Network Organization of the Huntingtin Proteomic Interactome in Mammalian Brain
Open accessAbstract
We used affinity-purification mass spectrometry to identify 747 candidate proteins that are complexed with Huntingtin (Htt) in distinct brain regions and ages in Huntington's disease (HD) and wild-type mouse brains. To gain a systems-level view of the Htt interactome, we applied Weighted Correlation Network Analysis to the entire proteomic data set to unveil a verifiable rank of Htt-correlated proteins and a network of Htt-interacting protein modules, with each module highlighting distinct aspects of Htt biology. Importantly, the Htt-containing module is highly enriched with proteins involved in 14-3-3 signaling, microtubule-based transport, and proteostasis. Top-ranked proteins in this module were validated as Htt interactors and genetic modifiers in an HD Drosophila model. Our study provides a compendium of spatiotemporal Htt-interacting proteins in the mammalian brain and presents an approach for analyzing proteomic interactome data sets to build in vivo protein networks in complex tissues, such as the brain.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In vivo PPI screening by large-scale co-immunoprecipitation and mass spectrometry provided tissue- and time-specific information not found by Y2H studies.
“Interestingly, in vivo PPI screening by large-scale co-immunoprecipitation and mass spectrometry provided tissue- and time-specific information that was not found by Y2H studies167.”
From Systems biology and gene networks in neurodevelopmental and neurodegenerative disorders (2015) · cites this paper as [167]
WGCNA identified spatially and temporally specific modules associated with mutant Htt, and hub proteins with high intra-modular connectivity modulated neurodegeneration in flies.
“WGCNA identified spatially and temporally specific modules associated with mutant Htt (which encodes huntingtin); and proteins with high intra-modular connectivity (hub proteins) modulated neurodegeneration in flies.”
From Systems biology and gene networks in neurodevelopmental and neurodegenerative disorders (2015) · cites this paper as [167]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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 · see citing works
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 · see citing works
Self-citationHuang, D. W., Sherman, B. T., & Lempicki, R. A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn923 · Cited by 14,108 · see citing works
MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366 · see citing works
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 · see citing works
Self-citationHierarchical 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 · see citing works
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 · see citing works
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 2,486 · see citing works
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 · see citing works
Self-citationTranscriptomic 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 · see citing works
Self-citationInteractome Networks and Human Disease
Vidal, M., Cusick, M. E., & Barabási, A.-L. (2011) · Cell · doi:10.1016/j.cell.2011.02.016 · Cited by 1,771 · see citing works
Trinucleotide Repeat Disorders
Orr, H. T., & Zoghbi, H. Y. (2007) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.29.051605.113042 · Cited by 1,365 · see citing works
