User menu

Tau interactome mapping based identification of Otub1 as Tau deubiquitinase involved in accumulation of pathological Tau forms in vitro and in vivo.

Bibliographic reference Wang, Peng ; Joberty, G ; Buist, A ; Vanoosthuyse, Alexandre ; Stancu, Ilie-Cosmin ; et. al. Tau interactome mapping based identification of Otub1 as Tau deubiquitinase involved in accumulation of pathological Tau forms in vitro and in vivo.. In: Acta Neuropathologica,
Permanent URL http://hdl.handle.net/2078.1/181292
  1. Babu Jeganathan Ramesh, Geetha Thangiah, Wooten Marie W., Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation, 10.1111/j.1471-4159.2005.03181.x
  2. Balakirev M. Y., Tcherniuk S. O., Jaquinod M., Chroboczek J., Otubains: a new family of cysteine proteases in the ubiquitin pathway, 10.1038/sj.embor.embor824
  3. Bantscheff Marcus, Eberhard Dirk, Abraham Yann, Bastuck Sonja, Boesche Markus, Hobson Scott, Mathieson Toby, Perrin Jessica, Raida Manfred, Rau Christina, Reader Valérie, Sweetman Gavain, Bauer Andreas, Bouwmeester Tewis, Hopf Carsten, Kruse Ulrich, Neubauer Gitte, Ramsden Nigel, Rick Jens, Kuster Bernhard, Drewes Gerard, Quantitative chemical proteomics reveals mechanisms of action of clinical ABL kinase inhibitors, 10.1038/nbt1328
  4. Bantscheff Marcus, Hopf Carsten, Savitski Mikhail M, Dittmann Antje, Grandi Paola, Michon Anne-Marie, Schlegl Judith, Abraham Yann, Becher Isabelle, Bergamini Giovanna, Boesche Markus, Delling Manja, Dümpelfeld Birgit, Eberhard Dirk, Huthmacher Carola, Mathieson Toby, Poeckel Daniel, Reader Valérie, Strunk Katja, Sweetman Gavain, Kruse Ulrich, Neubauer Gitte, Ramsden Nigel G, Drewes Gerard, Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes, 10.1038/nbt.1759
  5. Bantscheff Marcus, Schirle Markus, Sweetman Gavain, Rick Jens, Kuster Bernhard, Quantitative mass spectrometry in proteomics: a critical review, 10.1007/s00216-007-1486-6
  6. Berger Z., Roder H., Hanna A., Carlson A., Rangachari V., Yue M., Wszolek Z., Ashe K., Knight J., Dickson D., Andorfer C., Rosenberry T. L., Lewis J., Hutton M., Janus C., Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy, 10.1523/jneurosci.0587-07.2007
  7. Berke Sarah J Shoesmith, Paulson Henry L, Protein aggregation and the ubiquitin proteasome pathway: gaining the UPPer hand on neurodegeneration, 10.1016/s0959-437x(03)00053-4
  8. Blair Laura J., Nordhues Bryce A., Hill Shannon E., Scaglione K. Matthew, O’Leary John C., Fontaine Sarah N., Breydo Leonid, Zhang Bo, Li Pengfei, Wang Li, Cotman Carl, Paulson Henry L., Muschol Martin, Uversky Vladimir N., Klengel Torsten, Binder Elisabeth B., Kayed Rakez, Golde Todd E., Berchtold Nicole, Dickey Chad A., Accelerated neurodegeneration through chaperone-mediated oligomerization of tau, 10.1172/jci69003
  9. Braak H., Braak E., Neuropathological stageing of Alzheimer-related changes, 10.1007/bf00308809
  10. Brajenovic Miro, Joberty Gerard, Küster Bernhard, Bouwmeester Tewis, Drewes Gerard, Comprehensive Proteomic Analysis of Human Par Protein Complexes Reveals an Interconnected Protein Network, 10.1074/jbc.m312171200
  11. Castillo-Carranza Diana L., Gerson Julia E., Sengupta Urmi, Guerrero-Muñoz Marcos J., Lasagna-Reeves Cristian A., Kayed Rakez, Specific Targeting of Tau Oligomers in Htau Mice Prevents Cognitive Impairment and Tau Toxicity Following Injection with Brain-Derived Tau Oligomeric Seeds, 10.3233/jad-132477
