., Wang, Y., & Hu, F. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02702-4 · Cited by 21 · see citing works
Self-citationThe role of the endolysosomal pathway in α-synuclein pathogenesis in Parkinson’s disease
Smith, J. K., Mellick, G. D., & Sykes, A. M. (2023) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.1081426 · Cited by 20 · see citing works
TMEM106B coding variant is protective and deletion detrimental in a mouse model of tauopathy
Edwards, G. A., Wood, C. A., He, Y., Nguyen, Q., Kim, P. J., Gomez‐Gutierrez, R., Park, K.-W., Xu, Y., Zurhellen, C., Al‐Ramahi, I., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02701-5 · Cited by 20 · see citing works
TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins
Levine, T. P. (2021) · bioRxiv · doi:10.1002/prot.26201 · Cited by 18 · see citing works
Case report: TMEM106B haplotype alters penetrance of GRN mutation in frontotemporal dementia family
Perneel, J., Manoochehri, M., Huey, E. D., Rademakers, R., & Goldman, J. S. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1160248 · Cited by 17 · see citing works
Salih, A. M., Galazzo, I. B., Raisi‐Estabragh, Z., Rauseo, E., Gkontra, P., Petersen, S. E., Lekadir, K., Altmann, A., Radeva, P. I., & Menegaz, G. (2021) · Scientific Reports · doi:10.1038/s41598-021-99153-8 · Cited by 16 · see citing works
Molecular Pathogenic Mechanisms of Hypomyelinating Leukodystrophies (HLDs)
Torii, T., & Yamauchi, J. (2023) · Neurology International · doi:10.3390/neurolint15030072 · Cited by 16 · see citing works
Li, S., Li, M., Li, G., Li, L., Yang, X., Zuo, Z., Zhang, L., Hu, X., & He, X. (2025) · Aging Cell · doi:10.1111/acel.14496 · Cited by 16 · see citing works
Know your enemy and know yourself – the case of SARS-CoV-2 host factors
Lee, W. S., Yousefi, M., Yan, B., Yong, C. L., & Ooi, Y. S. (2021) · Current Opinion in Virology · doi:10.1016/j.coviro.2021.08.007 · Cited by 16 · see citing works
Lysosomal TMEM106B interacts with galactosylceramidase to regulate myelin lipid metabolism
Takahashi, H., Pérez‐Cañamás, A., Lee, C. W., Ye, H., Han, X., & Strittmatter, S. M. (2024) · Communications Biology · doi:10.1038/s42003-024-06810-5 · Cited by 15 · see citing works
Localized proteomic differences in the choroid plexus of Alzheimer's disease and epilepsy patients
Leitner, D., Kanshin, E., Faustin, A., Thierry, M., Friedman, D. J., Devore, S., Ueberheide, B. M., Devinsky, O., & Wısnıewskı, T. (2023) · Frontiers in Neurology · doi:10.3389/fneur.2023.1221775 · Cited by 15 · see citing works
Perneel, J., Osua, M. L., Alidadiani, S., Peeters, N., Witte, L. D., Heeman, B., Manzella, S., Rycke, R. M. D., Brooks, M., Perkerson, R. B., et al. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00831-2 · Cited by 13 · see citing works
The unique neuropathological vulnerability of the human brain to aging
Ferrer, I. (2023) · Ageing Research Reviews · doi:10.1016/j.arr.2023.101916 · Cited by 14 · see citing works
Cognitive resilience to Alzheimer's disease characterized by cell‐type abundance
O’Neill, N. K., Stein, T. D., Olayinka, O. A., Empawi, J. A., Hu, J., Tong, T., Zhang, X., & Farrer, L. A. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14187 · Cited by 13 · see citing works
The role of endolysosomal progranulin and TMEM106B in neurodegenerative diseases
Takahashi, H., & Strittmatter, S. M. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00873-6 · Cited by 13 · see citing works
Gilchrist, L., Spargo, T. P., Green, R., Coleman, J. R. I., Howard, D. M., Thorp, J. G., Adey, B. N., Lord, J., Davies, H. L., Mundy, J., et al. (2025) · Nature Mental Health · doi:10.1038/s44220-024-00369-0 · Cited by 12 · see citing works
Signal peptide peptidase-like 2 proteases: Regulatory switches or proteasome of the membrane?