Vonsattel, J. P., & DiFiglia, M. (1998) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199805000-00001 · Cited by 1,305 · see citing works
Proteomic analysis of NMDA receptor–adhesion protein signaling complexes
Husi, H., Ward, M. A., Choudhary, J. S., Blackstock, W. P., & Grant, S. G. N. (2000) · Nature Neuroscience · doi:10.1038/76615 · Cited by 1,194 · see citing works
Gauthier, L. R., Charrin, B. C., Borrell-Pagès, M., Dompierre, J. P., Rangone, H., Cordelières, F. P., De Mey, J., MacDonald, M. E., Leßmann, V., Humbert, S., et al. (2004) · Cell · doi:10.1016/j.cell.2004.06.018 · Cited by 1,178 · see citing works
Geometric Interpretation of Gene Coexpression Network Analysis
Horvath, S., & Dong, J. (2008) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000117 · Cited by 849 · see citing works
Self-citationLim, J., Hao, T., Shaw, C., Patel, A. J., Szabó, G., Rual, J.-F., Fisk, C. J., Li, N., Smolyar, A., Hill, D. E., et al. (2006) · Cell · doi:10.1016/j.cell.2006.03.032 · Cited by 789 · see citing works
Functional organization of the transcriptome in human brain
Oldham, M. C., Konopka, G., Iwamoto, K., Langfelder, P., Kato, T., Horvath, S., & Geschwind, D. H. (2008) · Nature Neuroscience · doi:10.1038/nn.2207 · Cited by 752 · see citing works
Self-citationKrüger, M., Moser, M., Ussar, S., Thievessen, I., Luber, C. A., Forner, F., Schmidt, S., Zanivan, S., Fässler, R., & Mann, M. (2008) · Cell · doi:10.1016/j.cell.2008.05.033 · Cited by 680 · see citing works
Gene network interconnectedness and the generalized topological overlap measure
Yip, A. M., & Horvath, S. (2007) · BMC Bioinformatics · doi:10.1186/1471-2105-8-22 · Cited by 633 · see citing works
Self-citationGray, M., Shirasaki, D., Cepeda, C., André, V., Wilburn, B., Lu, X.-H., Tao, J., Yamazaki, I., Li, S.-H., Sun, Y. E., et al. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0857-08.2008 · Cited by 616 · see citing works
Self-citationMorrison, D. K. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.10.003 · Cited by 604 · see citing works
Zeron, M. M., Hansson, O., Chen, N., Wellington, C. L., Leavitt, B. R., Brundin, P., Hayden, M. R., & Raymond, L. A. (2002) · Neuron · doi:10.1016/s0896-6273(02)00615-3 · Cited by 600 · see citing works
Humbert, S., Bryson, E. A., Cordelières, F. P., Connors, N. C., Datta, S. R., Finkbeiner, S. M., Greenberg, M. E., & Saudou, F. (2002) · Developmental Cell · doi:10.1016/s1534-5807(02)00188-0 · Cited by 510 · see citing works
Dynein mutations impair autophagic clearance of aggregate-prone proteins
Ravikumar, B., Acevedo‐Arozena, A., Imarisio, S., Berger, Z., Vacher, C., O’Kane, C. J., Brown, S. D. M., & Rubinsztein, D. C. (2005) · Nature Genetics · doi:10.1038/ng1591 · Cited by 458 · see citing works
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 · see citing works
Huntingtin Interacting Proteins Are Genetic Modifiers of Neurodegeneration
Kaltenbach, L. S., Romero, E., Becklin, R. R., Chettier, R., Bell, R. N., Phansalkar, A. R., Strand, A. D., Torcassi, C., Savage, J. R., Hurlburt, A. P., et al. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030082 · Cited by 430 · see citing works
Self-citationNollen, E. A. A., Garcia, S. M., van Haaften, G., Kim, S., Chavez, A., Morimoto, R. I., & Plasterk, R. H. A. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0307697101 · Cited by 416 · see citing works
Chen, H.-K., Fernandez-Funez, P., Acevedo, S. F., Lam, Y. C., Kaytor, M. D., Fernandez, M. H., Aitken, A., Skoulakis, E. M. C., Orr, H. T., Botas, J., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00349-0 · Cited by 414 · see citing works