  12. Castillo-Carranza D. L., Sengupta U., Guerrero-Munoz M. J., Lasagna-Reeves C. A., Gerson J. E., Singh G., Estes D. M., Barrett A. D. T., Dineley K. T., Jackson G. R., Kayed R., Passive Immunization with Tau Oligomer Monoclonal Antibody Reverses Tauopathy Phenotypes without Affecting Hyperphosphorylated Neurofibrillary Tangles, 10.1523/jneurosci.3192-13.2014
  13. Cripps Diane, Thomas Stefani N., Jeng Young, Yang Frank, Davies Peter, Yang Austin J., Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation, 10.1074/jbc.m512786200
  14. David Della C., Layfield Robert, Serpell Louise, Narain Yolanda, Goedert Michel, Spillantini Maria Grazia, Proteasomal degradation of tau protein : Tau and the proteasome, 10.1046/j.1471-4159.2002.01137.x
  15. Deger Jennifer M., Gerson Julia E., Kayed Rakez, The interrelationship of proteasome impairment and oligomeric intermediates in neurodegeneration, 10.1111/acel.12359
  16. Dickey C. A., Yue M., Lin W.-L., Dickson D. W., Dunmore J. H., Lee W. C., Zehr C., West G., Cao S., Clark A. M. K., Caldwell G. A., Caldwell K. A., Eckman C., Patterson C., Hutton M., Petrucelli L., Deletion of the Ubiquitin Ligase CHIP Leads to the Accumulation, But Not the Aggregation, of Both Endogenous Phospho- and Caspase-3-Cleaved Tau Species, 10.1523/jneurosci.0746-06.2006
  17. Edelmann Mariola J., Iphöfer Alexander, Akutsu Masato, Altun Mikael, di Gleria Katalin, Kramer Holger B., Fiebiger Edda, Dhe-Paganon Sirano, Kessler Benedikt M., Structural basis and specificity of human otubain 1-mediated deubiquitination, 10.1042/bj20081318
  18. Eroglu B., Moskophidis D., Mivechi N. F., Loss of Hsp110 Leads to Age-Dependent Tau Hyperphosphorylation and Early Accumulation of Insoluble Amyloid  , 10.1128/mcb.01493-09
  19. Flach Katharina, Ramminger Ellen, Hilbrich Isabel, Arsalan-Werner Annika, Albrecht Franziska, Herrmann Lydia, Goedert Michel, Arendt Thomas, Holzer Max, Axotrophin/MARCH7 acts as an E3 ubiquitin ligase and ubiquitinates tau protein in vitro impairing microtubule binding, 10.1016/j.bbadis.2014.05.029
  20. Giannakopoulos P., Herrmann F. R., Bussiere T., Bouras C., Kovari E., Perl D. P., Morrison J. H., Gold G., Hof P. R., Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer's disease, 10.1212/01.wnl.0000063311.58879.01
  21. Goldbaum O, Oppermann M, Handschuh M, Dabir D, Zhang B, Forman MS, Trojanowski JQ, Lee VM, Richter-Landsberg C (2003) Proteasome inhibition stabilizes tau inclusions in oligodendroglial cells that occur after treatment with okadaic acid. J Neurosci 23:8872–8880
  22. Goldberg Alfred L., Protein degradation and protection against misfolded or damaged proteins, 10.1038/nature02263
  23. Goncharov Tatiana, Niessen Kyle, de Almagro Maria Cristina, Izrael-Tomasevic Anita, Fedorova Anna V, Varfolomeev Eugene, Arnott David, Deshayes Kurt, Kirkpatrick Donald S, Vucic Domagoj, OTUB1 modulates c-IAP1 stability to regulate signalling pathways, 10.1038/emboj.2013.62
  24. Guo Jing L., Lee Virginia M.-Y., Seeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles, 10.1074/jbc.m110.209296
