Physiological and pathological functions of TMEM106B: a gene associated with brain aging and multiple brain disorders

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576

TFEB Links Autophagy to Lysosomal Biogenesis

Settembre, C., Di Malta, C., Polito, V. A., Arencibia, M. G., Vetrini, F., Erdin, S., Erdin, S. U., Huynh, T., Medina, D., Colella, P., et al. (2011) · Science · doi:10.1126/science.1204592 · Cited by 3,365

Mutations in progranulin cause tau-negative frontotemporal dementia linked to chromosome 17

Baker, M., Mackenzie, I. R., Pickering-Brown, S. M., Gass, J., Rademakers, R., Lindholm, C., Snowden, J., Adamson, J., Sadovnick, A. D., Rollinson, S., et al. (2006) · Nature · doi:10.1038/nature05016 · Cited by 2,058

Converging Mechanisms in ALS and FTD: Disrupted RNA and Protein Homeostasis

Ling, S.-C., Polymenidou, M., & Cleveland, D. W. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.033 · Cited by 1,811 · cited 1×

State of play in amyotrophic lateral sclerosis genetics

Renton, A. E., Chiò, A., & Traynor, B. J. (2013) · Nature Neuroscience · doi:10.1038/nn.3584 · Cited by 1,626

Limbic-predominant age-related TDP-43 encephalopathy (LATE): consensus working group report

Nelson, P. T., Dickson, D. W., Trojanowski, J. Q., Jack, C. R., Boyle, P. A., Arfanakis, K., Rademakers, R., Alafuzoff, I., Attems, J., Brayne, C., et al. (2019) · Brain · doi:10.1093/brain/awz099 · Cited by 1,547

Autophagy pathway: Cellular and molecular mechanisms

Yu, L., Chen, Y., & Tooze, S. A. (2017) · Autophagy · doi:10.1080/15548627.2017.1378838 · Cited by 1,522

Null mutations in progranulin cause ubiquitin-positive frontotemporal dementia linked to chromosome 17q21

Cruts, M., Gijselinck, I., van der Zee, J., Engelborghs, S., Wils, H., Pirici, D., Rademakers, R., Vandenberghe, R., Dermaut, B., Martin, J.-J., et al. (2006) · Nature · doi:10.1038/nature05017 · Cited by 1,512

The prevalence of frontotemporal dementia

Ratnavalli, E., Brayne, C., Dawson, K. E., & Hodges, J. R. (2002) · Neurology · doi:10.1212/wnl.58.11.1615 · Cited by 1,182

Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities

Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134

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

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 191

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 159

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

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

Generic amyloid fibrillation of TMEM106B in patient with Parkinson’s disease dementia and normal elders

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

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

The major TMEM106B dementia risk allele affects TMEM106B protein levels, fibril formation, and myelin lipid homeostasis in the ageing human hippocampus

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 46

C-terminal TMEM106B fragments in human brain correlate with disease-associated TMEM106B haplotypes

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

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 43

Identification of TMEM106B amyloid fibrils provides an updated view of TMEM106B biology in health and disease

Perneel, J., & Rademakers, R. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02486-5 · Cited by 35

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 38

Astrocytes: Dissecting Their Diverse Roles in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Valori, C. F., Sulmona, C., Brambilla, L., & Rossi, D. (2023) · Cells · doi:10.3390/cells12111450 · Cited by 30

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 28

Investigating the Mechanism of Neurotoxic Effects of PFAS in Differentiated Neuronal Cells through Transcriptomics and Lipidomics Analysis

Running, 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 26

Limbic-predominant age-related TDP-43 proteinopathy (LATE-NC) is associated with abundant TMEM106B pathology

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

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 23

Progranulin 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

Spreading of Alzheimer tau seeds is enhanced by aging and template matching with limited impact of amyloid-β

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 25

Autophagy and mitophagy at the synapse and beyond: implications for learning, memory and neurological disorders

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 22

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 22

The 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 22

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

TMEM106B in humans and Vac7 and Tag1 in yeast are predicted to be lipid transfer proteins

Levine, T. P. (2021) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26201 · Cited by 17

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

Brain age estimation at tract group level and its association with daily life measures, cardiac risk factors and genetic variants