Self-citationWilms Tumor Suppressor WTX Negatively Regulates WNT/ß-Catenin Signaling
Major, M. B., Camp, N. D., Berndt, J. D., Yi, X., Goldenberg, S. J., Hubbert, C. C., Biechele, T. L., Gingras, A., Zheng, N., MacCoss, M. J., et al. (2007) · Science · doi:10.1126/science/1141515 · Cited by 405 · see citing works
IKK phosphorylates Huntingtin and targets it for degradation by the proteasome and lysosome
Thompson, L. M., Aiken, C. T., Kaltenbach, L. S., Agrawal, N., Illes, K., Khoshnan, A., Martínez‐Vicente, M., Arrasate, M., O’Rourke, J. G., Khashwji, H., et al. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200909067 · Cited by 396 · see citing works
17-AAG, an Hsp90 inhibitor, ameliorates polyglutamine-mediated motor neuron degeneration
Waza, M., Adachi, H., Katsuno, M., Minamiyama, M., Sang, C., Tanaka, F., Inukai, A., Doyu, M., & Sobue, G. (2005) · Nature Medicine · doi:10.1038/nm1298 · Cited by 395 · see citing works
A Systems Level Analysis of Transcriptional Changes in Alzheimer's Disease and Normal Aging
Miller, J. A., Oldham, M. C., & Geschwind, D. H. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.4098-07.2008 · Cited by 385 · see citing works
Self-citationSIRT2 inhibition achieves neuroprotection by decreasing sterol biosynthesis
Luthi‐Carter, R., Taylor, D. M., Pallos, J., Lambert, E., Amore, A. M., Parker, J. A., Moffitt, H., Smith, D. L., Runne, H., Gökçe, Ö., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002924107 · Cited by 338 · see citing works
Systematic behavioral evaluation of Huntington's disease transgenic and knock-in mouse models
Menalled, L., El‐Khodor, B. F., Patry, M., Suárez‐Fariñas, M., Orenstein, S. J., Zahasky, B., Leahy, C. L., Wheeler, V. C., Yang, X. W., MacDonald, M. E., et al. (2009) · Neurobiology of Disease · doi:10.1016/j.nbd.2009.05.007 · Cited by 325 · see citing works
Self-citationGu, X., Greiner, E. R., Mishra, R. K., Kodali, R. B., Osmand, A., Finkbeiner, S. M., Steffan, J. S., Thompson, L. M., Wetzel, R. B., & Yang, X. W. (2009) · Neuron · doi:10.1016/j.neuron.2009.11.020 · Cited by 320 · see citing works
Self-citationRaymond, L. A., André, V. M., Cepeda, C., Gladding, C. M., Milnerwood, A. J., & Levine, M. S. (2011) · Neuroscience · doi:10.1016/j.neuroscience.2011.08.052 · Cited by 319 · see citing works
Creatine in Huntington disease is safe, tolerable, bioavailable in brain and reduces serum 8OH2′dG
Hersch, S. M., Gevorkian, S., Marder, K., Moskowitz, C., Feigin, A., Cox, M., Como, P., Zimmerman, C., Lin, M., Zhang, L., et al. (2006) · Neurology · doi:10.1212/01.wnl.0000194318.74946.b6 · Cited by 313 · see citing works
Opposing effects of polyglutamine expansion on native protein complexes contribute to SCA1
Lim, J., Crespo-Barreto, J., Jafar-Nejad, P., Bowman, A. B., Richman, R., Hill, D. E., Orr, H. T., & Zoghbi, H. Y. (2008) · Nature · doi:10.1038/nature06731 · Cited by 311 · see citing works
Tam, S. J., Geller, R., Spiess, C., & Frydman, J. (2006) · Nature Cell Biology · doi:10.1038/ncb1477 · Cited by 308 · see citing works
Serine 776 of Ataxin-1 Is Critical for Polyglutamine-Induced Disease in SCA1 Transgenic Mice
Emamian, E. S., Kaytor, M. D., Duvick, L. A., Zu, T., Tousey, S. K., Zoghbi, H. Y., Clark, H. B., & Orr, H. T. (2003) · Neuron · doi:10.1016/s0896-6273(03)00258-7 · Cited by 305 · see citing works