  25. Han Dong Hoon, Na Hee-Kyung, Choi Won Hoon, Lee Jung Hoon, Kim Yun Kyung, Won Cheolhee, Lee Seung-Han, Kim Kwang Pyo, Kuret Jeff, Min Dal-Hee, Lee Min Jae, Direct cellular delivery of human proteasomes to delay tau aggregation, 10.1038/ncomms6633
  26. Herhaus Lina, Al-Salihi Mazin, Macartney Thomas, Weidlich Simone, Sapkota Gopal P., OTUB1 enhances TGFβ signalling by inhibiting the ubiquitylation and degradation of active SMAD2/3, 10.1038/ncomms3519
  27. Huber Kilian V M, Olek Karin M, Müller André C, Tan Chris Soon Heng, Bennett Keiryn L, Colinge Jacques, Superti-Furga Giulio, Proteome-wide drug and metabolite interaction mapping by thermal-stability profiling, 10.1038/nmeth.3590
  28. Ihara Y., Morishima-Kawashima M., Nixon R., The Ubiquitin-Proteasome System and the Autophagic-Lysosomal System in Alzheimer Disease, 10.1101/cshperspect.a006361
  29. Irmler Martin, Gentier Romina J. G., Dennissen Frank J. A., Schulz Holger, Bolle Ines, Hölter Sabine M., Kallnik Magdalena, Cheng Jing Jun, Klingenspor Martin, Rozman Jan, Ehrhardt Nicole, Hermes Denise J. H. P., Gailus-Durner Valérie, Fuchs Helmut, Hrabě de Angelis Martin, Meyer Helmut E., Hopkins David A., Van Leeuwen Fred W., Beckers Johannes, Long-term proteasomal inhibition in transgenic mice by UBB+1 expression results in dysfunction of central respiration control reminiscent of brainstem neuropathology in Alzheimer patients, 10.1007/s00401-012-1003-7
  30. Jinwal Umesh K., O'Leary John C., Borysov Sergiy I., Jones Jeffrey R., Li Qingyou, Koren John, Abisambra Jose F., Vestal Grant D., Lawson Lisa Y., Johnson Amelia G., Blair Laura J., Jin Ying, Miyata Yoshinari, Gestwicki Jason E., Dickey Chad A., Hsc70 Rapidly Engages Tau after Microtubule Destabilization, 10.1074/jbc.m110.113753
  31. Juang Yu-Chi, Landry Marie-Claude, Sanches Mario, Vittal Vinayak, Leung Charles C.Y., Ceccarelli Derek F., Mateo Abigail-Rachele F., Pruneda Jonathan N., Mao Daniel Y.L., Szilard Rachel K., Orlicky Stephen, Munro Meagan, Brzovic Peter S., Klevit Rachel E., Sicheri Frank, Durocher Daniel, OTUB1 Co-opts Lys48-Linked Ubiquitin Recognition to Suppress E2 Enzyme Function, 10.1016/j.molcel.2012.01.011
  32. Karunarathna U, Kongsema M, Zona S, Gong C, Cabrera E, Gomes A R, Man E P S, Khongkow P, Tsang J W-H, Khoo U-S, Medema R H, Freire R, Lam E W-F, OTUB1 inhibits the ubiquitination and degradation of FOXM1 in breast cancer and epirubicin resistance, 10.1038/onc.2015.208
  33. Kayed Rakez, Jackson George R, Prefilament tau species as potential targets for immunotherapy for Alzheimer disease and related disorders, 10.1016/j.coi.2009.05.001
  34. Keck Susi, Nitsch Robert, Grune Tilman, Ullrich Oliver, Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease : Proteasome inhibition in Alzheimer's disease, 10.1046/j.1471-4159.2003.01642.x
  35. Keller J, The proteasome in brain aging, 10.1016/s1568-1637(01)00006-x
  36. Kraft Claudine, Peter Matthias, Hofmann Kay, Selective autophagy: ubiquitin-mediated recognition and beyond, 10.1038/ncb0910-836
  37. Krüger Lars, Mandelkow Eva Maria, Tau neurotoxicity and rescue in animal models of human Tauopathies, 10.1016/j.conb.2015.09.004
  38. Lam Y. A., Pickart C. M., Alban A., Landon M., Jamieson C., Ramage R., Mayer R. J., Layfield R., Inhibition of the ubiquitin-proteasome system in Alzheimer's disease, 10.1073/pnas.170173897
