Cited by 21

The DOI matches its Crossref record; 19 of the 19 references it cites were found in a registry or an index.

The fine-tuning of proteolytic pathways in Alzheimer’s disease

Cecarini, Valentina, Bonfili, Laura, Cuccioloni, Massimiliano, Mozzicafreddo, Matteo, Angeletti, Mauro, Keller, Jeffrey N., Eleuteri, Anna Maria·2016·Cellular and Molecular Life Sciences

Overview

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.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.1007/s00018-016-2238-6

Cites

19 of 19 references verified0 citation errors · 0 not checkable

Statistics

Verification

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.

A few free checks a day · papers already verified open instantly · results are public

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Flagged first, then by citations

Show all 19 references

Research works printed but not linked: 183

  1. Ciechanover A (2005) Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Cell Death Differ 12(9):1178–1190. doi: 10.1038/sj.cdd.4401692 · DOI
  2. Fecto F, Esengul YT, Siddique T (2014) Protein recycling pathways in neurodegenerative diseases. Alzheimers Res Ther 6(2):13. doi: 10.1186/alzrt243 · DOI
  3. Tanaka K (1843) Matsuda N (2014) Proteostasis and neurodegeneration: the roles of proteasomal degradation and autophagy. Biochim Biophys Acta 1:197–204. doi: 10.1016/j.bbamcr.2013.03.012 · DOI
  4. Nijholt DAT, De Kimpe L, Elfrink HL, Hoozemans JJM, Scheper W (2011) Removing protein aggregates: the role of proteolysis in neurodegeneration. Curr Med Chem 18(16):2459–2476 · DOI
  5. Stadtman ER (2006) Protein oxidation and aging. Free Radical Res 40(12):1250–1258. doi: 10.1080/10715760600918142 · DOI
  6. Stadtman ER (2001) Protein oxidation in aging and age-related diseases. Ann N Y Acad Sci 928:22–38 · DOI · Paper page
  7. Haass C, Selkoe DJ (2007) Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer’s amyloid beta-peptide. Nat Rev Mol Cell Biol 8(2):101–112. doi: 10.1038/nrm2101 · DOI · Paper page
  8. Serrano-Pozo A, Frosch MP, Masliah E, Hyman BT (2011) Neuropathological alterations in Alzheimer disease. Cold Spring Harbor perspectives in medicine 1(1):a006189. doi: 10.1101/cshperspect.a006189 · DOI · Paper page
  9. Varshavsky A (2005) Regulated protein degradation. Trends Biochem Sci 30(6):283–286. doi: 10.1016/j.tibs.2005.04.005 · DOI
  10. Wang DW, Peng ZJ, Ren GF, Wang GX (2015) The different roles of selective autophagic protein degradation in mammalian cells. Oncotarget 6(35):37098–37116. doi: 10.18632/oncotarget.5776 · DOI
  11. Kirkegaard T, Jaattela M (2009) Lysosomal involvement in cell death and cancer. Biochim Biophys Acta 1793(4):746–754. doi: 10.1016/j.bbamcr.2008.09.008 · DOI
  12. Cuervo AM (2004) Autophagy: in sickness and in health. Trends Cell Biol 14(2):70–77. doi: 10.1016/j.tcb.2003.12.002 · DOI
  13. Massey AC, Zhang C, Cuervo AM (2006) Chaperone-mediated autophagy in aging and disease. Curr Top Dev Biol 73:205–235. doi: 10.1016/S0070-2153(05)73007-6 · DOI · Paper page
  14. Martinez-Vicente M, Cuervo AM (2007) Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol 6(4):352–361. doi: 10.1016/S1474-4422(07)70076-5 · DOI
  15. Wolfe DM, Lee JH, Kumar A, Lee S, Orenstein SJ, Nixon RA (2013) Autophagy failure in Alzheimer’s disease and the role of defective lysosomal acidification. Euro J Neurosci 37(12):1949–1961. doi: 10.1111/ejn.12169 · DOI
  16. Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, Suzuki-Migishima R, Yokoyama M, Mishima K, Saito I, Okano H, Mizushima N (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441(7095):885–889. doi: 10.1038/nature04724 · DOI · Paper page
  17. Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I, Ueno T, Koike M, Uchiyama Y, Kominami E, Tanaka K (2006) Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441(7095):880–884. doi: 10.1038/nature04723 · DOI · Paper page
  18. Piras A, Collin L, Gruninger F, Graff C, Ronnback A (2016) Autophagic and lysosomal defects in human tauopathies: analysis of post-mortem brain from patients with familial Alzheimer disease, corticobasal degeneration and progressive supranuclear palsy. Acta Neuropathol Commun 4(1):22. doi: 10.1186/s40478-016-0292-9 · DOI · Paper page
  19. Jung T, Catalgol B, Grune T (2009) The proteasomal system. Mol Aspects Med 30(4):191–296. doi: 10.1016/j.mam.2009.04.001 · DOI
  20. Tu Y, Chen C, Pan J, Xu J, Zhou ZG, Wang CY (2012) The Ubiquitin Proteasome Pathway (UPP) in the regulation of cell cycle control and DNA damage repair and its implication in tumorigenesis. Int J Clin Experim Pathol 5(8):726–738
  21. Loda M, Cukor B, Tam SW, Lavin P, Fiorentino M, Draetta GF, Jessup JM, Pagano M (1997) Increased proteasome-dependent degradation of the cyclin-dependent kinase inhibitor p27 in aggressive colorectal carcinomas. Nat Med 3(2):231–234 · DOI
  22. Spataro V, Norbury C, Harris AL (1998) The ubiquitin-proteasome pathway in cancer. Br J Cancer 77(3):448–455 · DOI