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 17

Molecular Pathogenic Mechanisms of Hypomyelinating Leukodystrophies (HLDs)

Torii, T., & Yamauchi, J. (2023) · Neurology International · doi:10.3390/neurolint15030072 · Cited by 16

Physical Exercise Decreases Complement‐Mediated Synaptic Loss and Protects Against Cognitive Impairment by Inhibiting Microglial Tmem9‐ ATP6V0D1 in Alzheimer's Disease

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 17

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

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 16

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 17

Increased TMEM106B levels lead to lysosomal dysfunction which affects synaptic signaling and neuronal health

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

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 15

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 15

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 14

Depression symptom-specific genetic associations in clinically diagnosed and proxy case Alzheimer’s disease

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 11

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 16

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

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

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 12

Viral 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

Ruptured mesenteric varices in hepatic cirrhosis: a rare cause of intraperitoneal hemorrhage.

Jhung, J. W., & Micolonghi, T. S. (1985) · PubMed · Cited by 10

Vector enabled CRISPR gene editing – A revolutionary strategy for targeting the diversity of brain pathologies

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

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

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 12

TMEM106B deficiency leads to alterations in lipid metabolism and obesity in the TDP-43Q331K knock-in mouse model

Yang, C., Lee, G. B., Hao, L., & Hu, F. (2025) · Communications Biology · doi:10.1038/s42003-025-07752-2 · Cited by 9

Disease-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 11

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

TMEM106B Puncta Is Increased in Multiple Sclerosis Plaques, and Reduced Protein in Mice Results in Delayed Lipid Clearance Following CNS Injury

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

Hypomyelinating Leukodystrophy 15 (HLD15)-Associated Mutation of EPRS1 Leads to Its Polymeric Aggregation in Rab7-Positive Vesicle Structures, Inhibiting Oligodendroglial Cell Morphological Differentiation

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

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

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 7

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

From plasma proteomics Mendelian randomization to neuropathological validation: The potential role of CTSH-GRN-TMEM106B and TREM2-IL-34 networks of microglia in Alzheimer's disease

Yuan, Y., Wang, S., Lian, P., Yu, Z., Gao, X., Duan, Y., Mao, L., & Zhou, Y. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.178297 · Cited by 6

TMEM106B C‐terminal fragments aggregate and drive neurodegenerative proteinopathy in transgenic Caenorhabditis elegans

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 9

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

Divergent 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

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 5

Hypomyelination Leukodystrophy 16 (HLD16)-Associated Mutation p.Asp252Asn of TMEM106B Blunts Cell Morphological Differentiation

Sawaguchi, S., Ishida, M., Miyamoto, Y., & Yamauchi, J. (2024) · Current Issues in Molecular Biology · doi:10.3390/cimb46080478 · Cited by 4

Two novel variants in GRN: the relevance of CNV analysis and genetic screening in FTLD patients with a negative family history

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

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

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

The TMEM106B T186S coding variant increases neurite arborization and synaptic density in primary hippocampal neurons

Nguyen, Q., Wood, C. A., Kim, P. J., & Jankowsky, J. L. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1275959 · Cited by 3

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 4

Superresolution live-cell imaging reveals that the localization of TMEM106B to filopodia in oligodendrocytes is compromised by the hypomyelination-related D252N mutation

Xing, 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 4

TMEM106B knockdown exhibits a neuroprotective effect in Parkinson's disease models via regulating autophagy-lysosome pathway

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

Defining diverse spike-receptor interactions involved in SARS-CoV-2 entry: Mechanisms and therapeutic opportunities

Anderson, M. C., Lopez, J., Wyr, M., & Ramirez, P. W. (2025) · Virology · doi:10.1016/j.virol.2025.110507 · Cited by 4

A common Alu element insertion in the 3’UTR of TMEM106B is associated with an increased risk of dementiaPreprint

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

Insights into the intramembrane protease SPPL2b and its substrates: Functions and disease implications

Badman, J., Parracino, A., Kumar, R., & Tambaro, S. (2025) · Science Signaling · doi:10.1126/scisignal.adt2272 · Cited by 3