  39. Lasagna-Reeves Cristian A., Castillo-Carranza Diana L., Guerrero-Muñoz Marcos J., Jackson George R., Kayed Rakez, Preparation and Characterization of Neurotoxic Tau Oligomers, 10.1021/bi1016233
  40. Lasagna-Reeves C. A., Castillo-Carranza D. L., Sengupta U., Sarmiento J., Troncoso J., Jackson G. R., Kayed R., Identification of oligomers at early stages of tau aggregation in Alzheimer's disease, 10.1096/fj.11-199851
  41. Lee Gloria, Neve Rachael L., Kosik Kenneth S., The microtubule binding domain of tau protein, 10.1016/0896-6273(89)90050-0
  42. Leroy Elisabeth, Boyer Rebecca, Auburger Georg, Leube Barbara, Ulm Gudrun, Mezey Eva, Harta Gyongyi, Brownstein Michael J., Jonnalagada Sobhanadditya, Chernova Tanya, Dehejia Anindya, Lavedan Christian, Gasser# Thomas, Steinbach Peter J., Wilkinson Keith D., Polymeropoulos Mihael H., 10.1038/26652
  43. Levine Beth, Klionsky Daniel J, Development by Self-Digestion, 10.1016/s1534-5807(04)00099-1
  44. Li Shu, Zheng Hao, Mao Ai-Ping, Zhong Bo, Li Ying, Liu Yu, Gao Yan, Ran Yong, Tien Po, Shu Hong-Bing, Regulation of Virus-triggered Signaling by OTUB1- and OTUB2-mediated Deubiquitination of TRAF3 and TRAF6, 10.1074/jbc.m109.074971
  45. Lindsten Kristina, de Vrij Femke M.S., Verhoef Lisette G.G.C., Fischer David F., van Leeuwen Fred W., Hol Elly M., Masucci Maria G., Dantuma Nico P., Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation, 10.1083/jcb.200111034
  46. Luo Hong-Bin, Xia Yi-Yuan, Shu Xi-Ji, Liu Zan-Chao, Feng Ye, Liu Xing-Hua, Yu Guang, Yin Gang, Xiong Yan-Si, Zeng Kuan, Jiang Jun, Ye Keqiang, Wang Xiao-Chuan, Wang Jian-Zhi, SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination, 10.1073/pnas.1417548111
  47. Magnani Enrico, Fan Juan, Gasparini Laura, Golding Matthew, Williams Meredith, Schiavo Giampietro, Goedert Michel, Amos Linda A, Spillantini Maria Grazia, Interaction of tau protein with the dynactin complex, 10.1038/sj.emboj.7601878
  48. Messick Troy Eugene, Russell Nathaniel Scott, Iwata Ayaka Jennifer, Sarachan Kathryn Lorenz, Shiekhattar Ramin, Shanks John R., Reyes-Turcu Francisca E., Wilkinson Keith D., Marmorstein Ronen, Structural Basis for Ubiquitin Recognition by the Otu1 Ovarian Tumor Domain Protein, 10.1074/jbc.m704398200
  49. Mori H, Kondo J, Ihara Y, Ubiquitin is a component of paired helical filaments in Alzheimer's disease, 10.1126/science.3029875
  50. Morishima-Kawashima Maho, Hasegawa Masato, Takio Koji, Suzuki Masami, Titani Koiti, Ihara Yasuo, Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments, 10.1016/0896-6273(93)90063-w
  51. Morris Meaghan, Knudsen Giselle M, Maeda Sumihiro, Trinidad Jonathan C, Ioanoviciu Alexandra, Burlingame Alma L, Mucke Lennart, Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice, 10.1038/nn.4067
  52. Myeku Natura, Clelland Catherine L, Emrani Sheina, Kukushkin Nikolay V, Yu Wai Haung, Goldberg Alfred L, Duff Karen E, Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling, 10.1038/nm.4011
  53. Nakada Shinichiro, Tai Ikue, Panier Stephanie, Al-Hakim Abdallah, Iemura Shun-ichiro, Juang Yu-Chi, O’Donnell Lara, Kumakubo Ayako, Munro Meagan, Sicheri Frank, Gingras Anne-Claude, Natsume Tohru, Suda Toshio, Durocher Daniel, Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1, 10.1038/nature09297