Mentrup, T., & Schröder, B. (2021) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2021.119163 · Cited by 12 · see citing works
Autophagy in severe acute respiratory syndrome coronavirus 2 infection
Chen, D., & Zhang, H. (2022) · Current Opinion in Physiology · doi:10.1016/j.cophys.2022.100596 · Cited by 12 · see citing works
A common Alu insertion in the 3'UTR of TMEM106B is associated with risk of dementia
Rodney, A. R., Karanjeet, K. B., Benzow, K. A., & Koob, M. D. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14090 · Cited by 12 · see citing works
AAV-GRN partially corrects motor deficits and ALS/FTLD-related pathology in Tmem106b−/−Grn−/− mice
Feng, T., Minevich, G., Liu, P., Qin, H. X., Wozniak, G. G., Pham, J., Pham, K., Korgaonkar, A. A., Kurnellas, M., Defranoux, N. A., et al. (2023) · iScience · doi:10.1016/j.isci.2023.107247 · Cited by 11 · see citing works
Self-citationViral Clearance and Neuroinflammation in Acute TMEV Infection Vary by Host Genetic Background
Lawley, K. S., Rech, R. R., Gómez, A. A. P., Hopkins, L., Han, G., Amstalden, K. A. Z., Welsh, C. J., Young, C. R., Jones‐Hall, Y., Threadgill, D. W., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231810482 · Cited by 11 · see citing works
Ruptured mesenteric varices in hepatic cirrhosis: a rare cause of intraperitoneal hemorrhage.
Jhung, J. W., & Micolonghi, T. S. (1985) · PubMed · Cited by 10 · see citing works
Forgham, H., Liu, L., Zhu, J., Javed, I., Cai, W., Qiao, R., & Davis, T. P. (2023) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2023.215172 · Cited by 9 · see citing works
Cleaved TMEM106B forms amyloid aggregates in central and peripheral nervous systems
Bacioglu, M., Schweighauser, M., Gray, D. A., Lövestam, S., Katsinelos, T., Quaegebeur, A., Swieten, J. C. V., Jaunmuktane, Z., Davies, S. W., Scheres, S. H. W., et al. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01813-z · Cited by 9 · see citing works
Physiological and pathological functions of TMEM106B in neurodegenerative diseases
Zhu, M., Zhang, G., Meng, L., Xiao, T., Fang, X., & Zhang, Z. (2024) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-024-05241-z · Cited by 8 · see citing works
Yang, C., Lee, G. B., Hao, L., & Hu, F. (2025) · Communications Biology · doi:10.1038/s42003-025-07752-2 · Cited by 7 · see citing works
Self-citationDisease-modifying effects of TMEM106B in genetic frontotemporal dementia: a longitudinal GENFI study
Mirza, S. S., Pasternak, M. M., Paterson, A. D., Rogaeva, E. A., Tartaglia, M. C., Mitchell, S. B., Black, S. E., Freedman, M., Tang‐Wai, D. F., Bouzigues, A., et al. (2025) · Brain · doi:10.1093/brain/awaf019 · Cited by 7 · see citing works
TMEM106B reduction does not rescue GRN deficiency in iPSC-derived human microglia and mouse models
Domínguez, S. L., Laufer, B. I., Ghosh, A. S., Li, Q., Ruggeri, G., Emani, M., Phu, L., Friedman, B. A., Sandoval, W. N., Rose, C. M., et al. (2023) · iScience · doi:10.1016/j.isci.2023.108362 · Cited by 7 · see citing works
Shafit‐Zagardo, B., Sidoli, S., Goldman, J. E., DuBois, J. C., Corboy, J. R., Strittmatter, S. M., Guzik, H. M., Edema, U., Arackal, A. G., Botbol, Y. M., et al. (2023) · Cells · doi:10.3390/cells12131734 · Cited by 9 · see citing works
Sawaguchi, S., Goto, M., Kato, Y., Tanaka, M., Tago, K., Oizumi, H., Ohbuchi, K., Mizoguchi, K., Miyamoto, Y., & Yamauchi, J. (2021) · Polymers · doi:10.3390/polym13071074 · Cited by 7 · see citing works
An AluYb8 retrotransposon characterises a risk haplotype of TMEM106B associated in neurodegenerationPreprint
Salazar, A., Tesi, N., Knoop, L., Pijnenburg, Y. A. L., van der Lee, S. J., Wijesekera, S., Křížová, J., Hiltunen, M. O., Daμμe, M., Petrucelli, L., et al. (2023) · medRxiv · doi:10.1101/2023.07.16.23292721 · Cited by 7 · see citing works