Fernández, E., Collins, M. O., Uren, R. T., Kopanitsa, M. V., Komiyama, N. H., Croning, M. D. R., Zografos, L., Armstrong, J. D., Choudhary, J. S., & Grant, S. G. N. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.27 · Cited by 275 · see citing works
Pallos, J., Bodai, L., Lukácsovich, T., Purcell, J. M., Steffan, J. S., Thompson, L. M., & Marsh, J. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn273 · Cited by 265 · see citing works
Huntingtin as an essential integrator of intracellular vesicular trafficking
Caviston, J. P., & Holzbaur, E. L. F. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.01.005 · Cited by 257 · see citing works
Tam, S. J., Spiess, C., Auyeung, W., Joachimiak, Ł. A., Chen, B., Poirier, M. A., & Frydman, J. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1700 · Cited by 243 · see citing works
Neuroscience in the era of functional genomics and systems biology
Geschwind, D. H., & Konopka, G. (2009) · Nature · doi:10.1038/nature08537 · Cited by 213 · see citing works
Self-citationWnt signaling in neuroprotection and stem cell differentiation
Toledo, E. M., Colombres, M., & Inestrosa, N. C. (2008) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2008.08.001 · Cited by 211 · see citing works
Maxwell, M. M., Tomkinson, E. M., Nobles, J., Wizeman, J. W., Amore, A. M., Quinti, L., Chopra, V., Hersch, S. M., & Kazantsev, A. G. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr326 · Cited by 209 · see citing works
Comparing Statistical Methods for Constructing Large Scale Gene Networks
Allen, J. D., Xie, Y., Chen, M., Girard, L., & Xiao, G. (2012) · PLoS ONE · doi:10.1371/journal.pone.0029348 · Cited by 186 · see citing works
Romero, E., Cha, G., Verstreken, P., Ly, C. V., Hughes, R. E., Bellen, H. J., & Botas, J. (2008) · Neuron · doi:10.1016/j.neuron.2007.11.025 · Cited by 171 · see citing works
Self-citationZhang, S., Binari, R., Zhou, R., & Perrimon, N. (2010) · Genetics · doi:10.1534/genetics.109.112516 · Cited by 160 · see citing works
Wang, Y., Meriin, A. B., Zaarur, N., Romanova, N. V., Chernoff, Y. O., Costello, C. E., & Sherman, M. Y. (2008) · The FASEB Journal · doi:10.1096/fj.08-117614 · Cited by 155 · see citing works
Decreased cAMP Response Element-mediated Transcription
Sugars, K. L., Brown, R. L., Cook, L. J., Swartz, J., & Rubinsztein, D. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310226200 · Cited by 139 · see citing works
Anne, S. L., Saudou, F., & Humbert, S. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1831-07.2007 · Cited by 132 · see citing works
Identification of ter94, Drosophila VCP, as a modulator of polyglutamine-induced neurodegeneration
Higashiyama, H., Hirose, F., Yamaguchi, M., Inoue, Y. H., Fujikake, N., Matsukage, A., & Kakizuka, A. (2002) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4400955 · Cited by 129 · see citing works
Gokhale, K., Newnam, G. P., Sherman, M. Y., & Chernoff, Y. O. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500390200 · Cited by 129 · see citing works
Mutant huntingtin‐impaired degradation of β‐catenin causes neurotoxicity in Huntington's disease
Godin, J. D., Poizat, G., Hickey, M. A., Maschat, F., & Humbert, S. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.117 · Cited by 126 · see citing works
A Genetic Screening Strategy Identifies Novel Regulators of the Proteostasis Network
Silva, M. C., Fox, S. G., Beam, M., Thakkar, H., Amaral, M. D., & Morimoto, R. I. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002438 · Cited by 116 · see citing works
Multiple pathways contribute to the pathogenesis of Huntington disease.
