Network Organization of the Huntingtin Proteomic Interactome in Mammalian Brain

Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources

Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nature Protocols · doi:10.1038/nprot.2008.211 · Cited by 35,890

WGCNA: an R package for weighted correlation network analysis

Langfelder, P., & Horvath, S. (2008) · BMC Bioinformatics · doi:10.1186/1471-2105-9-559 · Cited by 27,252

Bioinformatics enrichment tools: paths toward the comprehensive functional analysis of large gene lists

Huang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn923 · Cited by 14,108

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes

MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366

A General Framework for Weighted Gene Co-Expression Network Analysis

Zhang, B., & Horvath, S. (2005) · Statistical Applications in Genetics and Molecular Biology · doi:10.2202/1544-6115.1128 · Cited by 5,684

Hierarchical Organization of Modularity in Metabolic Networks

Ravasz, E., Somera, A. L., Mongru, D. A., Oltvai, Z. N., & Barabási, A.-L. (2002) · Science · doi:10.1126/science.1073374 · Cited by 4,224

A Model for Random Sampling and Estimation of Relative Protein Abundance in Shotgun Proteomics

Liu, H., Sadygov, R. G., & Yates, J. R. (2004) · Analytical Chemistry · doi:10.1021/ac0498563 · Cited by 2,533

Adapting Proteostasis for Disease Intervention

Balch, W. E., Morimoto, R. I., Dillin, A., & Kelly, J. W. (2008) · Science · doi:10.1126/science.1141448 · Cited by 2,495

Defining clusters from a hierarchical cluster tree: the Dynamic Tree Cut package for R

Langfelder, P., Zhang, B., & Horvath, S. (2008) · Bioinformatics · doi:10.1093/bioinformatics/btm563 · Cited by 1,892

Transcriptomic Analysis of Autistic Brain Reveals Convergent Molecular Pathology

Voineagu, I., Wang, X., Johnston, P., Lowe, J. K., Tian, Y., Horvath, S., Mill, J., Cantor, R. M., Blencowe, B. J., & Geschwind, D. H. (2011) · Nature · doi:10.1038/nature10110 · Cited by 1,874

The Biology of Huntingtin

Saudou, F., & Humbert, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.02.003 · Cited by 945

Proteostasis impairment in protein-misfolding and -aggregation diseases

Hipp, M. S., Park, S.-H., & Hartl, F. U. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.05.003 · Cited by 683

Extrasynaptic NMDA Receptor Involvement in Central Nervous System Disorders

Parsons, M. P., & Raymond, L. A. (2014) · Neuron · doi:10.1016/j.neuron.2014.03.030 · Cited by 567

Vesicular Glycolysis Provides On-Board Energy for Fast Axonal Transport

Zala, D., Hinckelmann, M.-V., Yu, H., da Cunha, M. M. L., Liot, G., Cordelières, F. P., Marco, S., & Saudou, F. (2013) · Cell · doi:10.1016/j.cell.2012.12.029 · Cited by 494

Systems biology and gene networks in neurodevelopmental and neurodegenerative disorders

Parikshak, N. N., Gandal, M. J., & Geschwind, D. H. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3934 · Cited by 430

Integrated genomics and proteomics define huntingtin CAG length-dependent networks in mice

Langfelder, P., Cantle, J. P., Chatzopoulou, D., Wang, N., Gao, F., Al-Ramahi, I., Lu, X.-H., Ramos, E. M., El-Zein, K., Zhao, Y., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4256 · Cited by 385

Epigenetic mechanisms in neurogenesis

Yao, B., Christian, K. M., He, C., Jin, P., Ming, G., & Song, H. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.70 · Cited by 406

Huntington's disease: underlying molecular mechanisms and emerging concepts

Labbadia, J. P., & Morimoto, R. I. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.05.003 · Cited by 383

Signaling by cGAS–STING in Neurodegeneration, Neuroinflammation, and Aging

Paul, B. D., Snyder, S. H., & Bohr, V. A. (2020) · Trends in Neurosciences · doi:10.1016/j.tins.2020.10.008 · Cited by 336

Neuronal targets for reducing mutant huntingtin expression to ameliorate disease in a mouse model of Huntington's disease