  23. Hu X, Bryington M, Fisher AB, Liang X, Zhang X, Cui D, Datta I, Zuckerman KS (2002) Ubiquitin/proteasome-dependent degradation of D-type cyclins is linked to tumor necrosis factor-induced cell cycle arrest. J Biol Chem 277(19):16528–16537. doi: 10.1074/jbc.M109929200 · DOI
  24. Yam CH, Siu WY, Lau A, Poon RY (2000) Degradation of cyclin A does not require its phosphorylation by CDC2 and cyclin-dependent kinase 2. J Biol Chem 275(5):3158–3167 · DOI
  25. Dimova NV, Hathaway NA, Lee BH, Kirkpatrick DS, Berkowitz ML, Gygi SP, Finley D, King RW (2012) APC/C-mediated multiple monoubiquitylation provides an alternative degradation signal for cyclin B1. Nat Cell Biol 14(2):168–176. doi: 10.1038/ncb2425 · DOI
  26. Ikeuchi K, Marusawa H, Fujiwara M, Matsumoto Y, Endo Y, Watanabe T, Iwai A, Sakai Y, Takahashi R, Chiba T (2009) Attenuation of proteolysis-mediated cyclin E regulation by alternatively spliced Parkin in human colorectal cancers. Int J Cancer J Int du Cancer 125(9):2029–2035. doi: 10.1002/ijc.24565 · DOI
  27. Gregory MA, Hann SR (2000) c-Myc proteolysis by the ubiquitin-proteasome pathway: stabilization of c-Myc in Burkitt’s lymphoma cells. Mol Cell Biol 20(7):2423–2435 · DOI
  28. He H, Qi XM, Grossmann J, Distelhorst CW (1998) c-Fos degradation by the proteasome. An early, Bcl-2-regulated step in apoptosis. J Biol Chem 273(39):25015–25019 · DOI
  29. Ciechanover A (1998) The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J 17(24):7151–7160. doi: 10.1093/emboj/17.24.7151 · DOI
  30. Tramutola A, Di Domenico F, Barone E, Perluigi M, Butterfield DA (2016) It Is All about (U)biquitin: Role of Altered Ubiquitin-Proteasome System and UCHL1 in Alzheimer Disease. Oxidat Med Cell Long 2016:2756068. doi: 10.1155/2016/2756068 · DOI
  31. Baumeister W, Walz J, Zuhl F, Seemuller E (1998) The proteasome: paradigm of a self-compartmentalizing protease. Cell 92(3):367–380 · DOI
  32. Ellgaard L, Helenius A (2003) Quality control in the endoplasmic reticulum. Nat Rev Mol Cell Biol 4(3):181–191. doi: 10.1038/nrm1052 · DOI
  33. Ruggiano A, Foresti O, Carvalho P (2014) Quality control: ER-associated degradation: protein quality control and beyond. J Cell Biol 204(6):869–879. doi: 10.1083/jcb.201312042 · DOI
  34. Luo GR, Le WD (2010) Collective roles of molecular chaperones in protein degradation pathways associated with neurodegenerative diseases. Curr Pharm Biotechnol 11(2):180–187 · DOI
  35. Sulistio YA, Heese K (2016) The ubiquitin-proteasome system and molecular chaperone deregulation in Alzheimer’s disease. Mol Neurobiol 53(2):905–931. doi: 10.1007/s12035-014-9063-4 · DOI
  36. Yerbury JJ, Ooi L, Dillin A, Saunders DN, Hatters DM, Beart PM, Cashman NR, Wilson MR, Ecroyd H (2016) Walking the tightrope: Proteostasis and neurodegenerative disease. J Neurochem. doi: 10.1111/jnc.13575 · DOI
  37. 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(26):8872–8880 · DOI
  38. Cecarini V, Ding Q, Keller JN (2007) Oxidative inactivation of the proteasome in Alzheimer’s disease. Free Radical Res 41(6):673–680. doi: 10.1080/10715760701286159 · DOI
  39. Keck S, Nitsch R, Grune T, Ullrich O (2003) Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer’s disease. J Neurochem 85(1):115–122 · DOI · Paper page
  40. Sullivan PG, Dragicevic NB, Deng JH, Bai Y, Dimayuga E, Ding Q, Chen Q, Bruce-Keller AJ, Keller JN (2004) Proteasome inhibition alters neural mitochondrial homeostasis and mitochondria turnover. J Biol Chem 279(20):20699–20707. doi: 10.1074/jbc.M313579200 · DOI
  41. McKinnon C, Goold R, Andre R, Devoy A, Ortega Z, Moonga J, Linehan JM, Brandner S, Lucas JJ, Collinge J, Tabrizi SJ (2016) Prion-mediated neurodegeneration is associated with early impairment of the ubiquitin-proteasome system. Acta Neuropathol 131(3):411–425. doi: 10.1007/s00401-015-1508-y · DOI
  42. Dasgupta S, Fishman MA, Mahallati H, Castro LM, Tashima AK, Ferro ES, Fricker LD (2015) Reduced Levels of Proteasome Products in a Mouse Striatal Cell Model of Huntington’s Disease. PLoS ONE 10(12):e0145333. doi: 10.1371/journal.pone.0145333 · DOI
  43. Lindersson E, Beedholm R, Hojrup P, Moos T, Gai W, Hendil KB, Jensen PH (2004) Proteasomal inhibition by alpha-synuclein filaments and oligomers. J Biol Chem 279(13):12924–12934. doi: 10.1074/jbc.M306390200 · DOI
  44. Zheng Q, Li J, Wang X (2009) Interplay between the ubiquitin-proteasome system and autophagy in proteinopathies. Int J Physiol Pathophysiol Pharmacol 1(2):127–142
  45. Groll M, Ditzel L, Lowe J, Stock D, Bochtler M, Bartunik HD, Huber R (1997) Structure of 20S proteasome from yeast at 2.4 A resolution. Nature 386(6624):463–471. doi: 10.1038/386463a0 · DOI
  46. Jung T, Grune T (2013) The proteasome and the degradation of oxidized proteins: Part I-structure of proteasomes. Redox Biol 1:178–182. doi: 10.1016/j.redox.2013.01.004 · DOI
  47. Groll M, Bochtler M, Brandstetter H, Clausen T, Huber R (2005) Molecular machines for protein degradation. Chem Bio Chem 6(2):222–256. doi: 10.1002/cbic.200400313 · DOI
  48. Seemuller E, Lupas A, Stock D, Lowe J, Huber R, Baumeister W (1995) Proteasome from Thermoplasma acidophilum: a threonine protease. Science 268(5210):579–582 · DOI