Li, S., & Li, X. (2006) · Molecular Neurodegeneration · doi:10.1186/1750-1326-1-19 · Cited by 109 · see citing works
CONNEXIN EXPRESSION IN HUNTINGTON'S DISEASED HUMAN BRAIN
Vis, J. C., Nicholson, L. F. B., Faull, R. L. M., Evans, W. H., Severs, N. J., & Green, C. R. (1998) · Cell Biology International · doi:10.1006/cbir.1998.0388 · Cited by 102 · see citing works
Isolation of a 40-kDa Huntingtin-associated Protein
Peters, M. F., & Ross, C. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m008099200 · Cited by 101 · see citing works
Fan, J., Cowan, C. M., Zhang, L. Y. J., Hayden, M. R., & Raymond, L. A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.2491-09.2009 · Cited by 100 · see citing works
Aggregation of Expanded Polyglutamine Domain in Yeast Leads to Defects in Endocytosis
Meriin, A. B., Zhang, X., Miliaras, N. B., Kazantsev, A., Chernoff, Y. O., McCaffery, J. M., Wendland, B., & Sherman, M. Y. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.21.7554-7565.2003 · Cited by 100 · see citing works
Kleiman, R. J., Kimmel, L. H., Bove, S. E., Lanz, T. A., Harms, J. F., Romegialli, A., Miller, K. S., Willis, A. D., Etages, S. D., Kuhn, M., et al. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.173294 · Cited by 97 · see citing works
Loss of SNAP‐25 and rabphilin 3a in sensory‐motor cortex in Huntington’s disease
Smith, R. A., Klein, P., Koc‐Schmitz, Y., Waldvogel, H. J., Faull, R. L. M., Brundin, P., Plomann, M., & Li, J. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04703.x · Cited by 87 · see citing works
Attar, N., & Cullen, P. J. (2009) · Advances in Enzyme Regulation · doi:10.1016/j.advenzreg.2009.10.002 · Cited by 86 · see citing works
Proteomic Studies of a Single CNS Synapse Type: The Parallel Fiber/Purkinje Cell Synapse
Selimi, F., Cristea, I. M., Heller, E. A., Chait, B. T., & Heintz, N. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000083 · Cited by 66 · see citing works
Small Molecule Inducers of Heat-Shock Response Reduce polyQ-Mediated Huntingtin Aggregation
Herbst, M., & Wanker, E. E. (2007) · Neurodegenerative Diseases · doi:10.1159/000101849 · Cited by 62 · see citing works
Wexler, E. M., Rosen, E., Lu, D., Osborn, G. E., Martin, E., Raybould, H., & Geschwind, D. H. (2011) · Science Signaling · doi:10.1126/scisignal.2002282 · Cited by 56 · see citing works
Self-citationShotgun Proteomics in Neuroscience
Liao, L., McClatchy, D. B., & Yates, J. R. (2009) · Neuron · doi:10.1016/j.neuron.2009.06.011 · Cited by 53 · see citing works
Tiagabine is neuroprotective in the N171-82Q and R6/2 mouse models of Huntington's disease
Masuda, N., Peng, Q., Li, Q., Jiang, M., Liang, Y., Wang, X., Zhao, M., Wang, W., Ross, C. A., & Duan, W. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.01.014 · Cited by 51 · see citing works
14-3-3zeta is indispensable for aggregate formation of polyglutamine-expanded huntingtin protein
Omi, K., Hachiya, N., Tanaka, M., Tokunaga, K., & Kaneko, K. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2007.11.018 · Cited by 43 · see citing works
Dupont, P., Besson, M. T., Devaux, J. J., & Liévens, J.-C. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.04.007 · Cited by 43 · see citing works
Wang, Y., Steimle, P. A., Ren, Y., Ross, C. A., Robinson, D. N., Egelhoff, T. T., Sesaki, H., & Iijima, M. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-11-0926 · Cited by 39 · see citing works
Angeli, S., Shao, J., & Diamond, M. I. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009053 · Cited by 36 · see citing works
Neurobiology of Huntington's Disease
Lo, D. C., & Hughes, R. E. (2010) · CRC Press eBooks · doi:10.1201/ebk0849390005 · Cited by 35 · see citing works
ROCK and PRK‐2 mediate the inhibitory effect of Y‐27632 on polyglutamine aggregation
Shao, J., Welch, W. J., & Diamond, M. I. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.04.009 · Cited by 33 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Saudou, F., & Humbert, S. (2016) · Neuron · doi:10.1016/j.neuron.2016.02.003 · Cited by 945 · see citing works
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 656 · see citing works
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 555 · see citing works
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 459 · see citing works
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 · see citing works
Self-citationIntegrated 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 · see citing works
Self-citationEpigenetic 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 391 · see citing works
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 368 · see citing works
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 324 · see citing works
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 201 · see citing works
Self-citationMass 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 199 · see citing works
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 · see citing works
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 201 · see citing works
Protein-protein interaction networks: probing disease mechanisms using model systems