Molecular mechanisms of SARS-CoV-2 entry: implications for biomedical strategies
Santamaria-Castro, I., Leiva-Rebollo, R., Marín‐Wong, S., Jiménez-Guardeño, J. M., & Ortega‐Prieto, A. M. (2025) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00260-24 · Cited by 6 · see citing works
Flying under the radar: TMEM106B(120–254) fibrils break out in diverse neurodegenerative disorders
Copley, K. E., & Shorter, J. (2022) · Cell · doi:10.1016/j.cell.2022.03.032 · Cited by 6 · see citing works
Yuan, Y.-H., Wang, S., Lian, P.-P., Yu, Z.-H., Gao, X.-T., Duan, Y.-J., Mao, L., & Zhou, Y.-W. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.178297 · Cited by 4 · see citing works
Riordan, R., Saxton, A. D., Han, M., McMillan, P. J., Kow, R. L., Liachko, N. F., & Kraemer, B. C. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14468 · Cited by 5 · see citing works
Unveiling TMEM106B: SARS-CoV-2’s secret entrance to the cell
Lacrampe, A., & Hu, F. (2023) · Cell · doi:10.1016/j.cell.2023.07.005 · Cited by 5 · see citing works
Self-citationDivergent and convergent TMEM106B pathology in murine models of neurodegeneration and human disease
Du, M., Akerman, S. C., Fare, C. M., Ruan, L., Vidensky, S., Mamedova, L., Koo, K., Lee, J. Y., & Rothstein, J. D. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02087-9 · Cited by 4 · see citing works
Convergent Evolution and Host-Limiting Impacts of SARS-CoV-2 Revealed by Cellular Experiments
Zhang, T., Tian, R., Li, F., Tang, X., He, W., Hao, Z.-P., Zhuo, L., Lü, J., Lu, X., & Zheng, Y. (2025) · Molecular Biology and Evolution · doi:10.1093/molbev/msaf274 · Cited by 4 · see citing works
Sawaguchi, S., Ishida, M., Miyamoto, Y., & Yamauchi, J. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46080478 · Cited by 4 · see citing works
Houwer, J. F. H. D., Dopper, E. G. P., Rajicic, A., van Buuren, R., Arcaro, M., Galimberti, D., Breedveld, G. J., Wilke, M., van Minkelen, R., Jiskoot, L. C., et al. (2024) · Journal of Neurology · doi:10.1007/s00415-024-12758-7 · Cited by 4 · see citing works
A Novel Genetic TDP‐43 Pig Model Mimics Multiple Key ALS‐Like Features
Huang, C., Zheng, X., Wu, J., Li, J., Lin, Y., Chen, Y., Li, C., Song, X., Wang, W., Liu, Z., et al. (2025) · MedComm · doi:10.1002/mco2.70330 · Cited by 3 · see citing works
ACE2-independent entry factors for SARS-CoV-2 infection and immune activation
Sun, Y., Wong, L.-Y. R., & Chang, T. L.-Y. (2025) · mBio · doi:10.1128/mbio.01897-24 · Cited by 3 · see citing works
Nguyen, Q., Wood, C. A., Kim, P. J., & Jankowsky, J. L. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1275959 · Cited by 3 · see citing works
Myristoylation of TMEM106B by NMT1/2 regulates TMEM106B trafficking and turnover
Lacrampe, A., Hou, D., Perez, I. G., Gong, B., Franco-Hernandez, N., Yee, A., Chen, W., Young-Chapon, M. A., Lin, H., & Hu, F. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110322 · Cited by 3 · see citing works
Self-citationXing, S., Zheng, X., Yan, H., Mo, Y., Duan, R., Chen, Z., Wang, K., Gao, K., Chen, T., Zhao, S., et al. (2023) · Science China Life Sciences · doi:10.1007/s11427-022-2290-1 · Cited by 3 · see citing works
Liu, Y., Qin, K., Dou, K., Ren, J., Hou, B., & Xie, A. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167553 · Cited by 3 · see citing works
Anderson, M. C., Lopez, J., Wyr, M., & Ramirez, P. W. (2025) · Virology · doi:10.1016/j.virol.2025.110507 · Cited by 3 · see citing works
Rodney, A. R., Karanjeet, K. B., Benzow, K. A., & Koob, M. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.09.07.555370 · Cited by 3 · see citing works
Badman, J., Parracino, A., Kumar, R., & Tambaro, S. (2025) · Science Signaling · doi:10.1126/scisignal.adt2272 · Cited by 3 · see citing works
Compensatory roles of STT3A and ALG5 in glucose metabolism of aged macaque hippocampus