  49. Orlowski M, Wilk S (2003) Ubiquitin-independent proteolytic functions of the proteasome. Arch Biochem Biophys 415(1):1–5 · DOI
  50. Shringarpure R, Grune T, Davies KJ (2001) Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells. Cell Mol Life Sci 58(10):1442–1450 · DOI
  51. Ciechanover A, Orian A, Schwartz AL (2000) The ubiquitin-mediated proteolytic pathway: mode of action and clinical implications. J Cell Biochem Suppl 34:40–51 · DOI
  52. Wilkinson KD (2000) Ubiquitination and deubiquitination: targeting of proteins for degradation by the proteasome. Semin Cell Dev Biol 11(3):141–148. doi: 10.1006/scdb.2000.0164 · DOI
  53. Koegl M, Hoppe T, Schlenker S, Ulrich HD, Mayer TU, Jentsch S (1999) A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell 96(5):635–644 · DOI
  54. Thrower JS, Hoffman L, Rechsteiner M, Pickart CM (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J 19(1):94–102. doi: 10.1093/emboj/19.1.94 · DOI
  55. Ciechanover A (1843) Stanhill A (2014) The complexity of recognition of ubiquitinated substrates by the 26S proteasome. Biochim Biophys Acta 1:86–96. doi: 10.1016/j.bbamcr.2013.07.007 · DOI
  56. Haglund K, Sigismund S, Polo S, Szymkiewicz I, Di Fiore PP, Dikic I (2003) Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation. Nat Cell Biol 5(5):461–466. doi: 10.1038/ncb983 · DOI · Paper page
  57. Hicke L (2001) Protein regulation by monoubiquitin. Nat Rev Mol Cell Biol 2(3):195–201. doi: 10.1038/35056583 · DOI
  58. Tenno T, Fujiwara K, Tochio H, Iwai K, Morita EH, Hayashi H, Murata S, Hiroaki H, Sato M, Tanaka K (2004) Shirakawa M (2004) Structural basis for distinct roles of Lys63- and Lys48-linked polyubiquitin chains. Genes Cells 9(11):1137. doi: 10.1111/j.1365-2443.2004.00810.x · DOI
  59. Nathan JA, Kim HT, Ting L, Gygi SP, Goldberg AL (2013) Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes? EMBO J 32(4):552–565. doi: 10.1038/emboj.2012.354 · DOI
  60. Saeki Y, Kudo T, Sone T, Kikuchi Y, Yokosawa H, Toh-e A, Tanaka K (2009) Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome. EMBO J 28(4):359–371. doi: 10.1038/emboj.2008.305 · DOI
  61. Xu P, Duong DM, Seyfried NT, Cheng D, Xie Y, Robert J, Rush J, Hochstrasser M, Finley D, Peng J (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation. Cell 137(1):133–145. doi: 10.1016/j.cell.2009.01.041 · DOI
  62. Benbrook DM, Long A (2012) Integration of autophagy, proteasomal degradation, unfolded protein response and apoptosis. Experimental oncology 34(3):286–297
  63. Kirkin V, Lamark T, Sou YS, Bjorkoy G, Nunn JL, Bruun JA, Shvets E, McEwan DG, Clausen TH, Wild P, Bilusic I, Theurillat JP, Overvatn A, Ishii T, Elazar Z, Komatsu M, Dikic I, Johansen T (2009) A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol Cell 33(4):505–516. doi: 10.1016/j.molcel.2009.01.020 · DOI · Paper page
  64. Olzmann JA, Li L, Chudaev MV, Chen J, Perez FA, Palmiter RD, Chin LS (2007) Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J Cell Biol 178(6):1025–1038. doi: 10.1083/jcb.200611128 · DOI
  65. Li W, Ye Y (2008) Polyubiquitin chains: functions, structures, and mechanisms. Cell Mol Life Sci 65(15):2397–2406. doi: 10.1007/s00018-008-8090-6 · DOI
  66. Spence J, Sadis S, Haas AL, Finley D (1995) A ubiquitin mutant with specific defects in DNA repair and multiubiquitination. Mol Cell Biol 15(3):1265–1273 · DOI
  67. Lauwers E, Jacob C, Andre B (2009) K63-linked ubiquitin chains as a specific signal for protein sorting into the multivesicular body pathway. J Cell Biol 185(3):493–502. doi: 10.1083/jcb.200810114 · DOI
  68. Huang F, Zeng X, Kim W, Balasubramani M, Fortian A, Gygi SP, Yates NA, Sorkin A (2013) Lysine 63-linked polyubiquitination is required for EGF receptor degradation. Proc Natl Acad Sci USA 110(39):15722–15727. doi: 10.1073/pnas.1308014110 · DOI
  69. Sato M, Konuma R, Sato K, Tomura K, Sato K (2014) Fertilization- induced K63-linked ubiquitylation mediates clearance of maternal membrane proteins. Development 141(6):U1268–U1324. doi: 10.1242/dev.103044 · DOI
  70. Fritsch J, Stephan M, Tchikov V, Winoto-Morbach S, Gubkina S, Kabelitz D, Schutze S (2014) Cell fate decisions regulated by K63 ubiquitination of tumor necrosis factor receptor 1. Mol Cell Biol 34(17):3214–3228. doi: 10.1128/MCB.00048-14 · DOI
  71. Tan JM, Wong ES, Kirkpatrick DS, Pletnikova O, Ko HS, Tay SP, Ho MW, Troncoso J, Gygi SP, Lee MK, Dawson VL, Dawson TM, Lim KL (2008) Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases. Hum Mol Genet 17(3):431–439. doi: 10.1093/hmg/ddm320 · DOI
  72. Lim KL, Chew KC, Tan JM, Wang C, Chung KK, Zhang Y, Tanaka Y, Smith W, Engelender S, Ross CA, Dawson VL, Dawson TM (2005) Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation. J Neurosci 25(8):2002–2009. doi: 10.1523/JNEUROSCI.4474-04.2005 · DOI · Paper page
  73. Hong X, Liu J, Zhu G, Zhuang Y, Suo H, Wang P, Huang D, Xu J, Huang Y, Yu M, Bian M, Sheng Z, Fei J, Song H, Behnisch T, Huang F (2014) Parkin overexpression ameliorates hippocampal long-term potentiation and beta-amyloid load in an Alzheimer’s disease mouse model. Hum Mol Genet 23(4):1056–1072. doi: 10.1093/hmg/ddt501 · DOI
