TBC proteins: GAPs for mammalian small GTPase Rab?

Rab GTPases as coordinators of vesicle traffic

Stenmark, H. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2728 · Cited by 3,413

Rabs and their effectors: achieving specificity in membrane traffic

Grosshans, B. L., Ortiz, D., & Novick, P. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601617103 · Cited by 1,005

Insulin-stimulated Phosphorylation of a Rab GTPase-activating Protein Regulates GLUT4 Translocation

Sano, H., Kane, S., Sano, E., Mı̂inea, C. P., Asara, J. M., Lane, W. S., Garner, C. W., & Lienhard, G. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300063200 · Cited by 964

Regulation of exosome secretion by Rab35 and its GTPase-activating proteins TBC1D10A–C

Hsu, C., Morohashi, Y., Yoshimura, S., Manrique‐Hoyos, N., Jung, S., Lauterbach, M. A., Bakhti, M., Grønborg, M., Möbius, W., Rhee, J., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200911018 · Cited by 916

Evolution of the rab family of small GTP-binding proteins

Pereira‐Leal, J. B., & Seabra, M. C. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5072 · Cited by 795

A Method to Identify Serine Kinase Substrates

Kane, S., Sano, H., Liu, S. C. H., Asara, J. M., Lane, W. S., Garner, C. C., & Lienhard, G. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200198200 · Cited by 529

Rab GTPases, intracellular traffic and disease

Seabra, M. C., Mules, E. H., & Hume, A. N. (2002) · Trends in Molecular Medicine · doi:10.1016/s1471-4914(01)02227-4 · Cited by 473

AS160, the Akt substrate regulating GLUT4 translocation, has a functional Rab GTPase-activating protein domain

Mîinea, C. P., Sano, H., Kane, S., Sano, E., Fukuda, M., Peränen, J., Lane, W. S., & Lienhard, G. E. (2005) · Biochemical Journal · doi:10.1042/bj20050887 · Cited by 449

Rab GEFs and GAPs

Barr, F. A., & Lambright, D. G. (2010) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2010.04.007 · Cited by 433

Membrane traffic in the secretory pathway

Fukuda, M. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8351-4 · Cited by 403

Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Genome biology · doi:10.1186/s13059-022-02752-5 · Cited by 21

Cadmium exposure enhances organic cation transporter 2 trafficking to the kidney membrane and exacerbates cisplatin nephrotoxicity

Yang, H., Tang, J., Guo, D., Zhao, Q., Wen, J., Zhang, Y., Obianom, O. N., Zhou, S., Zhang, W., & Shu, Y. (2019) · Kidney International · doi:10.1016/j.kint.2019.11.012 · Cited by 21

PmTBC1D20, a Rab GTPase-activating protein from the black tiger shrimp, Penaeus monodon, is involved in white spot syndrome virus infection

Yingvilasprasert, W., Supungul, P., & Tassanakajon, A. (2013) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2013.09.008 · Cited by 20

Rab23 activities and human cancer—emerging connections and mechanisms

Chen, Y., Ng, F., & Tang, B. L. (2016) · Tumor Biology · doi:10.1007/s13277-016-5207-7 · Cited by 20

Mouse Models of Human Pathogenic Variants of TBC1D24 Associated with Non-Syndromic Deafness DFNB86 and DFNA65 and Syndromes Involving Deafness

Tona, R., López, I. A., Fenollar‐Ferrer, C., Faridi, R., Anselmi, C., Khan, A. A., Shahzad, M., Morell, R. J., Gu, S., Hoa, M., et al. (2020) · Genes · doi:10.3390/genes11101122 · Cited by 20

Cancer: Linking Powerhouses to Suicidal Bags

Martínez-Carreres, L., Nasrallah, A., & Fajas, L. (2017) · Frontiers in Oncology · doi:10.3389/fonc.2017.00204 · Cited by 21

Biallelic loss‐of‐function variants in TBC1D2B cause a neurodevelopmental disorder with seizures and gingival overgrowth

Harms, F. L., Parthasarathy, P., Zorndt, D., Alawi, M., Fuchs, S., Halliday, B. J., McKeown, C., Sampaio, H. A., Radhakrishnan, N., Radhakrishnan, S. K., et al. (2020) · Human Mutation · doi:10.1002/humu.24071 · Cited by 19