Wang, N., Gray, M., Lu, X., Cantle, J. P., Holley, S. M., Greiner, E. R., Gu, X., Shirasaki, D., Cepeda, C., Li, Y., et al. (2014) · Nature Medicine · doi:10.1038/nm.3514 · Cited by 205

Mass spectrometry‐based protein–protein interaction networks for the study of human diseases

Richards, A., Eckhardt, M., & Krogan, N. J. (2021) · Molecular Systems Biology · doi:10.15252/msb.20188792 · Cited by 205

VCP recruitment to mitochondria causes mitophagy impairment and neurodegeneration in models of Huntington’s disease

Guo, X., Sun, X., Hu, D., Wang, Y.-J., Fujioka, H., Vyas, R., Chakrapani, S., Joshi, A. U., Luo, Y., Mochly-Rosen, D., et al. (2016) · Nature Communications · doi:10.1038/ncomms12646 · Cited by 200

Mutant HTT (huntingtin) impairs mitophagy in a cellular model of Huntington disease

Franco-Iborra, S., Plaza‐Zabala, A., Montpeyó, M., Sebastián, D., Vila, M., & Martínez‐Vicente, M. (2020) · Autophagy · doi:10.1080/15548627.2020.1728096 · Cited by 205

Protein-protein interaction networks: probing disease mechanisms using model systems

Kuzmanov, U., & Emili, A. (2013) · Genome Medicine · doi:10.1186/gm441 · Cited by 197

The cryo-electron microscopy structure of huntingtin

Guo, Q., Huang, B., Cheng, J., Seefelder, M., Engler, T., Pfeifer, G., Oeckl, P., Otto, M., Moser, F., Maurer, M., et al. (2018) · Nature · doi:10.1038/nature25502 · Cited by 197

Selective motor activation in organelle transport along axons

Cason, S. E., & Holzbaur, E. L. F. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00491-w · Cited by 185

Mechanism and therapeutic potential of targeting cGAS-STING signaling in neurological disorders

Huang, Y., Liu, B., Sinha, S. C., Amin, S., & Gan, L. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00672-x · Cited by 164

Integrated proteomics and network analysis identifies protein hubs and network alterations in Alzheimer’s disease

Zhang, Q., Ma, C., Gearing, M., Wang, P. G., Chin, L.-S., & Li, L. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0524-2 · Cited by 165

Alterations in synaptic function and plasticity in Huntington disease

Smith-Dijak, A., Sepers, M. D., & Raymond, L. A. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14723 · Cited by 158

Huntingtin Is Required for Normal Excitatory Synapse Development in Cortical and Striatal Circuits

McKinstry, S. U., Karadeniz, Y., Worthington, A. K., Hayrapetyan, V. Y., Ozlu, M. I., Serafin-Molina, K., Risher, W. C., Ustunkaya, T., Dragatsis, I., Zeitlin, S. O., et al. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.4699-13.2014 · Cited by 159

Huntington’s Disease and Mitochondria

Farshbaf, M. J., & Ghaedi, K. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9766-1 · Cited by 153

Ablation of huntingtin in adult neurons is nondeleterious but its depletion in young mice causes acute pancreatitis

Wang, G., Liu, X., Gaertig, M. A., Li, S., & Li, X.-J. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1524575113 · Cited by 146

Targeting ATM ameliorates mutant Huntingtin toxicity in cell and animal models of Huntington’s disease

Lu, X., Mattis, V. B., Wang, N., Al‐Ramahi, I., van den Berg, N., Fratantoni, S. A., Waldvogel, H. J., Greiner, E. R., Osmand, A., Merz, K. E., et al. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3010523 · Cited by 142

Systems Bioinformatics: increasing precision of computational diagnostics and therapeutics through network-based approaches

Oulas, A., Minadakis, G., Zachariou, M., Sokratous, K., Bourdakou, M. M., & Spyrou, G. M. (2017) · Briefings in Bioinformatics · doi:10.1093/bib/bbx151 · Cited by 143

Profilin reduces aggregation and phase separation of huntingtin N-terminal fragments by preferentially binding to soluble monomers and oligomers

Posey, A. E., Ruff, K. M., Harmon, T. S., Crick, S. L., Li, A., Diamond, M. I., & Pappu, R. V. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra117.000357 · Cited by 120

Huntington’s Disease: Complex Pathogenesis and Therapeutic Strategies

Tong, H., Yang, T., Xu, S., Li, X., Liu, L., Zhou, G., Yang, S., Yin, S., Li, X., & Li, S. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25073845 · Cited by 142