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

Genetic correlation analysis identifies TMEM106B , ACE , and ERC2 as genetic loci shared between Alzheimer's disease and primary psychiatric disorders

Kumar, A., Ray, N. R., Kurup, J. T., del Rosario, P., Manoochehri, M., Stein, C. M., Vito, A. N. D., Cholerton, B., Sweet, R. A., Jager, P. L. D., et al. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71278 · Cited by 2

Significant contralaterality of temporal-predominant neuroastroglial tauopathy and FTLD-TDP type C presenting with the right temporal variant FTD

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

Identification of a de novo Mutation in TMEM106B in a Saudi Child Causes Hypomyelination Leukodystrophy

Alotaibi, L., & AlQassmi, A. (2023) · Global Medical Genetics · doi:10.1055/s-0043-1764370 · Cited by 3

Genetic architecture of epigenetic cortical clock age in brain tissue from older individuals: alterations in CD46 and other loci

Grodstein, F., Lemos, B., Yang, J., Lopes, K. D. P., Vialle, R. A., Seyfried, N. T., Wang, Y., Shireby, G. L., Hannon, E. J., Thomas, A. J., et al. (2024) · Epigenetics · doi:10.1080/15592294.2024.2392050 · Cited by 2

Novel approaches for the treatment of frontotemporal dementia: is there hope for the future?

Lozupone, M., Dibello, V., Sardone, R., Castellana, F., Zupo, R., Lampignano, L., Bortone, I., Sborgia, G., Daniele, A., Solfrizzi, V., et al. (2025) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2025.2546867 · Cited by 3

TMEM106B is increased in Multiple Sclerosis plaques, and deletion causes accumulation of lipid after demyelinationPreprint

Shafit‐Zagardo, B., Sidoli, S., Goldman, J. E., DuBois, J. C., Corboy, J. R., Strittmatter, S. M., Guzik, H. M., Graff, S., & Nagra, R. M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.05.05.490697 · Cited by 2

TMEM106B C-terminal fragments aggregate and drive neurodegenerative proteinopathyPreprint

Riordan, R., Saxton, A. D., McMillan, P. J., Kow, R. L., Liachko, N. F., & Kraemer, B. C. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.11.598478 · Cited by 2

Sex-specific genetic regulation of proteomics in cerebrospinal fluid uncovers genetic causes for sex differences in neurodegenerationPreprint

Song, S., Do, A. N., Wang, L., Heo, G., Kwon, J., Western, D., Yang, S. J., Timsina, J., Liu, M., Budde, J., et al. (2025) · medRxiv · doi:10.1101/2025.10.29.25339064 · Cited by 2

Future Prospects and Challenges

Gupta, G. (2025) · Springer eBooks · doi:10.1007/978-981-96-8873-9_12 · Cited by 2

Genetic variation in TMEM106B alters microglial activation and cytokine responses in chronic traumatic encephalopathy

Hartman, S., Aytan, N., Nicks, R., Hawkins, S., Cherry, J. D., Alvarez, V. E., Meng, G., Tripodis, Y., Martin, B. M., Palmisano, J. N., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02955-7 · Cited by 1

Associations between TMEM106B C‐terminal fragment aggregation, age, and TDP ‐43 or tau pathology

Acewicz, A., Tarka, S., Grzegorczyk, M., Rzepliński, R., Wierzba‐Bobrowicz, T., & Stępień, T. (2026) · Brain Pathology · doi:10.1111/bpa.70090 · Cited by 2

Transcriptomics effects of per- and polyfluorinated alkyl substances in differentiated neuronal cellsPreprint

Running, L. S., Cristobal, J. R., Karageorgiou, C., Camdzic, M., Aguilar, J. M. N., Gökçümen, Ö., Aga, D. S., & Atilla‐Gokcumen, G. E. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.01.26.577438 · Cited by 1

NAD+ hydrolase Sarm1 is a key driver of synapse degeneration and memory loss in Alzheimer’s disease

Fan, F., Joshi, P., Liu, X., Kotturu, S. K., Abiola, M., Liu, Q., & Lou, X. (2025) · doi:10.64898/2025.12.21.695860

Investigating the genetic relationship between depression symptoms and Alzheimer’s Disease in clinically diagnosed and proxy casesPreprint