Regulation of Lipid Homeostasis by the TBC Protein dTBC1D22 Via Modulation of the Small GTPase Rab40

Duan, X., Xu, L., Li, Y., Jia, L., Liu, W., Shao, W., Bayat, V., Shang, W., Wang, L., Liu, J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109541 · Cited by 19

EPI64 Protein Functions as a Physiological GTPase-activating Protein for Rab27 Protein and Regulates Amylase Release in Rat Parotid Acinar Cells

Imai, A., Yoshie, S., Ishibashi, K., Haga‐Tsujimura, M., Nashida, T., Shimomura, H., & Fukuda, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.281394 · Cited by 19

TBC1D21 is an essential factor for sperm mitochondrial sheath assembly and male fertility

Chen, Y., Chen, X., Zhang, H., Sha, Y., Meng, R., Shao, T., Yang, X., Jin, P., Zhuang, Y., Min, W., et al. (2022) · Biology of Reproduction · doi:10.1093/biolre/ioac069 · Cited by 18

The RabGAP Gene Family in Tomato (Solanum lycopersicum) and Wild Relatives: Identification, Interaction Networks, and Transcriptional Analysis during Plant Development and in Response to Salt Stress

Madrid‐Espinoza, J., Salinas‐Cornejo, J., & Ruíz-Lara, S. (2019) · Genes · doi:10.3390/genes10090638 · Cited by 17

Structure-Function Analyses of the Small GTPase Rab35 and Its Effector Protein Centaurin-β2/ACAP2 during Neurite Outgrowth of PC12 Cells

Etoh, K., & Fukuda, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.611301 · Cited by 16

The GTPase-Activating Protein FgGyp1 Is Important for Vegetative Growth, Conidiation, and Virulence and Negatively Regulates DON Biosynthesis in Fusarium graminearum

Zheng, Q., Yu, Z., Yuan, Y., Sun, D., Abubakar, Y. S., Zhou, J., Wang, Z., & Zheng, H. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.621519 · Cited by 16

Rab GTPases in Osteoclastic Endomembrane Systems

Roy, M., & Roux, S. (2018) · BioMed Research International · doi:10.1155/2018/4541538 · Cited by 16

Systematic characterization of all Toxoplasma gondii TBC domain-containing proteins identifies an essential regulator of Rab2 in the secretory pathway

Quan, J. J., Nikolov, L. A., Sha, J., Wohlschlegel, J. A., Coppens, I., & Bradley, P. J. (2024) · PLoS Biology · doi:10.1371/journal.pbio.3002634 · Cited by 15

Dennd3 Functions as a Guanine Nucleotide Exchange Factor for Small GTPase Rab12 in Mouse Embryonic Fibroblasts

Matsui, T., Noguchi, K., & Fukuda, M. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.546689 · Cited by 15

Signal integration in the (m)TORC1 growth pathway

Ramlaul, K., & Aylett, C. H. S. (2018) · Frontiers in Biology · doi:10.1007/s11515-018-1501-7 · Cited by 12

Crystal structure of TBC1D15 GTPase‐activating protein (GAP) domain and its activity on Rab GTPases

Chen, Y., Gu, X., Zhou, X. E., Wang, W., Cheng, D., Ge, Y., Ye, F., Xu, H. E., & Lv, Z. (2017) · Protein Science · doi:10.1002/pro.3132 · Cited by 12

Rab17 regulates apical delivery of hepatic transcytotic vesicles

Striz, A., Stephan, A., López-Coral, A., & Tuma, P. L. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e18-07-0433 · Cited by 15

FgGyp8 as a putative FgRab1 GAP is required for growth and pathogenesis by regulating FgSnc1-mediated secretory vesicles fusion in Fusarium graminearum

ZHANG, X.-Z., Shuang, C. H. E. N., Abubakar, Y. S., Mao, X., Peng-fei, M. I. A. O., Zong-hua, W. A. N. G., Zhou, J., & Zheng, H. (2023) · Journal of Integrative Agriculture · doi:10.1016/j.jia.2023.04.005 · Cited by 11

SopD from Salmonella specifically inactivates Rab8

Savitskiy, S., & Itzen, A. (2021) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2021.140661 · Cited by 11

TBC1D24 emerges as an important contributor to progressive postlingual dominant hearing loss