Spatiotemporal Proteomic Profiling of Huntington’s Disease Inclusions Reveals Widespread Loss of Protein Function

Hosp, F., Gutiérrez-Ángel, S., Schaefer, M. H., Cox, J., Meissner, F., Hipp, M. S., Hartl, F. U., Klein, R., Dudanova, I., & Mann, M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.097 · Cited by 119

Cortical and Striatal Circuits in Huntington’s Disease

Blumenstock, S., & Dudanova, I. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00082 · Cited by 128

Regulated cell death: discovery, features and implications for neurodegenerative diseases

Cui, J., Zhao, S., Li, Y., Zhang, D., Wang, B., Xie, J., & Wang, J. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00799-8 · Cited by 130

An Atlas of Protein-Protein Interactions Across Mouse Tissues

Skinnider, M. A., Scott, N. E., Prudova, A., Kerr, C. H., Stoynov, N., Stacey, R. G., Chan, Q. W. T., Rattray, D., Gsponer, J. A., & Foster, L. J. (2021) · Cell · doi:10.1016/j.cell.2021.06.003 · Cited by 108

Autophagy in neurodegenerative diseases: From pathogenic dysfunction to therapeutic modulation

Martínez‐Vicente, M. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.03.005 · Cited by 114

Restoring GABAergic inhibition rescues memory deficits in a Huntington’s disease mouse model

Dargaei, Z., Bang, J. Y., Mahadevan, V., Khademullah, C. S., Bedard, S., Parfitt, G. M., Kim, J. C., & Woodin, M. A. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1716871115 · Cited by 105

A Large Scale Huntingtin Protein Interaction Network Implicates Rho GTPase Signaling Pathways in Huntington Disease

Tourette, C., Li, B., Bell, R. N., O’Hare, S., Kaltenbach, L. S., Mooney, S. D., & Hughes, R. E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.523696 · Cited by 100

Real-time imaging of glutamate clearance reveals normal striatal uptake in Huntington disease mouse models

Parsons, M. P., Vanni, M. P., Woodard, C. L., Kang, R., Murphy, T. H., & Raymond, L. A. (2016) · Nature Communications · doi:10.1038/ncomms11251 · Cited by 103

The pathobiology of perturbed mutant huntingtin protein–protein interactions in Huntington's disease

Wanker, E. E., Ast, A., Schindler, F., Trepte, P., & Schnoegl, S. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14853 · Cited by 102

Identification of NUB1 as a suppressor of mutant Huntingtin toxicity via enhanced protein clearance

Lu, B., Al‐Ramahi, I., Valencia, A., Wang, Q., Berenshteyn, F., Yang, H., Gallego‐Flores, T., Ichcho, S., Lacoste, A., Hild, M., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3367 · Cited by 101

TRiC subunits enhance BDNF axonal transport and rescue striatal atrophy in Huntington’s disease

Zhao, X., Chen, X., Han, E. K., Hu, Y., Paik, P. K., Ding, Z., Overman, J., Lau, A., Shahmoradian, S. H., Chiu, W., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1603020113 · Cited by 101

Insights into GABA A ergic system alteration in Huntington's disease

Hsu, Y., Chang, Y., & Chern, Y. (2018) · Open Biology · doi:10.1098/rsob.180165 · Cited by 97

Proteome profiling in IL-1β and VEGF-activated human umbilical vein endothelial cells delineates the interlink between inflammation and angiogenesis

Mohr, T. T., Haudek‐Prinz, V. J., Slany, A., Grillari, J., Micksche, M., & Gerner, C. (2017) · PLoS ONE · doi:10.1371/journal.pone.0179065 · Cited by 93

Striatal synaptic dysfunction and altered calcium regulation in Huntington disease

Raymond, L. A. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.07.058 · Cited by 92

Protein interaction networks in neurodegenerative diseases: From physiological function to aggregation

Calabrese, G., Molzahn, C. M., & Mayor, T. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102062 · Cited by 92

Huntingtin and the Synapse

Barron, J. C., Hurley, E. P., & Parsons, M. P. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.689332 · Cited by 85

Cysteine string protein (CSP) and its role in preventing neurodegeneration

Burgoyne, R. D., & Morgan, A. (2015) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2015.03.008 · Cited by 80