  74. Khandelwal PJ, Herman AM, Hoe HS, Rebeck GW, Moussa CE (2011) Parkin mediates beclin-dependent autophagic clearance of defective mitochondria and ubiquitinated Abeta in AD models. Hum Mol Genet 20(11):2091–2102. doi: 10.1093/hmg/ddr091 · DOI
  75. Zhang M, Cai F, Zhang S, Zhang S, Song W (2014) Overexpression of ubiquitin carboxyl-terminal hydrolase L1 (UCHL1) delays Alzheimer’s progression in vivo. Scient Rep 4:7298. doi: 10.1038/srep07298 · DOI
  76. McKeon JE, Sha D, Li L, Chin LS (2015) Parkin-mediated K63-polyubiquitination targets ubiquitin C-terminal hydrolase L1 for degradation by the autophagy-lysosome system. Cell Mol Life Sci 72(9):1811–1824. doi: 10.1007/s00018-014-1781-2 · DOI
  77. Lee KM, Hwang SK, Lee JA (2013) Neuronal autophagy and neurodevelopmental disorders. Exp Neurobiol 22(3):133–142. doi: 10.5607/en.2013.22.3.133 · DOI
  78. Park C, Cuervo AM (2013) Selective autophagy: talking with the UPS. Cell Biochem Biophys 67(1):3–13. doi: 10.1007/s12013-013-9623-7 · DOI
  79. Reggiori F, Komatsu M, Finley K, Simonsen A (2012) Autophagy: more than a nonselective pathway. Int J Cell Biol 2012:219625. doi: 10.1155/2012/219625 · DOI
  80. Mizushima N, Levine B, Cuervo AM, Klionsky DJ (2008) Autophagy fights disease through cellular self-digestion. Nature 451(7182):1069–1075. doi: 10.1038/nature06639 · DOI · Paper page
  81. Wong E, Cuervo AM (2010) Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb Perspect Biol 2(12):a006734. doi: 10.1101/cshperspect.a006734 · DOI
  82. Klionsky DJ, Cregg JM, Dunn WA Jr, Emr SD, Sakai Y, Sandoval IV, Sibirny A, Subramani S, Thumm M, Veenhuis M, Ohsumi Y (2003) A unified nomenclature for yeast autophagy-related genes. Dev Cell 5(4):539–545 · DOI
  83. Nixon RA (2013) The role of autophagy in neurodegenerative disease. Nat Med 19(8):983–997. doi: 10.1038/nm.3232 · DOI · Paper page
  84. Wong AS, Cheung ZH (1812) Ip NY (2011) Molecular machinery of macroautophagy and its deregulation in diseases. Biochim Biophys Acta 11:1490–1497. doi: 10.1016/j.bbadis.2011.07.005 · DOI
  85. Williams RS, Cheng L, Mudge AW, Harwood AJ (2002) A common mechanism of action for three mood-stabilizing drugs. Nature 417(6886):292–295. doi: 10.1038/417292a · DOI
  86. Sarkar S, Floto RA, Berger Z, Imarisio S, Cordenier A, Pasco M, Cook LJ, Rubinsztein DC (2005) Lithium induces autophagy by inhibiting inositol monophosphatase. J Cell Biol 170(7):1101–1111. doi: 10.1083/jcb.200504035 · DOI · Paper page
  87. Sarkar S, Ravikumar B, Floto RA, Rubinsztein DC (2009) Rapamycin and mTOR-independent autophagy inducers ameliorate toxicity of polyglutamine-expanded huntingtin and related proteinopathies. Cell Death Differ 16(1):46–56. doi: 10.1038/cdd.2008.110 · DOI · Paper page
  88. Hyttinen JM, Amadio M, Viiri J, Pascale A, Salminen A, Kaarniranta K (2014) Clearance of misfolded and aggregated proteins by aggrephagy and implications for aggregation diseases. Ageing Res Rev 18:16–28. doi: 10.1016/j.arr.2014.07.002 · DOI
  89. Lamark T, Johansen T (2012) Aggrephagy: selective disposal of protein aggregates by macroautophagy. Int J Cell Biol 2012:736905. doi: 10.1155/2012/736905 · DOI
  90. Chiang HL, Terlecky SR, Plant CP, Dice JF (1989) A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science 246(4928):382–385 · DOI
  91. Agarraberes FA, Dice JF (2001) A molecular chaperone complex at the lysosomal membrane is required for protein translocation. J Cell Sci 114(Pt 13):2491–2499 · DOI
  92. Kon M, Cuervo AM (2010) Chaperone-mediated autophagy in health and disease. FEBS Lett 584(7):1399–1404. doi: 10.1016/j.febslet.2009.12.025 · DOI
  93. Cuervo AM, Wong E (2014) Chaperone-mediated autophagy: roles in disease and aging. Cell Res 24(1):92–104. doi: 10.1038/cr.2013.153 · DOI
  94. Bandyopadhyay U, Kaushik S, Varticovski L, Cuervo AM (2008) The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 28(18):5747–5763. doi: 10.1128/MCB.02070-07 · DOI
  95. Kaushik S, Massey AC, Mizushima N, Cuervo AM (2008) Constitutive activation of chaperone-mediated autophagy in cells with impaired macroautophagy. Mol Biol Cell 19(5):2179–2192. doi: 10.1091/mbc.E07-11-1155 · DOI
  96. Marzella L, Ahlberg J, Glaumann H (1981) Autophagy, heterophagy, microautophagy and crinophagy as the means for intracellular degradation. Virchows Archiv B, Cell pathology including molecular pathology 36(2–3):219–234 · DOI
  97. Li WW, Li J, Bao JK (2012) Microautophagy: lesser-known self-eating. Cell Mol Life Sci 69(7):1125–1136. doi: 10.1007/s00018-011-0865-5 · DOI
  98. Mijaljica D, Prescott M, Devenish RJ (2011) Microautophagy in mammalian cells: revisiting a 40-year-old conundrum. Autophagy 7(7):673–682 · DOI
  99. Todde V, Veenhuis M, van der Klei IJ (2009) Autophagy: principles and significance in health and disease. Biochim Biophys Acta 1792(1):3–13. doi: 10.1016/j.bbadis.2008.10.016 · DOI
  100. Sahu R, Kaushik S, Clement CC, Cannizzo ES, Scharf B, Follenzi A, Potolicchio I, Nieves E, Cuervo AM, Santambrogio L (2011) Microautophagy of cytosolic proteins by late endosomes. Dev Cell 20(1):131–139. doi: 10.1016/j.devcel.2010.12.003 · DOI · Paper page