Oziębło, D., Leja, M. L., Łaźniewski, M., Sarosiak, A., Tacikowska, G., Kochanek, K., Plewczyński, D., Skarżyńśki, H., & Ołdak, M. (2021) · Scientific Reports · doi:10.1038/s41598-021-89645-y · Cited by 11

TBC1D16 predicts chemosensitivity and prognosis in adult acute myeloid leukemia (AML) patients

Liu, H., Chen, P., Yang, Y., Zhu, K., Wang, T., Tang, L. Y., Liu, Y., Cao, S., Zhou, G., Zeng, H., et al. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173894 · Cited by 10

Crystal Structure of the Rab9A-RUTBC2 RBD Complex Reveals the Molecular Basis for the Binding Specificity of Rab9A with RUTBC2

Zhang, Z., Wang, S., Shen, T., Chen, J., & Ding, J. (2014) · Structure · doi:10.1016/j.str.2014.08.005 · Cited by 10

Silencing of TBC1D15 promotes RhoA activation and membrane blebbing

Takahara, Y., Maeda, M., Hasegawa, H., Ito, S., Hyodo, T., Asano, E., Takahashi, M., Hamaguchi, M., & Senga, T. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1921-2 · Cited by 10

All members of the EPI64 subfamily of TBC/RabGAPs also have GAP activities towards Ras

Nagai, H., Yasuda, S., Ohba, Y., Fukuda, M., & Nakamura, T. (2012) · The Journal of Biochemistry · doi:10.1093/jb/mvs147 · Cited by 10

Rab32/38 and the xenophagic restriction of intracellular bacteria replication

Tang, B. L. (2016) · Microbes and Infection · doi:10.1016/j.micinf.2016.05.006 · Cited by 10

The Rab3 family proteins in age-related neurodegeneration: unraveling molecular pathways and potential therapeutic targets

He, H., Ai, R., Fang, E. F., & Palikaras, K. (2025) · npj Aging · doi:10.1038/s41514-025-00257-6 · Cited by 10

Distinct pathways for export of silencing RNA in Caenorhabditis elegans systemic RNAi

Yoshida, K., Suehiro, Y., Dejima, K., Yoshina, S., & Mitani, S. (2023) · iScience · doi:10.1016/j.isci.2023.108067 · Cited by 9

TBC1D5 reverses the capability of HIF-2α in tumor progression and lipid metabolism in clear cell renal cell carcinoma by regulating the autophagy

Huang, Y., Xiong, Z., Wang, J., Gao, Y., Cao, Q., Wang, D., Shi, J., Chen, Z., & Yang, X. W. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05015-y · Cited by 9

Transcriptional Response of Bovine Monocyte-Derived Macrophages after the Infection with Different ArgentineanMycobacterium bovisIsolates

Caimi, K. C., Blanco, F. C., Soria, M. A., & Bigi, F. (2013) · BioMed Research International · doi:10.1155/2013/458278 · Cited by 9

Pontocerebellar hypoplasia type 11: Does the genetic defect determine timing of cerebellar pathology?

Laugwitz, L., Buchert, R., Groeschel, S., Rieß, A., Grimmel, M., Beck‐Wödl, S., Sturm, M., Gohla, G., Döbler‐Neumann, M., Krägeloh‐Mann, I., et al. (2020) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2020.103938 · Cited by 9

LMTK1, a Novel Modulator of Endosomal Trafficking in Neurons

Hisanaga, S., Wei, R., Huo, A., & Tomomura, M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00112 · Cited by 9

Neurogenetic disorders associated with mutations in the FERRY complex: a novel disease class?

Riffe, R. M., & Downes, G. B. (2025) · Biology Open · doi:10.1242/bio.061808 · Cited by 8

A Cross-Tissue Transcriptome-Wide Association Study Identifies Novel Susceptibility Genes for Juvenile Idiopathic Arthritis in Asia and Europe

Xu, J., Ma, J., Zeng, Y., Si, H., Wu, Y., Zhang, S., & Shen, B. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.941398 · Cited by 8

Expression of TBC1D16 Is Associated with Favorable Prognosis of Epithelial Ovarian Cancer

Yang, Z., Shen, H., He, W., Ouyang, L., Guo, Y., Fang, Q., Xu, B., Xie, D., & Yang, G. (2018) · The Tohoku Journal of Experimental Medicine · doi:10.1620/tjem.245.141 · Cited by 8

The multiple facets of Rab proteins modulating the cellular distribution of cholesterol from the late endosomal compartment