  54. Oddo Salvatore, Billings Lauren, Kesslak J.Patrick, Cribbs David H., LaFerla Frank M., Aβ Immunotherapy Leads to Clearance of Early, but Not Late, Hyperphosphorylated Tau Aggregates via the Proteasome, 10.1016/j.neuron.2004.07.003
  55. Olzmann James A., Chin Lih-Shen, Parkin-mediated K63-linked polyubiquitination: A signal for targeting misfolded proteins to the aggresome-autophagy pathway, 10.4161/auto.5172
  56. Paine Simon, Bedford Lynn, Thorpe Julian R., Mayer R. John, Cavey James R., Bajaj Nin, Sheppard Paul W., Lowe James, Layfield Robert, Immunoreactivity to Lys63-linked polyubiquitin is a feature of neurodegeneration, 10.1016/j.neulet.2009.05.074
  57. Petrucelli L., CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation, 10.1093/hmg/ddh083
  58. Reinhard Friedrich B M, Eberhard Dirk, Werner Thilo, Franken Holger, Childs Dorothee, Doce Carola, Savitski Maria Fälth, Huber Wolfgang, Bantscheff Marcus, Savitski Mikhail M, Drewes Gerard, Thermal proteome profiling monitors ligand interactions with cellular membrane proteins, 10.1038/nmeth.3652
  59. Roberson E. D., Scearce-Levie K., Palop J. J., Yan F., Cheng I. H., Wu T., Gerstein H., Yu G.-Q., Mucke L., Reducing Endogenous Tau Ameliorates Amyloid  -Induced Deficits in an Alzheimer's Disease Mouse Model, 10.1126/science.1141736
  60. SantaCruz K., Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function, 10.1126/science.1113694
  61. Sato Yusuke, Yamagata Atsushi, Goto-Ito Sakurako, Kubota Keiko, Miyamoto Rikako, Nakada Shinichiro, Fukai Shuya, Molecular Basis of Lys-63-linked Polyubiquitination Inhibition by the Interaction between Human Deubiquitinating Enzyme OTUB1 and Ubiquitin-conjugating Enzyme UBC13, 10.1074/jbc.m112.364752
  62. Savitski M. M., Reinhard F. B. M., Franken H., Werner T., Savitski M. F., Eberhard D., Molina D. M., Jafari R., Dovega R. B., Klaeger S., Kuster B., Nordlund P., Bantscheff M., Drewes G., Tracking cancer drugs in living cells by thermal profiling of the proteome, 10.1126/science.1255784
  63. Shimura Hideki, Schwartz Daniel, Gygi Steven P., Kosik Kenneth S., CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival, 10.1074/jbc.m305838200
  64. Stancu I.-C., Ris L., Vasconcelos B., Marinangeli C., Goeminne L., Laporte V., Haylani L. E., Couturier J., Schakman O., Gailly P., Pierrot N., Kienlen-Campard P., Octave J.-N., Dewachter I., Tauopathy contributes to synaptic and cognitive deficits in a murine model for Alzheimer's disease, 10.1096/fj.13-246702
  65. Stancu Ilie-Cosmin, Vasconcelos Bruno, Ris Laurence, Wang Peng, Villers Agnès, Peeraer Eve, Buist Arjan, Terwel Dick, Baatsen Peter, Oyelami Tutu, Pierrot Nathalie, Casteels Cindy, Bormans Guy, Kienlen-Campard Pascal, Octave Jean-Nöel, Moechars Diederik, Dewachter Ilse, Templated misfolding of Tau by prion-like seeding along neuronal connections impairs neuronal network function and associated behavioral outcomes in Tau transgenic mice, 10.1007/s00401-015-1413-4
  66. Sun Xiao-Xin, Challagundla Kishore B, Dai Mu-Shui, Positive regulation of p53 stability and activity by the deubiquitinating enzyme Otubain 1 : Regulation of p53 by Otub1, 10.1038/emboj.2011.434