  101. Santambrogio L, Nosotti M, Palleschi A, Gazzano G, De Simone M, Cioffi U (2011) Primary pulmonary glomangioma: a coin lesion negative on PET study. Case report and literature review. Thorac Cardiovasc Surg 59(6):380–382. doi: 10.1055/s-0030-1250577 · DOI
  102. Lopez Salon M, Pasquini L, Besio Moreno M, Pasquini JM, Soto E (2003) Relationship between beta-amyloid degradation and the 26S proteasome in neural cells. Exp Neurol 180(2):131–143 · DOI
  103. Cecarini V, Bonfili L, Amici M, Angeletti M, Keller JN, Eleuteri AM (2008) Amyloid peptides in different assembly states and related effects on isolated and cellular proteasomes. Brain Res 1209:8–18. doi: 10.1016/j.brainres.2008.03.003 · DOI
  104. Tseng BP, Green KN, Chan JL, Blurton-Jones M, LaFerla FM (2008) Abeta inhibits the proteasome and enhances amyloid and tau accumulation. Neurobiol Aging 29(11):1607–1618. doi: 10.1016/j.neurobiolaging.2007.04.014 · DOI · Paper page
  105. Umeda T, Tomiyama T, Sakama N, Tanaka S, Lambert MP, Klein WL, Mori H (2011) Intraneuronal amyloid beta oligomers cause cell death via endoplasmic reticulum stress, endosomal/lysosomal leakage, and mitochondrial dysfunction in vivo. J Neurosci Res 89(7):1031–1042. doi: 10.1002/jnr.22640 · DOI
  106. Chu J, Li JG, Hoffman NE, Madesh M, Pratico D (2015) Degradation of gamma secretase activating protein by the ubiquitin-proteasome pathway. J Neurochem 133(3):432–439. doi: 10.1111/jnc.13011 · DOI
  107. Dehvari N, Mahmud T, Persson J, Bengtsson T, Graff C, Winblad B, Ronnback A, Behbahani H (2012) Amyloid precursor protein accumulates in aggresomes in response to proteasome inhibitor. Neurochem Int 60(5):533–542. doi: 10.1016/j.neuint.2012.02.012 · DOI
  108. El Ayadi A, Stieren ES, Barral JM, Boehning D (2012) Ubiquilin-1 regulates amyloid precursor protein maturation and degradation by stimulating K63-linked polyubiquitination of lysine 688. Proc Natl Acad Sci USA 109(33):13416–13421. doi: 10.1073/pnas.1206786109 · DOI
  109. Wang H, Saunders AJ (2014) The role of ubiquitin-proteasome in the metabolism of amyloid precursor protein (APP): implications for novel therapeutic strategies for Alzheimer’s disease. Dis Med 18(97):41–50
  110. Brown MR, Bondada V, Keller JN, Thorpe J, Geddes JW (2005) Proteasome or calpain inhibition does not alter cellular tau levels in neuroblastoma cells or primary neurons. J Alzheimer’s Dis JAD 7(1):15–24 · DOI
  111. Delobel P, Leroy O, Hamdane M, Sambo AV, Delacourte A, Buee L (2005) Proteasome inhibition and Tau proteolysis: an unexpected regulation. FEBS Lett 579(1):1–5. doi: 10.1016/j.febslet.2004.11.018 · DOI
  112. Ren QG, Liao XM, Wang ZF, Qu ZS, Wang JZ (2006) The involvement of glycogen synthase kinase-3 and protein phosphatase-2A in lactacystin-induced tau accumulation. FEBS Lett 580(10):2503–2511. doi: 10.1016/j.febslet.2006.03.073 · DOI
  113. Liu YH, Wei W, Yin J, Liu GP, Wang Q, Cao FY, Wang JZ (2009) Proteasome inhibition increases tau accumulation independent of phosphorylation. Neurobiol Aging 30(12):1949–1961. doi: 10.1016/j.neurobiolaging.2008.02.012 · DOI
  114. Zhang JY, Liu SJ, Li HL, Wang JZ (2005) Microtubule-associated protein tau is a substrate of ATP/Mg(2+)-dependent proteasome protease system. J Neural Trans 112(4):547–555. doi: 10.1007/s00702-004-0196-x · DOI
  115. David DC, Layfield R, Serpell L, Narain Y, Goedert M, Spillantini MG (2002) Proteasomal degradation of tau protein. J Neurochem 83(1):176–185 · DOI · Paper page
  116. van Tijn P, de Vrij FM, Schuurman KG, Dantuma NP, Fischer DF, van Leeuwen FW, Hol EM (2007) Dose-dependent inhibition of proteasome activity by a mutant ubiquitin associated with neurodegenerative disease. J Cell Sci 120(Pt 9):1615–1623. doi: 10.1242/jcs.03438 · DOI
  117. Irmler M, Gentier RJ, Dennissen FJ, Schulz H, Bolle I, Holter SM, Kallnik M, Cheng JJ, Klingenspor M, Rozman J, Ehrhardt N, Hermes DJ, Gailus-Durner V, Fuchs H, Hrabe de Angelis M, Meyer HE, Hopkins DA, Van Leeuwen FW, Beckers J (2012) 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. Acta Neuropathol 124(2):187–197. doi: 10.1007/s00401-012-1003-7 · DOI
  118. Bilguvar K, Tyagi NK, Ozkara C, Tuysuz B, Bakircioglu M, Choi M, Delil S, Caglayan AO, Baranoski JF, Erturk O, Yalcinkaya C, Karacorlu M, Dincer A, Johnson MH, Mane S, Chandra SS, Louvi A, Boggon TJ, Lifton RP, Horwich AL, Gunel M (2013) Recessive loss of function of the neuronal ubiquitin hydrolase UCHL1 leads to early-onset progressive neurodegeneration. Proc Natl Acad Sci USA 110(9):3489–3494. doi: 10.1073/pnas.1222732110 · DOI
  119. Dasuri K, Ebenezer P, Zhang L, Fernandez-Kim SO, Bruce-Keller AJ, Markesbery WR, Keller JN (2010) Increased protein hydrophobicity in response to aging and Alzheimer disease. Free Radic Biol Med 48(10):1330–1337. doi: 10.1016/j.freeradbiomed.2010.02.012 · DOI
  120. Petropoulos I, Conconi M, Wang X, Hoenel B, Bregegere F, Milner Y, Friguet B (2000) Increase of oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells. J Gerontol Series A Biol Sci Med Sci 55(5):B220–B227 · DOI