Nguyen, M. K. L., Pinkenburg, C., Du, J. J., Bernaus‐Esqué, M., Enrich, C., Rentero, C., & Grewal, T. (2025) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2025.119896 · Cited by 7

Isoform-dependent subcellular localization of LMTK1A and LMTK1B and their roles in axon outgrowth and spine formation

Wei, R., Sugiyama, A., Sato, Y., Nozumi, M., Nishino, H., Takahashi, M., Saito, T., Ando, K., Fukuda, M., Tomomura, M., et al. (2020) · The Journal of Biochemistry · doi:10.1093/jb/mvaa019 · Cited by 7

Light-emitting diode photomodulation of uterine adenocarcinoma cells inhibited angiogenesis capacity via the regulation of exosome biogenesis

Mojtahedin, S., Nasimi, F. S., Tajalli, H., Ebrahimi, S., Alimohammadzadeh, B., Rahbarghazi‬, R., & Mahdipour, M. (2022) · Lasers in Medical Science · doi:10.1007/s10103-022-03597-x · Cited by 7

A New Member of the TBC1D15 Family from Chiloscyllium plagiosum: Rab GTPase-Activating Protein Based on Rab7 as a Substrate

Li, Y., Wang, W., Cheng, D., Wang, T., Lu, C., Chen, J., Nie, Z., Zhang, W., Lv, Z., Wu-tong, W., et al. (2015) · Marine Drugs · doi:10.3390/md13052955 · Cited by 7

Corrigendum: The GTPase-Activating Protein FgGyp1 Is Important for Vegetative Growth, Conidiation, and Virulence and Negatively Regulates DON Biosynthesis in Fusarium graminearum

Zheng, Q., Yu, Z., Yuan, Y., Sun, D., Abubakar, Y. S., Zhou, J., Wang, Z., & Zheng, H. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.666050 · Cited by 6

Genomic Amplification of TBC1D31 Promotes Hepatocellular Carcinoma Through Reducing the Rab22A‐Mediated Endolysosomal Trafficking and Degradation of EGFR

Cao, P., Chen, H., Zhang, Y., Zhang, Q., Shi, M., Han, H., Wang, X., Jin, L., Guo, B., Hao, R., et al. (2024) · Advanced Science · doi:10.1002/advs.202405459 · Cited by 5

Increased expression of TBC1D10B as a potential prognostic and immunotherapy relevant biomarker in liver hepatocellular carcinoma

Fan, L., Tang, Y., Li, J., & Huang, W. (2023) · Scientific Reports · doi:10.1038/s41598-022-20341-1 · Cited by 5

Loss of TBC1D2B causes a progressive neurological disorder with gingival overgrowth

Harms, F. L., Rexach, J. E., Efthymiou, S., Aynekin, B., Per, H., Güleç, A., Nampoothiri, S., Sampaio, H. A., Sachdev, R., Stoeva, R., et al. (2024) · European Journal of Human Genetics · doi:10.1038/s41431-024-01563-5 · Cited by 5

Lipid Modification of Ras Superfamily GTPases

Chenette, E., & Der, C. (2011) · The Enzymes · doi:10.1016/b978-0-12-381339-8.00005-6 · Cited by 5

Interaction between the TBC1D24 TLDc domain and the KIBRA C2 domain is disrupted by two epilepsy-associated TBC1D24 missense variants

Tona, R., Inagaki, S., Ishibashi, Y., Faridi, R., Yousaf, R., Roux, I., Wilson, E. A. H., Fenollar‐Ferrer, C., Chien, W. W., Belyantseva, I. A., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107725 · Cited by 4

Roles of Rab-GAPs in Regulating Autophagy

Itoh, T., & Fukuda, M. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-805420-8.00006-8 · Cited by 4

TBC1D10B promotes tumor progression in colon cancer via PAK4‑mediated promotion of the PI3K/AKT/mTOR pathway

Chi, X.-J., Song, Y.-B., Zhang, H., Wei, L.-Q., Gao, Y., Miao, X.-J., Yang, S.-T., Lin, C., Dong, L., & Zhang, X. (2024) · APOPTOSIS · doi:10.1007/s10495-024-01972-3 · Cited by 4

Novel TBC1D8B Variant in a 6-Month-Old Boy With Steroid-Sensitive Nephrotic Syndrome: A Case Report