Kuzmanov, U., & Emili, A. (2013) · Genome Medicine · doi:10.1186/gm441 · Cited by 197 · see citing works
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 188 · see citing works
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 169 · see citing works
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 · see citing works
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 · see citing works
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 153 · see citing works
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 152 · see citing works
Huntington’s Disease and Mitochondria
Farshbaf, M. J., & Ghaedi, K. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9766-1 · Cited by 148 · see citing works
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 · see citing works
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 138 · see citing works
Self-citationOulas, A., Minadakis, G., Zachariou, M., Sokratous, K., Bourdakou, M. M., & Spyrou, G. M. (2017) · Briefings in Bioinformatics · doi:10.1093/bib/bbx151 · Cited by 135 · see citing works
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 130 · see citing works
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 135 · see citing works
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 117 · see citing works
Cortical and Striatal Circuits in Huntington’s Disease
Blumenstock, S., & Dudanova, I. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00082 · Cited by 118 · see citing works
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 125 · see citing works
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 107 · see citing works
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 109 · see citing works
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 104 · see citing works
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 · see citing works
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 101 · see citing works
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 99 · see citing works
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 99 · see citing works
Self-citationTRiC 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 97 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Calabrese, G., Molzahn, C. M., & Mayor, T. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102062 · Cited by 90 · see citing works
Barron, J. C., Hurley, E. P., & Parsons, M. P. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.689332 · Cited by 85 · see citing works
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 · see citing works
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 79 · see citing works
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 · see citing works
Self-citationTranscriptional regulatory networks underlying gene expression changes in Huntington's disease
Ament, S. A., Pearl, J. R., Cantle, J. P., Bragg, R. M., Skene, P. J., Coffey, S. R., Bergey, D. E., Wheeler, V. C., MacDonald, M. E., Baliga, N. S., et al. (2018) · Molecular Systems Biology · doi:10.15252/msb.20167435 · Cited by 78 · see citing works
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 78 · see citing works
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 74 · see citing works
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 · see citing works
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 · see citing works
Self-citationXu, 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 · see citing works
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 · see citing works
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 67 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
Wang, J. K. T., Langfelder, P., Horvath, S., & Palazzolo, M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00149 · Cited by 60 · see citing works
Self-citationKedaigle, 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 59 · see citing works
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 58 · see citing works
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 58 · see citing works
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 52 · see citing works
Lee, C. Y. D., Cantle, J. P., & Yang, X. W. (2013) · FEBS Journal · doi:10.1111/febs.12418 · Cited by 56 · see citing works
Self-citationIs 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 55 · see citing works
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 · see citing works
Mammalian nerve globins in search of functions
Ascenzi, P., Gustincich, S., & Marino, M. (2014) · IUBMB Life · doi:10.1002/iub.1267 · Cited by 54 · see citing works
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 · see citing works
Brandstaetter, H., Kruppa, A. J., & Buß, F. (2014) · Disease Models & Mechanisms · doi:10.1242/dmm.017368 · Cited by 52 · see citing works
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 · see citing works
Self-citationThe Expanding Therapeutic Potential of Neuronal KCC2
Tang, B. L. (2020) · Cells · doi:10.3390/cells9010240 · Cited by 52 · see citing works
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 50 · see citing works
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 · see citing works