  121. Castegna A, Aksenov M, Aksenova M, Thongboonkerd V, Klein JB, Pierce WM, Booze R, Markesbery WR, Butterfield DA (2002) Proteomic identification of oxidatively modified proteins in Alzheimer’s disease brain. Part I: creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1. Free Radic Biol Med 33(4):562–571 · DOI · Paper page
  122. Swomley AM, Butterfield DA (2015) Oxidative stress in Alzheimer disease and mild cognitive impairment: evidence from human data provided by redox proteomics. Arch Toxicol 89(10):1669–1680. doi: 10.1007/s00204-015-1556-z · DOI
  123. Yang DS, Stavrides P, Mohan PS, Kaushik S, Kumar A, Ohno M, Schmidt SD, Wesson D, Bandyopadhyay U, Jiang Y, Pawlik M, Peterhoff CM, Yang AJ, Wilson DA, St George-Hyslop P, Westaway D, Mathews PM, Levy E, Cuervo AM, Nixon RA (2011) Reversal of autophagy dysfunction in the TgCRND8 mouse model of Alzheimer’s disease ameliorates amyloid pathologies and memory deficits. Brain J Neurol 134(Pt 1):258–277. doi: 10.1093/brain/awq341 · DOI · Paper page
  124. Jaeger PA, Pickford F, Sun CH, Lucin KM, Masliah E, Wyss-Coray T (2010) Regulation of amyloid precursor protein processing by the Beclin 1 complex. PLoS One 5(6):e11102. doi: 10.1371/journal.pone.0011102 · DOI
  125. Hamano T, Gendron TF, Causevic E, Yen SH, Lin WL, Isidoro C, Deture M, Ko LW (2008) Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression. Euro J Neurosci 27(5):1119–1130. doi: 10.1111/j.1460-9568.2008.06084.x · DOI · Paper page
  126. Bednarski E, Lynch G (1996) Cytosolic proteolysis of tau by cathepsin D in hippocampus following suppression of cathepsins B and L. J Neurochem 67(5):1846–1855 · DOI
  127. Nixon RA, Wegiel J, Kumar A, Yu WH, Peterhoff C, Cataldo A, Cuervo AM (2005) Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study. J Neuropathol Exp Neurol 64(2):113–122 · DOI · Paper page
  128. Lee S, Sato Y, Nixon RA (2011) Lysosomal proteolysis inhibition selectively disrupts axonal transport of degradative organelles and causes an Alzheimer’s-like axonal dystrophy. J Neurosci 31(21):7817–7830. doi: 10.1523/JNEUROSCI.6412-10.2011 · DOI
  129. Lee JH, Yu WH, Kumar A, Lee S, Mohan PS, Peterhoff CM, Wolfe DM, Martinez-Vicente M, Massey AC, Sovak G, Uchiyama Y, Westaway D, Cuervo AM, Nixon RA (2010) Lysosomal proteolysis and autophagy require presenilin 1 and are disrupted by Alzheimer-related PS1 mutations. Cell 141(7):1146–1158. doi: 10.1016/j.cell.2010.05.008 · DOI · Paper page
  130. Yu WH, Cuervo AM, Kumar A, Peterhoff CM, Schmidt SD, Lee JH, Mohan PS, Mercken M, Farmery MR, Tjernberg LO, Jiang Y, Duff K, Uchiyama Y, Naslund J, Mathews PM, Cataldo AM, Nixon RA (2005) Macroautophagy–a novel Beta-amyloid peptide-generating pathway activated in Alzheimer’s disease. J Cell Biol 171(1):87–98. doi: 10.1083/jcb.200505082 · DOI · Paper page
  131. Martin-Maestro P, Gargini R, Perry G, Avila J, Garcia-Escudero V (2016) PARK2 enhancement is able to compensate mitophagy alterations found in sporadic Alzheimer’s disease. Hum Mol Genet 25(4):792–806. doi: 10.1093/hmg/ddv616 · DOI · Paper page
  132. Liu H, Wang P, Song W, Sun X (2009) Degradation of regulator of calcineurin 1 (RCAN1) is mediated by both chaperone-mediated autophagy and ubiquitin proteasome pathways. FASEB J Off Publ Feder Am Soc Exp Biol 23(10):3383–3392. doi: 10.1096/fj.09-134296 · DOI
  133. Di Domenico F, Coccia R, Cocciolo A, Murphy MP, Cenini G, Head E, Butterfield DA, Giorgi A, Schinina ME, Mancuso C, Cini C (1832) Perluigi M (2013) Impairment of proteostasis network in Down syndrome prior to the development of Alzheimer’s disease neuropathology: redox proteomics analysis of human brain. Biochim Biophys Acta 8:1249–1259. doi: 10.1016/j.bbadis.2013.04.013 · DOI
  134. Di Domenico F, Pupo G, Tramutola A, Giorgi A, Schinina ME, Coccia R, Head E, Butterfield DA, Perluigi M (2014) Redox proteomics analysis of HNE-modified proteins in Down syndrome brain: clues for understanding the development of Alzheimer disease. Free Radic Biol Med 71:270–280. doi: 10.1016/j.freeradbiomed.2014.03.027 · DOI
  135. Kraft C, Peter M, Hofmann K (2010) Selective autophagy: ubiquitin-mediated recognition and beyond. Nat Cell Biol 12(9):836–841. doi: 10.1038/ncb0910-836 · DOI · Paper page
  136. Fuertes G, Villarroya A, Knecht E (2003) Role of proteasomes in the degradation of short-lived proteins in human fibroblasts under various growth conditions. Int J Biochem Cell Biol 35(5):651–664 · DOI
  137. Fuertes G, Martin De Llano JJ, Villarroya A, Rivett AJ, Knecht E (2003) Changes in the proteolytic activities of proteasomes and lysosomes in human fibroblasts produced by serum withdrawal, amino-acid deprivation and confluent conditions. Biochem J 375(Pt 1):75–86. doi: 10.1042/BJ20030282 · DOI · Paper page
  138. van Tijn P, Dennissen FJ, Gentier RJ, Hobo B, Hermes D, Steinbusch HW, Van Leeuwen FW, Fischer DF (2012) Mutant ubiquitin decreases amyloid beta plaque formation in a transgenic mouse model of Alzheimer’s disease. Neurochem Int 61(5):739–748. doi: 10.1016/j.neuint.2012.07.007 · DOI · Paper page
  139. Ding WX, Ni HM, Gao W, Yoshimori T, Stolz DB, Ron D, Yin XM (2007) Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 171(2):513–524. doi: 10.2353/ajpath.2007.070188 · DOI · Paper page