Hou, L., Yin, L., Wu, Y., Zhao, C., & Du, Y. (2021) · Frontiers in Pediatrics · doi:10.3389/fped.2021.732512 · Cited by 4

Decoding TBCK: from bioinformatic insights of domain architecture to disease implications

Cagwin, E. M., Padgett, C. M., Lin, Y. G., & Zhu, W. (2025) · Frontiers in Biophysics · doi:10.3389/frbis.2025.1560824 · Cited by 3

TBC1D8B, a GTPase-activating protein, is a novel apoptosis inducer

OKADA, J., Matsumoto, S., Yamada, E., Saito, T., Okada, K., Watanabe, T., Nakajima, Y., Ozawa, A., Yamada, M., Ohshima, K., et al. (2021) · Biomedical Research · doi:10.2220/biomedres.42.95 · Cited by 3

Methods for Establishing Rab Knockout MDCK Cells

Kinoshita, R., Homma, Y., & Fukuda, M. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1346-7_17 · Cited by 3

Targeting the Dbl and Dock-Family RhoGEFs

Blangy, A., & Fort, P. (2013) · The Enzymes · doi:10.1016/b978-0-12-416749-0.00008-7 · Cited by 4

The Rab GTPase activating protein Gyp2 contributes to UV stress tolerance in Metarhizium acridum

Xie, M., Xia, Y., & Cao, Y. (2018) · World Journal of Microbiology and Biotechnology · doi:10.1007/s11274-018-2457-0 · Cited by 3

Identifying novel spatiotemporal regulators of innate immunity

Victorino, F., & Alper, S. (2012) · Immunologic Research · doi:10.1007/s12026-012-8344-0 · Cited by 2

The small GTPase, Rab27, and its effectors and regulators participate in granule exocytosis by parotid acinar cells

Imai, A., & Haga‐Tsujimura, M. (2016) · Journal of Oral Biosciences · doi:10.1016/j.job.2016.10.003 · Cited by 2

Transferrin-induced signaling through transferrin receptor and AKT kinase mediates formation of Rab8- and MICAL-L1-positive tubules involved in receptor recyclingPreprint

Rangaraj, N., Vaibhava, V., Sudhakar, C., Moharir, S. C., & Swarup, G. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.02.06.527405 · Cited by 2

The Immunosuppressive Functions of Eosinophils Are Compromised in Patients With Allergic Rhinitis, Particularly Concerning Rab27a Expression

Liao, Y., Li, M., Song, S., Xu, X., Xiao, X., Liu, Y., Yang, G., & Yang, P. (2024) · Immunity Inflammation and Disease · doi:10.1002/iid3.70091 · Cited by 1

Identification of Rab GTPase ‐Activating Proteins Required for Tubular Endosome Formation

Nakashima, S., & Fukuda, M. (2025) · Traffic · doi:10.1111/tra.70007 · Cited by 1

A Novel Homozygous TBC1D2B Variant Disrupts Functional Domains and Suggests Impaired Rab‐GTPase Regulation in Neurodevelopmental Disorder

Ozturk, M., Arslan, C. B., Akbulut, E., Habiloğlu, E., Yaylı, E., & Uyguner, Z. O. (2025) · Developmental Neurobiology · doi:10.1002/dneu.22998 · Cited by 1

Arl8b inactivates the Rab11a recycling pathway to promote LAMP1 sorting and lysosome biogenesis

Chouhan, P., Phogat, Y., Walia, K., Debnath, S., Choubey, S., Gupta, M., Tuli, A., & Sharma, M. (2026) · The Journal of Cell Biology · doi:10.1083/jcb.202509040 · Cited by 1

TBC1D9 and TBC1D9B are ARL8 effectors that modulate exosome secretion through a RAB11A–exocyst pathway

Shelke, G. V., Williamson, C. D., Keren‐Kaplan, T., & Bonifacino, J. S. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2527864123 · Cited by 1

TBC1D24 regulates mitochondria and endoplasmic reticulum-mitochondria contact sitesPreprint

Benhammouda, S., Rousseau, J., Campeau, P. M., & Germain, M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.19.613961 · Cited by 1

Analysis of the RAB family of GTPases in C. elegans and their role in regulating neuronal membrane trafficking

Sasidharan, N. (2011) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-3162 · Cited by 1