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. (2023) · medRxiv · doi:10.1101/2023.06.05.23290588

Using exome analysis as a tool for genetics acquaintance in a psychiatry residence program

Vilar, A. F. C. B., Oliveira, D., Dourado, J. B., Zatz, M., & de Oliveira, J. R. M. (2024) · Brazilian Journal of Health Review · doi:10.34119/bjhrv7n2-017

Additional file 1 of The major TMEM106B dementia risk allele affects TMEM106B protein levels, fibril formation, and myelin lipid homeostasis in the ageing human hippocampus

Lee, J. Y., Harney, D., Teo, J. D., Kwok, J. B., Sutherland, G. T., Larance, M., & Don, A. S. (2023) · Figshare · doi:10.6084/m9.figshare.24165115

Additional file 2 of The major TMEM106B dementia risk allele affects TMEM106B protein levels, fibril formation, and myelin lipid homeostasis in the ageing human hippocampus

Lee, J. Y., Harney, D., Teo, J. D., Kwok, J. B., Sutherland, G. T., Larance, M., & Don, A. S. (2023) · Figshare · doi:10.6084/m9.figshare.24165118

Rare forms of hypomyelination and delayed myelination

Mura, E., Parazzini, C., & Tonduti, D. (2024) · Handbook of clinical neurology · doi:10.1016/b978-0-323-99209-1.00002-8

Genetic correlation analysis identifies TMEM106B, ACE , and ERC2 as genetic loci shared between Alzheimer’s disease and primary psychiatric disordersPreprint

Kumar, A., Ray, N. R., Kurup, J. T., del Rosario, P., Manoochehri, M., Stein, C. M., Vito, A. N. D., Cholerton, B., Sweet, R. A., Jager, P. L. D., et al. (2025) · medRxiv · doi:10.1101/2025.10.03.25336901

TFEB-depletion rescues TMEM106B-related myelin defects in zebrafishPreprint

Berdowski, W. M., van der Linde, H. C., Wolf, N. I., & van Ham, T. J. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.10.681547

Mendelian randomization study of the causal relationship between autoimmune diseases and anemia using proteomic and genetic data

Zhuang, X., & Pan, T. (2025) · Journal of Translational Autoimmunity · doi:10.1016/j.jtauto.2025.100333

A potential drug target in epilepsy and its role in other neurological disorders

Gao, S., Shen, Y., Shen, Y., Fang, X., Zhang, W., Wang, Y., Zhang, H.-P., Yang, S., & Liang, H. (2025) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-025-04696-6

Additional file 3 of 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) · Figshare · doi:10.6084/m9.figshare.26734848

Additional file 7 of Cleaved TMEM106B forms amyloid aggregates in central and peripheral nervous systems

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

Additional file 5 of 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) · Figshare · doi:10.6084/m9.figshare.26734854

Additional file 6 of 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) · Figshare · doi:10.6084/m9.figshare.26734857

Additional file 4 of 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) · Figshare · doi:10.6084/m9.figshare.26734851

Additional file 1 of 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) · Figshare · doi:10.6084/m9.figshare.19359709

Additional file 1 of 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) · Figshare · doi:10.6084/m9.figshare.26734842

Additional file 2 of 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) · Figshare · doi:10.6084/m9.figshare.26734845

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 28

Increased TMEM106B levels lead to lysosomal dysfunction which affects synaptic signaling and neuronal health

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

Novel Mechanistic Roles for TMEM106B in Regulating Lysosomal Inter-organelle Contact Sites and Misregulation in Frontotemporal Dementia (P6-13.005)

Ly, A. M., & Wong, Y. C. (2026) · Neurology · doi:10.1212/wnl.0000000000215661

Investigating the Effect of Increased TMEM106B in a Tauopathy Model

Amador, A. A., Aguirre‐Lamus, I., Timperman, D. L., Kim, P. J., Jankowsky, J. L., & Al‐Ramahi, I. (2025) · Alzheimer s & Dementia · doi:10.1002/alz70855_107573

Identification of TMEM106B amyloid fibrils provides an updated view of TMEM106B biology in health and disease

Perneel, J., & Rademakers, R. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02486-5 · Cited by 35