Hippo Signaling Pathway Dysregulation in Human Huntington’s Disease Brain and Neuronal Stem Cells

Mueller, K. A., Glajch, K. E., Huizenga, M. N., Wilson, R. A., Granucci, E. J., Dios, A. M., Tousley, A. R., Iuliano, M., Weisman, E., LaQuaglia, M. J., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-29319-4 · Cited by 80

N17 Modifies Mutant Huntingtin Nuclear Pathogenesis and Severity of Disease in HD BAC Transgenic Mice

Gu, X., Cantle, J. P., Greiner, E. R., Lee, C. Y. D., Barth, A. M., Gao, F., Park, C. S., Zhang, Z., Sandoval-Miller, S., Zhang, R. L., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.01.008 · Cited by 77

Transcriptional regulatory networks underlying gene expression changes in Huntington's disease

Ament, S. A., Pearl, J. R., Bragg, R. M., Skene, P. J., Coffey, S. R., Bergey, D. E., Plaisier, C. L., Wheeler, V. C., MacDonald, M. E., Baliga, N. S., et al. (2018) · Molecular Systems Biology · doi:10.15252/msb.20167435 · Cited by 79

Exploring genetic modifiers of Gaucher disease: The next horizon

Davidson, B. A., Hassan, S., Garcia, E. J., Tayebi, N., & Sidransky, E. (2018) · Human Mutation · doi:10.1002/humu.23611 · Cited by 79

Pulsed Azidohomoalanine Labeling in Mammals (PALM) Detects Changes in Liver-Specific LKB1 Knockout Mice

McClatchy, D. B., Ma, Y., Liu, C., Stein, B. D., Martínez‐Bartolomé, S., Vasquez, D. S., Hellberg, K., Shaw, R. J., & Yates, J. R. (2015) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b00653 · Cited by 75

Mitochondrial Abnormalities and Synaptic Damage in Huntington’s Disease: a Focus on Defective Mitophagy and Mitochondria-Targeted Therapeutics

Sawant, N. A., Morton, H., Kshirsagar, S., Reddy, A. P., & Reddy, P. H. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02556-x · Cited by 74

Identification of Coq11, a New Coenzyme Q Biosynthetic Protein in the CoQ-Synthome in Saccharomyces cerevisiae

Allan, C. M., Awad, A. M., Johnson, J. S., Shirasaki, D., Wang, C., Blaby, C., Merchant, S., Loo, J. A., & Clarke, C. F. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.633131 · Cited by 71

SP8 and SP9 coordinately promote D2-type medium spiny neuron production by activating Six3 expression

Xu, Z., Liang, Q., Song, X., Zhang, Z., Lindtner, S., Li, Z., Wen, Y. F., Liu, G., Guo, T., Qi, D., et al. (2018) · Development · doi:10.1242/dev.165456 · Cited by 69

Huntingtin’s Function in Axonal Transport Is Conserved in Drosophila melanogaster

Zala, D., Hinckelmann, M.-V., & Saudou, F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060162 · Cited by 66

Expanding the Arsenal Against Huntington's Disease-Herbal Drugs and Their Nanoformulations

Vishwas, S., Gulati, M., Kapoor, B., Gupta, S., Singh, S. K., Awasthi, A., Khan, A., Goyal, A., Bansal, A. K., Baishnab, S., et al. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666201109090824 · Cited by 68

Inhibiting pathologically active ADAM10 rescues synaptic and cognitive decline in Huntington’s disease

Vezzoli, E., Caron, I., Talpo, F., Besusso, D., Conforti, P., Battaglia, E., Sogne, E., Falqui, A., Petricca, L., Verani, M., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci120616 · Cited by 65

The palmitoyl acyltransferase HIP14 shares a high proportion of interactors with huntingtin: implications for a role in the pathogenesis of Huntington's disease

Butland, S. L., Sanders, S. S., Schmidt, M. E., Riechers, S., Lin, D. T. S., Martin, D. D. O., Vaid, K., Graham, R. K., Singaraja, R. R., Wanker, E. E., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu137 · Cited by 65

Widespread remodeling of proteome solubility in response to different protein homeostasis stresses