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 50 · see citing works
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 48 · see citing works
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 47 · see citing works
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 47 · see citing works
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 49 · see citing works
Élias, S., McGuire, J. R., Yu, H., & Humbert, S. (2015) · PLoS Biology · doi:10.1371/journal.pbio.1002142 · Cited by 47 · see citing works
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 46 · see citing works
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 44 · see citing works
Self-citationd-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 44 · see citing works
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 · see citing works
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 42 · see citing works
Cell Rearrangement and Oxidant/Antioxidant Imbalance in Huntington’s Disease
D’Egidio, F., Castelli, V., Cimini, A., & d’Angelo, M. (2023) · Antioxidants · doi:10.3390/antiox12030571 · Cited by 41 · see citing works
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 · see citing works
Self-citationStudying polyglutamine diseases in Drosophila
Xu, Z., Tito, A. J., Rui, Y., & Zhang, S. (2015) · Experimental Neurology · doi:10.1016/j.expneurol.2015.08.002 · Cited by 39 · see citing works
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 · see citing works
Dysregulation of 14‐3‐3 proteins in neurodegenerative diseases with Lewy body or Alzheimer pathology
McFerrin, M. B., Chi, X., Cutter, G., & Yacoubian, T. A. (2017) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.421 · Cited by 40 · see citing works
Cognitive dysfunction in H untington's disease: mechanisms and therapeutic strategies beyond BDNF
Puigdellívol, M., Saavedra, A., & Pérez‐Navarro, E. (2016) · Brain Pathology · doi:10.1111/bpa.12432 · Cited by 37 · see citing works
Heng, X., Guo, Q., Leung, A. W., & Li, J. Y. H. (2017) · eLife · doi:10.7554/elife.23253 · Cited by 39 · see citing works
Cause or compensation?—Altered neuronal Ca2+ handling in Huntington's disease
Mackay, J. P., Nassrallah, W. B., & Raymond, L. A. (2018) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12817 · Cited by 40 · see citing works
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 37 · see citing works
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 41 · see citing works
Kunowska, N., Rotival, M., Yu, L., Choudhary, J. S., & Dillon, N. (2015) · Nucleic Acids Research · doi:10.1093/nar/gku1350 · Cited by 38 · see citing works
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 33 · see citing works
14-3-3 mitigates alpha-synuclein aggregation and toxicity in the in vivo preformed fibril model
Underwood, R., Gannon, M. A., Pathak, A., Kapa, N., Chandra, S., Klop, A., & Yacoubian, T. A. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01110-5 · Cited by 37 · see citing works
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 38 · see citing works
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 38 · see citing works
Ratovitski, T., Chaerkady, R., Kammers, K., Stewart, J. C., Zavala, A., Pletniková, O., Troncoso, J. C., Rudnicki, D. D., Margolis, R. L., Cole, R. N., et al. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00448 · Cited by 37 · see citing works
- Authors
- Shirasaki, D. I., Greiner, E. R., Al-Ramahi, I., Gray, M., Boontheung, P., Geschwind, D. H., Botas, J., Coppola, G., Horvath, S., Loo, J. A., & Yang, X. W.
- Affiliations
- University of California, Los Angeles (US)
- Baylor College of Medicine (US)
- Corresponding author
- Loo, Joseph A.
- Yang, X. William
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2012-07
- Volume
- 75
- Issue
- 1
- Pages
- 41-57
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC3432264
- OpenAlex
- W2028159081
- Cited by
- 297
- References
- 77
- Citations by year
- 2026: 12 · 2025: 14 · 2024: 17 · 2023: 13 · 2022: 28 · 2021: 31 · 2020: 26 · 2019: 18 · 2018: 27 · 2017: 28 · 2016: 22 · 2015: 19 · 2014: 22 · 2013: 19 · 2012: 1
- FWCI
- 8.04
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Mental Health (R37MH060233)
- National Institute on Drug Abuse (R01DA030913)
- National Institute of General Medical Sciences (T32GM008496, R01GM103479)
- National Institute of Neurological Disorders and Stroke (T32NS043124, R01NS049501, R01NS074312, P30NS062691)
- National Center for Research Resources (R01RR020004, R01RR20004)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetics and Neurodevelopmental Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Bioinformatics and Genomic Networks
- Keywords
- huntingtin, protein-protein interaction network, Huntington's disease, brain regions, age-related changes, microtubule transport, proteostasis, genetic modifiers, Drosophila model, weighted gene co-expression network analysis
- MeSH terms
- Huntingtin Protein, Animals, Brain, Disease Models, Animal, Drosophila, Female, Humans, Mice, Transgenic, Nerve Tissue Proteins, Proteomics, Mice, Gene Regulatory Networks
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review