  140. Pandey UB, Batlevi Y, Baehrecke EH, Taylor JP (2007) HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration. Autophagy 3(6):643–645 · DOI
  141. Cecarini V, Bonfili L, Cuccioloni M, Mozzicafreddo M, Rossi G, Buizza L, Uberti D, Angeletti M (1822) Eleuteri AM (2012) Crosstalk between the ubiquitin-proteasome system and autophagy in a human cellular model of Alzheimer’s disease. Biochim Biophys Acta 11:1741–1751. doi: 10.1016/j.bbadis.2012.07.015 · DOI
  142. Cecarini V, Bonfili L, Cuccioloni M, Mozzicafreddo M, Rossi G, Keller JN, Angeletti M (1842) Eleuteri AM (2014) Wild type and mutant amyloid precursor proteins influence downstream effects of proteasome and autophagy inhibition. Biochim Biophys Acta 2:127–134. doi: 10.1016/j.bbadis.2013.11.002 · DOI
  143. Cecarini V, Bonfili L, Cuccioloni M, Keller JN, Bruce-Keller AJ, Eleuteri AM (2015) Effects of Ghrelin on the Proteolytic Pathways of Alzheimer’s Disease Neuronal Cells. Mol Neurobiol. doi: 10.1007/s12035-015-9227-x · DOI
  144. Rideout HJ, Lang-Rollin I, Stefanis L (2004) Involvement of macroautophagy in the dissolution of neuronal inclusions. Int J Biochem Cell Biol 36(12):2551–2562. doi: 10.1016/j.biocel.2004.05.008 · DOI
  145. Johansen T, Lamark T (2011) Selective autophagy mediated by autophagic adapter proteins. Autophagy 7(3):279–296 · DOI
  146. Kuusisto E, Salminen A, Alafuzoff I (2001) Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies. Neuro Report 12(10):2085–2090
  147. Nagaoka U, Kim K, Jana NR (2004) Doi H, Maruyama M, Mitsui K, Oyama F, Nukina N Increased expression of p62 in expanded polyglutamine-expressing cells and its association with polyglutamine inclusions. J Neurochem 91(1):57–68. doi: 10.1111/j.1471-4159.2004.02692.x · DOI
  148. Salminen A, Kaarniranta K, Haapasalo A, Hiltunen M, Soininen H, Alafuzoff I (2012) Emerging role of p62/sequestosome-1 in the pathogenesis of Alzheimer’s disease. Prog Neurobiol 96(1):87–95. doi: 10.1016/j.pneurobio.2011.11.005 · DOI · Paper page
  149. Kirkin V, McEwan DG, Novak I, Dikic I (2009) A role for ubiquitin in selective autophagy. Mol Cell 34(3):259–269. doi: 10.1016/j.molcel.2009.04.026 · DOI
  150. Seibenhener ML, Babu JR, Geetha T, Wong HC, Krishna NR, Wooten MW (2004) Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol Cell Biol 24(18):8055–8068. doi: 10.1128/MCB.24.18.8055-8068.2004 · DOI
  151. Babu JR, Geetha T, Wooten MW (2005) Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation. J Neurochem 94(1):192–203. doi: 10.1111/j.1471-4159.2005.03181.x · DOI · Paper page
  152. Ramesh Babu J, Lamar Seibenhener M, Peng J, Strom AL, Kemppainen R, Cox N, Zhu H, Wooten MC, Diaz-Meco MT, Moscat J, Wooten MW (2008) Genetic inactivation of p62 leads to accumulation of hyperphosphorylated tau and neurodegeneration. J Neurochem 106(1):107–120. doi: 10.1111/j.1471-4159.2008.05340.x · DOI · Paper page
  153. Kuusisto E, Salminen A, Alafuzoff I (2002) Early accumulation of p62 in neurofibrillary tangles in Alzheimer’s disease: possible role in tangle formation. Neuropathol Appl Neurobiol 28(3):228–237 · DOI
  154. Komatsu M, Waguri S, Koike M, Sou YS, Ueno T, Hara T, Mizushima N, Iwata J, Ezaki J, Murata S, Hamazaki J, Nishito Y, Iemura S, Natsume T, Yanagawa T, Uwayama J, Warabi E, Yoshida H, Ishii T, Kobayashi A, Yamamoto M, Yue Z, Uchiyama Y, Kominami E, Tanaka K (2007) Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 131(6):1149–1163. doi: 10.1016/j.cell.2007.10.035 · DOI · Paper page
  155. Campbell IG, Nicolai HM, Foulkes WD, Senger G, Stamp GW, Allan G, Boyer C, Jones K, Bast RC Jr, Solomon E (1994) A novel gene encoding a B-box protein within the BRCA1 region at 17q21.1. Hum Mol Genet 3(4):589–594 · DOI
  156. Lamark T, Kirkin V, Dikic I, Johansen T (2009) NBR1 and p62 as cargo receptors for selective autophagy of ubiquitinated targets. Cell Cycle 8(13):1986–1990 · DOI · Paper page
  157. Liu YH, Tian T (2011) Hypothesis of optineurin as a new common risk factor in normal-tension glaucoma and Alzheimer’s disease. Med Hypotheses 77(4):591–592. doi: 10.1016/j.mehy.2011.06.040 · DOI
  158. Ying H, Yue BY (2015) Optineurin: The autophagy connection. Exp Eye Res. doi: 10.1016/j.exer.2015.06.029 · DOI
  159. Shen X, Ying H, Qiu Y, Park JS, Shyam R, Chi ZL, Iwata T, Yue BY (2011) Processing of optineurin in neuronal cells. J Biol Chem 286(5):3618–3629. doi: 10.1074/jbc.M110.175810 · DOI
  160. Osawa T, Mizuno Y, Fujita Y, Takatama M, Nakazato Y, Okamoto K (2011) Optineurin in neurodegenerative diseases. Neuropathol Off J Japn Soc Neuropathol 31(6):569–574. doi: 10.1111/j.1440-1789.2011.01199.x · DOI
  161. Kim S, Lee D, Song JC, Cho SJ, Yun SM, Koh YH, Song J, Johnson GV, Jo C (2014) NDP52 associates with phosphorylated tau in brains of an Alzheimer disease mouse model. Biochem Biophys Res Commun 454(1):196–201. doi: 10.1016/j.bbrc.2014.10.066 · DOI
  162. Thurston TL, Ryzhakov G, Bloor S, von Muhlinen N, Randow F (2009) The TBK1 adaptor and autophagy receptor NDP52 restricts the proliferation of ubiquitin-coated bacteria. Nat Immunol 10(11):1215–1221. doi: 10.1038/ni.1800 · DOI