  67. Sydow A., Van der Jeugd A., Zheng F., Ahmed T., Balschun D., Petrova O., Drexler D., Zhou L., Rune G., Mandelkow E., D'Hooge R., Alzheimer C., Mandelkow E.-M., Tau-Induced Defects in Synaptic Plasticity, Learning, and Memory Are Reversible in Transgenic Mice after Switching Off the Toxic Tau Mutant, 10.1523/jneurosci.5245-10.2011
  68. Tan Jeanne M.M., Wong Esther S.P., Kirkpatrick Donald S., Pletnikova Olga, Ko Han Seok, Tay Shiam-Peng, Ho Michelle W.L., Troncoso Juan, Gygi Steven P., Lee Michael K., Dawson Valina L., Dawson Ted M., Lim Kah-Leong, Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases, 10.1093/hmg/ddm320
  69. Thal D. R., Rub U., Orantes M., Braak H., Phases of A -deposition in the human brain and its relevance for the development of AD, 10.1212/wnl.58.12.1791
  70. Van der Jeugd Ann, Hochgräfe Katja, Ahmed Tariq, Decker Jochen M., Sydow Astrid, Hofmann Anne, Wu Dan, Messing Lars, Balschun Detlef, D’Hooge Rudi, Mandelkow Eva-Maria, Cognitive defects are reversible in inducible mice expressing pro-aggregant full-length human Tau, 10.1007/s00401-012-0987-3
  71. van Leeuwen F. W., Frameshift Mutants of  Amyloid Precursor Protein and Ubiquitin-B in Alzheimer's and Down Patients, 10.1126/science.279.5348.242
  72. Vasconcelos Bruno, Stancu Ilie-Cosmin, Buist Arjan, Bird Matthew, Wang Peng, Vanoosthuyse Alexandre, Van Kolen Kristof, Verheyen An, Kienlen-Campard Pascal, Octave Jean-Noël, Baatsen Peter, Moechars Diederik, Dewachter Ilse, Heterotypic seeding of Tau fibrillization by pre-aggregated Abeta provides potent seeds for prion-like seeding and propagation of Tau-pathology in vivo, 10.1007/s00401-015-1525-x
  73. Verbitsky M., Altered Hippocampal Transcript Profile Accompanies an Age-Related Spatial Memory Deficit in Mice, 10.1101/lm.68204
  74. Wang Tao, Yin Luming, Cooper Eric M., Lai Ming-Yih, Dickey Seth, Pickart Cecile M., Fushman David, Wilkinson Keith D., Cohen Robert E., Wolberger Cynthia, Evidence for Bidentate Substrate Binding as the Basis for the K48 Linkage Specificity of Otubain 1, 10.1016/j.jmb.2008.12.085
  75. Weingarten M. D., Lockwood A. H., Hwo S. Y., Kirschner M. W., A protein factor essential for microtubule assembly., 10.1073/pnas.72.5.1858
  76. Werner Thilo, Becher Isabelle, Sweetman Gavain, Doce Carola, Savitski Mikhail M., Bantscheff Marcus, High-Resolution Enabled TMT 8-plexing, 10.1021/ac301553x
  77. Wiener Reuven, DiBello Anthony T, Lombardi Patrick M, Guzzo Catherine M, Zhang Xiangbin, Matunis Michael J, Wolberger Cynthia, E2 ubiquitin-conjugating enzymes regulate the deubiquitinating activity of OTUB1, 10.1038/nsmb.2655
  78. Wiener Reuven, Zhang Xiangbin, Wang Tao, Wolberger Cynthia, The mechanism of OTUB1-mediated inhibition of ubiquitination, 10.1038/nature10911
  79. Witman G. B., Cleveland D. W., Weingarten M. D., Kirschner M. W., Tubulin requires tau for growth onto microtubule initiating sites., 10.1073/pnas.73.11.4070
  80. Wooten Marie W., Geetha Thangiah, Babu J. Ramesh, Seibenhener M. Lamar, Peng Junmin, Cox Nancy, Diaz-Meco Maria-T., Moscat Jorge, Essential Role of Sequestosome 1/p62 in Regulating Accumulation of Lys63-ubiquitinated Proteins, 10.1074/jbc.m709496200
  81. Yoshiyama Yasumasa, Higuchi Makoto, Zhang Bin, Huang Shu-Ming, Iwata Nobuhisa, Saido Takaomi C., Maeda Jun, Suhara Tetsuya, Trojanowski John Q., Lee Virginia M.-Y., Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model, 10.1016/j.neuron.2007.01.010