Sui, X., Pires, D. E. V., Ormsby, A. R., Cox, D., Nie, S., Vecchi, G., Vendruscolo, M., Ascher, D. B., Reid, G. E., & Hatters, D. M. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1912897117 · Cited by 62

Multiple clinical features of Huntington’s disease correlate with mutant HTT gene CAG repeat lengths and neurodegeneration

Podvin, S., Reardon, H. T., Yin, K., Mosier, C., & HOOK, V. Y. H. (2018) · Journal of Neurology · doi:10.1007/s00415-018-8940-6 · Cited by 61

Intravitreal Administration of HA-1077, a ROCK Inhibitor, Improves Retinal Function in a Mouse Model of Huntington Disease

Li, M., Yasumura, D., Ma, A. A. K., Matthes, M. T., Yang, H., Nielson, G., Huang, Y., Szoka, F. C., LaVail, M. M., & Diamond, M. I. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056026 · Cited by 59

Exosomes and Homeostatic Synaptic Plasticity Are Linked to Each other and to Huntington's, Parkinson's, and Other Neurodegenerative Diseases by Database-Enabled Analyses of Comprehensively Curated Datasets

Wang, J. K. T., Langfelder, P., Horvath, S., & Palazzolo, M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00149 · Cited by 61

Bioenergetic deficits in Huntington’s disease iPSC-derived neural cells and rescue with glycolytic metabolites

Kedaigle, A. J., Fraenkel, E., Atwal, R. S., Wu, M., Gusella, J. F., MacDonald, M. E., Kaye, J., Finkbeiner, S. M., Mattis, V. B., Tom, C. M., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddy430 · Cited by 60

Impairment and Restoration of Homeostatic Plasticity in Cultured Cortical Neurons From a Mouse Model of Huntington Disease

Smith-Dijak, A., Nassrallah, W. B., Zhang, L. Y. J., Geva, M., Hayden, M. R., & Raymond, L. A. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00209 · Cited by 59

Huntingtin Regulates Mammary Stem Cell Division and Differentiation

Élias, S., Thion, M. S., Yu, H., Sousa, C. M., Lasgi, C., Morin, X., & Humbert, S. (2014) · Stem Cell Reports · doi:10.1016/j.stemcr.2014.02.011 · Cited by 68

Huntingtin structure is orchestrated by HAP40 and shows a polyglutamine expansion-specific interaction with exon 1

Harding, R., Deme, J. C., Hevler, J. F., Tamara, S., Lemak, A. S., Cantle, J. P., Szewczyk, M. M., Begeja, N., Goss, S., Zuo, X., et al. (2021) · Communications Biology · doi:10.1038/s42003-021-02895-4 · Cited by 56

Genetic manipulations of mutant huntingtin in mice: new insights into Huntington's disease pathogenesis

Lee, C. Y. D., Cantle, J. P., & Yang, X. W. (2013) · FEBS Journal · doi:10.1111/febs.12418 · Cited by 56

Is Huntingtin Dispensable in the Adult Brain?

Liu, J.-P., & Zeitlin, S. O. (2017) · Journal of Huntington s Disease · doi:10.3233/jhd-170235 · Cited by 58

Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted

Isas, J. M., PANDEY, N. K., Xu, H., Teranishi, K., Okada, A. K., Fultz, E. K., Rawat, A., Applebaum, A., Meier, F., Chen, J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24411-2 · Cited by 55

Mammalian nerve globins in search of functions

Ascenzi, P., Gustincich, S., & Marino, M. (2014) · IUBMB Life · doi:10.1002/iub.1267 · Cited by 53

A toxic mutant huntingtin species is resistant to selective autophagy

Fu, Y., Wu, P., Pan, Y., Sun, X., Yang, H., DiFiglia, M., & Lu, B. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2461 · Cited by 54

Huntingtin is required for ER-to-Golgi transport and for secretory vesicle fusion at the plasma membrane

Brandstaetter, H., Kruppa, A. J., & Buß, F. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.017368 · Cited by 52

Molecular insights into cortico-striatal miscommunications in Huntington's disease

Veldman, M. B., & Yang, X. W. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.10.019 · Cited by 49

The Expanding Therapeutic Potential of Neuronal KCC2

Tang, B. L. (2020) · Cells · doi:10.3390/cells9010240 · Cited by 52

Aberrant splicing in Huntington’s disease accompanies disrupted TDP-43 activity and altered m6A RNA modification