The Retromer Complex

Seaman, M. N. J. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-394447-4.20048-5 · Cited by 1

Erythropoietin Stimulation of Mitochondrial Protein Content - A Potential Mechanism through Direct Binding of Erythropoietin Receptor and AMP-Activated Protein Kinase

Pham, M. N. (2014) · UA Campus Repository (The University of Arizona)

Primary characterization of a putative novel TBC1 domain family member 13 from Haemaphysalis qinghaiensis

Tian, Z., Du, J., Gao, S., Yang, J., Luo, J., Xing, S., Du, X., Liu, G., Luo, J., & Yin, H. (2016) · Veterinary Parasitology · doi:10.1016/j.vetpar.2016.04.004

Dense-core vesicle maturation at the Golgi-endosomal interface in Caenorhabditis elegans

Hannemann, M. (2012) · doi:10.53846/goediss-3209

Functional Analysis of MicroRNAs as Regulators of Membrane Trafficking

Serva, A. (2012) · heiDOK (Heidelberg University) · doi:10.11588/heidok.00013119

Statins and Protein Prenylation in the Retina

Ling, J. Y. M. (2017) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r39s1m03v

Regulation of intracellular traffic by TBK1 and its relevance to ALS

Villarroel‐Campos, D. (2020) · UCL Discovery (University College London)

No evidence for change in expression of TBC1D1 and TBC1D4 genes in cultured human adipocytes stimulated by myokines and adipokines

Kępczyński, Ł., Wcisło, S., Korzeniewska-Dyl, I., Połatyńska, K., Gach, A., & Moczulski, D. K. (2021) · Adipocyte · doi:10.1080/21623945.2021.1900497

Abnormal molecular signatures of inflammation, energy metabolism and vesicle biology in human Huntington disease peripheral tissuesPreprint

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.02.03.475821

Faculty Opinions recommendation of Rab family of small GTPases: an updated view on their regulation and functions.

Westlake, C. J. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.738155646.793582059

Implicações de variantes bialélicas de perda de função no gene TBCK, no transporte de vesículas de células progenitoras neurais derivadas de células-tronco pluripotentes induzidas

Suzuki, Â. M. (2021) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.41.2021.tde-09122021-143412

The Retromer Complex

Seaman, M. N. J. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-821618-7.00054-7

Faculty Opinions recommendation of Specific TBC Domain-Containing Proteins Control the ER-Golgi-Plasma Membrane Trafficking of GPCRs.

Wedegaertner, P., & Randolph, C. E. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.736177314.793564858

Rab27

Oguchi, M. E., & Fukuda, M. (2017) · Springer eBooks · doi:10.1007/978-3-319-67199-4_101791

Rab27

Oguchi, M. E., & Fukuda, M. (2016) · Springer eBooks · doi:10.1007/978-1-4614-6438-9_101791-1

Adaptations of autophagy and lysosomal systems upon membrane damage and pathogenic invasion

Bhattacharya, A. (2023) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.73735

Additional file 18 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062301

Additional file 1 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062307

Additional file 2 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062322

Additional file 3 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062325

Additional file 10 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062277

Additional file 13 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062286

Additional file 20 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062310

Additional file 14 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062289

Additional file 19 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062304

Additional file 16 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062295

Additional file 11 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062280

Additional file 8 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062340

Additional file 7 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062337

Additional file 6 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062334

Additional file 12 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062283

Additional file 15 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062292

Additional file 9 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062343

Additional file 21 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062313

Additional file 5 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062331

Additional file 17 of Abnormal molecular signatures of inflammation, energy metabolism, and vesicle biology in human Huntington disease peripheral tissues

Neueder, A., Kojer, K., Hering, T., Lavery, D. J., Chen, J., Birth, N., Hallitsch, J., Trautmann, S., Parker, J., Flower, M. D., et al. (2022) · Figshare · doi:10.6084/m9.figshare.21062298

The critical roles of TBC proteins in human diseases.

Shi, M., Zhang, Y., & Zhou, G. (2018) · PubMed · doi:10.16288/j.yczz.17-343 · Cited by 10

TBC Proteins: Miraculous Regulators of Rabs GTPase Molecular Switches

Yan, J., Zheng, Y., Han, S. H., Yin, J., Li, Y., Chen, T.-X., Peng, B., & Liu, W. (2021) · Biomedical and health research · doi:10.3233/bhr210034 · Cited by 1

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