Zhu, G., He, R., Yang, Z.-Y., Wang, T., Yang, S.-C., Jiang, Y.-X., Li, J., Zhang, Y.-H., Zhao, F.-X., Deng, Y., et al. (2025) · Brain · doi:10.1093/brain/awaf282 · Cited by 2 · see citing works
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Tanaka, H., Hird, M. A., Tang‐Wai, D. F., & Kovács, G. G. (2022) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlac117 · Cited by 2 · see citing works
Alotaibi, L., & AlQassmi, A. (2023) · Global Medical Genetics · doi:10.1055/s-0043-1764370 · Cited by 3 · see citing works
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Novel approaches for the treatment of frontotemporal dementia: is there hope for the future?
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TMEM106B C-terminal fragments aggregate and drive neurodegenerative proteinopathyPreprint
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Future Prospects and Challenges
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Associations between TMEM106B C‐terminal fragment aggregation, age, and TDP ‐43 or tau pathology
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NAD+ hydrolase Sarm1 is a key driver of synapse degeneration and memory loss in Alzheimer’s disease
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Using exome analysis as a tool for genetics acquaintance in a psychiatry residence program
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Bacioglu, M., Schweighauser, M., Gray, D., Lövestam, S., Katsinelos, T., Quaegebeur, A., Swieten, J. C. V., Jaunmuktane, Z., Davies, S. W., Scheres, S. H. W., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26734860
Bacioglu, M., Schweighauser, M., Gray, D. A., Lövestam, S., Katsinelos, T., Quaegebeur, A., Swieten, J. C. V., Jaunmuktane, Z., Davies, S. W., Scheres, S. H. W., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26734854
Bacioglu, M., Schweighauser, M., Gray, D. A., Lövestam, S., Katsinelos, T., Quaegebeur, A., Swieten, J. C. V., Jaunmuktane, Z., Davies, S. W., Scheres, S. H. W., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26734857
Bacioglu, M., Schweighauser, M., Gray, D. A., Lövestam, S., Katsinelos, T., Quaegebeur, A., Swieten, J. C. V., Jaunmuktane, Z., Davies, S. W., Scheres, S. H. W., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26734851
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Bacioglu, M., Schweighauser, M., Gray, D. A., Lövestam, S., Katsinelos, T., Quaegebeur, A., Swieten, J. C. V., Jaunmuktane, Z., Davies, S. W., Scheres, S. H. W., et al. (2024) · Figshare · doi:10.6084/m9.figshare.26734845
- Authors
- Feng, T., Lacrampe, A., & Hu, F.
- Affiliations
- Cornell University (US)
- Corresponding author
- Hu, Fenghua
- Venue
- Acta Neuropathologica
- Published
- 2021-01-01
- Volume
- 141
- Issue
- 3
- Pages
- 327-339
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC8049516
- OpenAlex
- W3114567345
- Cited by
- 110
- References
- 94
- Citations by year
- 2026: 13 · 2025: 27 · 2024: 25 · 2023: 25 · 2022: 13 · 2021: 6
- FWCI
- 2.24
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Acta Neuropathologica (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (R01NS088448 & R01NS095954)
- the Bluefield project to cure frontotemporal dementia
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Health Sciences › Medicine › Physiology › Lysosomal Storage Disorders Research
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- TMEM106B, lysosomal function, lysosomal pH, lysosomal trafficking, lysosome exocytosis, hypomyelinating leukodystrophy, frontotemporal lobar degeneration, limbic-predominant age-related TDP-43 encephalopathy, brain aging, myelination defects, neurodegenerative diseases
- MeSH terms
- Aging, Animals, Brain, Brain Diseases, Humans, Membrane Proteins, Nerve Tissue Proteins
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