Nguyen, T. B., Miramontes, R., Chillón-Marinas, C., Maimon, R., Vazquez‐Sanchez, S., Lau, A., McClure, N. R., Wu, Z., Wang, K. Q., England, W., et al. (2025) · Nature Neuroscience · doi:10.1038/s41593-024-01850-w · Cited by 67

Personalized gene silencing therapeutics for Huntington disease

Kay, C., Skotte, N. H., Southwell, A. L., & Hayden, M. R. (2014) · Clinical Genetics · doi:10.1111/cge.12385 · Cited by 51

The Huntingtin-interacting protein SETD2/HYPB is an actin lysine methyltransferase

Seervai, R. N. H., Jangid, R. K., Karki, M., Tripathi, D. N., Jung, S. Y., Kearns, S. E., Verhey, K. J., Cianfrocco, M. A., Millis, B. A., Tyska, M. J., et al. (2020) · Science Advances · doi:10.1126/sciadv.abb7854 · Cited by 59

Phosphorylation of Mutant Huntingtin at Serine 116 Modulates Neuronal Toxicity

Watkin, E. E., Arbez, N., Waldron, E., O’Meally, R. N., Ratovitski, T., Cole, R. N., & Ross, C. A. (2014) · PLoS ONE · doi:10.1371/journal.pone.0088284 · Cited by 51

Subcellular Clearance and Accumulation of Huntington Disease Protein: A Mini-Review

Zhao, T., Hong, Y., Li, X., & Li, S.-H. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00027 · Cited by 49

Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification

Bondarev, S. A., Antonets, K. S., Kajava, A. V., Nizhnikov, A. A., & Zhouravleva, G. A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082292 · Cited by 49

Reactive Species in Huntington Disease: Are They Really the Radicals You Want to Catch?

Bono-Yagüe, J., Gómez-Escribano, A. P., Millán, J. M., & Vázquez‐Manrique, R. P. (2020) · Antioxidants · doi:10.3390/antiox9070577 · Cited by 52

Huntingtin Is Required for Epithelial Polarity through RAB11A-Mediated Apical Trafficking of PAR3-aPKC

Élias, S., McGuire, J. R., Yu, H., & Humbert, S. (2015) · PLoS Biology · doi:10.1371/journal.pbio.1002142 · Cited by 47

Karyopherin abnormalities in neurodegenerative proteinopathies

Pasha, T., Zatorska, A., Sharipov, D., Rogelj, B., Hortobágyi, T., & Hirth, F. (2021) · Brain · doi:10.1093/brain/awab201 · Cited by 51

High-Throughput Functional Analysis Distinguishes Pathogenic, Nonpathogenic, and Compensatory Transcriptional Changes in Neurodegeneration

Al‐Ramahi, I., Lu, B., Paola, S. D., Pang, K., de Haro, M., Peluso, I., Gallego‐Flores, T., Malik, N. T., Erikson, K., Bleiberg, B. A., et al. (2018) · Cell Systems · doi:10.1016/j.cels.2018.05.010 · Cited by 42

d-Polyglutamine Amyloid Recruits l-Polyglutamine Monomers and Kills Cells

Kar, K., Arduini, I., Drombosky, K. W., van der Wel, P. C. A., & Wetzel, R. B. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.11.019 · Cited by 45

Altered Regulation of Striatal Neuronal N-Methyl-D-Aspartate Receptor Trafficking by Palmitoylation in Huntington Disease Mouse Model

Kang, R., Wang, L., Sanders, S. S., Zuo, K., Hayden, M. R., & Raymond, L. A. (2019) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2019.00003 · Cited by 43

Striatal circuit development and its alterations in Huntington's disease

Lebouc, M., Richard, Q., Garret, M., & Baufreton, J. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105076 · Cited by 45

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D’Egidio, F., Castelli, V., Cimini, A., & d’Angelo, M. (2023) · Antioxidants · doi:10.3390/antiox12030571 · Cited by 42

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Greco, T. M., Secker, C., Ramos, E. S., Federspiel, J. D., Liu, J.-P., Perez, A. M., Al‐Ramahi, I., Cantle, J. P., Carroll, J. B., Botas, J., et al. (2022) · Cell Systems · doi:10.1016/j.cels.2022.01.005 · Cited by 42

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Xu, Z., Tito, A. J., Rui, Y., & Zhang, S. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.08.002 · Cited by 41

Bidirectional Control of Postsynaptic Density-95 (PSD-95) Clustering by Huntingtin

Parsons, M. P., Kang, R., Buren, C., Dau, A., Southwell, A. L., Doty, C. N., Sanders, S. S., Hayden, M. R., & Raymond, L. A. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.513945 · Cited by 41

Dysregulation of 14‐3‐3 proteins in neurodegenerative diseases with Lewy body or Alzheimer pathology

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Puigdellívol, M., Saavedra, A., & Pérez‐Navarro, E. (2016) · Brain Pathology · doi:10.1111/bpa.12432 · Cited by 38

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Heng, X., Guo, Q., Leung, A. W., & Li, J. Y. H. (2017) · eLife · doi:10.7554/elife.23253 · Cited by 40

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Mackay, J. P., Nassrallah, W. B., & Raymond, L. A. (2018) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12817 · Cited by 40

Design and characterization of mutant and wildtype huntingtin proteins produced from a toolkit of scalable eukaryotic expression systems

Harding, R., Loppnau, P., Ackloo, S. Z., Lemak, A. S., Hutchinson, A., Hunt, B., Holehouse, A. S., Ho, J. C., Fan, L., Toledo, L. M., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.007204 · Cited by 38

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Tshilenge, K., Aguirre, C. G., Bons, J., Gerencser, A. A., Basisty, N., Song, S., Rose, J., Lopez‐Ramirez, A., Naphade, S. B., Loureiro, A., et al. (2023) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2023.100534 · Cited by 42

Identification of protein complexes that bind to histone H3 combinatorial modifications using super-SILAC and weighted correlation network analysis

Kunowska, N., Rotival, M., Yu, L., Choudhary, J. S., & Dillon, N. (2015) · Nucleic Acids Research · doi:10.1093/nar/gku1350 · Cited by 38

SorCS2-mediated NR2A trafficking regulates motor deficits in Huntington’s disease

Ma, Q., Yang, J., Milner, T. A., Vonsattel, J., Palko, M. E., Tessarollo, L., & Hempstead, B. L. (2017) · JCI Insight · doi:10.1172/jci.insight.88995 · Cited by 34

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Mutations causing Lopes-Maciel-Rodan syndrome are huntingtin hypomorphs

Jung, R., Lee, Y., Barker, D., Correia, K., Shin, B., Loupe, J. M., Collins, R. L., Lucente, D. E., Ruliera, J., Gillis, T., et al. (2021) · Human Molecular Genetics · doi:10.1093/hmg/ddaa283 · Cited by 34

Huntingtin is required for ciliogenesis and neurogenesis during early Xenopus development

Haremaki, T., Deglincerti, A., & Brivanlou, A. H. (2015) · Developmental Biology · doi:10.1016/j.ydbio.2015.07.013 · Cited by 36

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The Role of the Huntingtin N17 Domain and its Modifications in Modulating Protein-Protein Interactions and Huntington's Disease Pathogenesis

Greiner, E. R. (2012) · eScholarship (California Digital Library)

Proteomic Analysis of Wild-type and Mutant Huntingtin-associated Proteins in Mouse Brains Identifies

Culver, B. P., Savas, J. N., Park, S. K., Choi, J. H., Zheng, S., Zeitlin, S. O., Yates, J. R., Tanese, N., & DepartmentofMicrobiology, F. ‡. (2012)

Identifizierung eines Protein-Interaktionsnetzwerks für Huntingtin und polyglutaminabhängige Induktion von Hefeprionen

Goehler, H. (2006) · Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver · doi:10.17169/refubium-4828 · Cited by 1

Mol Cell

Goehler, H., Lalowski, M., Stelzl, U., Waelter, S., Stroedicke, M., Worm, U., Dröge, A., Lindenberg, K., Knoblich, M., Haenig, C., et al. (2004) · MPG.PuRe (Max Planck Society)

A Protein Interaction Network Links GIT1, an Enhancer of Huntingtin Aggregation, to Huntington's Disease

Goehler, H., Lalowski, M., Stelzl, U., Waelter, S., Stroedicke, M., Worm, U., Droege, A., Lindenberg, K. S., Knoblich, M., Haenig, C., et al. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.016 · Cited by 453