  163. Jo C, Gundemir S, Pritchard S, Jin YN, Rahman I, Johnson GV (2014) Nrf2 reduces levels of phosphorylated tau protein by inducing autophagy adaptor protein NDP52. Nat Commun 5:3496. doi: 10.1038/ncomms4496 · DOI · Paper page
  164. Kawaguchi Y, Kovacs JJ, McLaurin A, Vance JM, Ito A, Yao TP (2003) The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress. Cell 115(6):727–738 · DOI
  165. Leyk J, Goldbaum O, Noack M, Richter-Landsberg C (2015) Inhibition of HDAC6 modifies tau inclusion body formation and impairs autophagic clearance. J Molecul Neurosci MN 55(4):1031–1046. doi: 10.1007/s12031-014-0460-y · DOI
  166. Yan J, Seibenhener ML, Calderilla-Barbosa L, Diaz-Meco MT, Moscat J, Jiang J, Wooten MW, Wooten MC (2013) SQSTM1/p62 interacts with HDAC6 and regulates deacetylase activity. PLoS One 8(9):e76016. doi: 10.1371/journal.pone.0076016 · DOI
  167. Perez M, Santa-Maria I, Gomez de Barreda E, Zhu X, Cuadros R, Cabrero JR, Sanchez-Madrid F, Dawson HN, Vitek MP, Perry G, Smith MA, Avila J (2009) Tau–an inhibitor of deacetylase HDAC6 function. J Neurochem 109(6):1756–1766. doi: 10.1111/j.1471-4159.2009.06102.x · DOI · Paper page
  168. Yang FC, Lin YH, Chen WH, Huang JY, Chang HY, Su SH, Wang HT, Chiang CY, Hsu PH, Tsai MD, Tan BC, Lee SC (2013) Interaction between salt-inducible kinase 2 (SIK2) and p97/valosin-containing protein (VCP) regulates endoplasmic reticulum (ER)-associated protein degradation in mammalian cells. J Biol Chem 288(47):33861–33872. doi: 10.1074/jbc.M113.492199 · DOI
  169. Uchiyama K, Kondo H (2005) p97/p47-Mediated biogenesis of Golgi and ER. J Biochem 137(2):115–119. doi: 10.1093/jb/mvi028 · DOI
  170. Yamanaka K, Sasagawa Y (1823) Ogura T (2012) Recent advances in p97/VCP/Cdc48 cellular functions. Biochim Biophys Acta 1:130–137. doi: 10.1016/j.bbamcr.2011.07.001 · DOI
  171. Rabinovich E, Kerem A, Frohlich KU, Diamant N, Bar-Nun S (2002) AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 22(2):626–634 · DOI
  172. Mori-Konya C, Kato N, Maeda R, Yasuda K, Higashimae N, Noguchi M, Koike M, Kimura Y, Ohizumi H, Hori S, Kakizuka A (2009) p97/valosin-containing protein (VCP) is highly modulated by phosphorylation and acetylation. Genes Cells Devoted Molecul Cell Mechan 14(4):483–497. doi: 10.1111/j.1365-2443.2009.01286.x · DOI
  173. Dargemont C, Ossareh-Nazari B (2012) Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways. Biochim Biophys Acta 1823(1):138–144. doi: 10.1016/j.bbamcr.2011.07.011 · DOI
  174. Boyault C, Gilquin B, Zhang Y, Rybin V, Garman E, Meyer-Klaucke W, Matthias P, Muller CW, Khochbin S (2006) HDAC6-p97/VCP controlled polyubiquitin chain turnover. EMBO J 25(14):3357–3366. doi: 10.1038/sj.emboj.7601210 · DOI
  175. Halawani D, Tessier S, Anzellotti D, Bennett DA, Latterich M, LeBlanc AC (2010) Identification of Caspase-6-mediated processing of the valosin containing protein (p97) in Alzheimer’s disease: a novel link to dysfunction in ubiquitin proteasome system-mediated protein degradation. J Neurosci 30(17):6132–6142. doi: 10.1523/JNEUROSCI.5874-09.2010 · DOI
  176. Isakson P, Holland P, Simonsen A (2013) The role of ALFY in selective autophagy. Cell Death Differ 20(1):12–20. doi: 10.1038/cdd.2012.66 · DOI
  177. Simonsen A, Birkeland HC, Gillooly DJ, Mizushima N, Kuma A, Yoshimori T, Slagsvold T, Brech A, Stenmark H (2004) Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes. J Cell Sci 117(Pt 18):4239–4251. doi: 10.1242/jcs.01287 · DOI
  178. Clausen TH, Lamark T, Isakson P, Finley K, Larsen KB, Brech A, Overvatn A, Stenmark H, Bjorkoy G, Simonsen A, Johansen T (2010) p62/SQSTM1 and ALFY interact to facilitate the formation of p62 bodies/ALIS and their degradation by autophagy. Autophagy 6(3):330–344 · DOI
  179. Finley KD, Edeen PT, Cumming RC, Mardahl-Dumesnil MD, Taylor BJ, Rodriguez MH, Hwang CE, Benedetti M, McKeown M (2003) Blue cheese mutations define a novel, conserved gene involved in progressive neural degeneration. J Neurosci 23(4):1254–1264 · DOI
  180. Elliott E, Tsvetkov P, Ginzburg I (2007) BAG-1 associates with Hsc70.Tau complex and regulates the proteasomal degradation of Tau protein. J Biol Chem 282(51):37276–37284. doi: 10.1074/jbc.M706379200 · DOI
  181. Elliott E, Laufer O, Ginzburg I (2009) BAG-1M is up-regulated in hippocampus of Alzheimer’s disease patients and associates with tau and APP proteins. J Neurochem 109(4):1168–1178. doi: 10.1111/j.1471-4159.2009.06047.x · DOI
  182. Lei ZN, Brizzee C, Johnson GVW (2015) BAG3 facilitates the clearance of endogenous tau in primary neurons. Neurobiol Aging 36(1):241–248. doi: 10.1016/j.neurobiolaging.2014.08.012 · DOI
  183. Paine MG, Babu JR, Seibenhener ML, Wooten MW (2005) Evidence for p62 aggregate formation: role in cell survival. FEBS Lett 579(22):5029–5034. doi: 10.1016/j.febslet.2005.08.010 · DOI

Cited by

Sorted by citations

See all 21

Metadata

Authors
Cecarini, V., Bonfili, L., Cuccioloni, M., Mozzicafreddo, M., Angeletti, M., Keller, J. N., & Eleuteri, A. M.
Venue
Cellular and Molecular Life Sciences
Published
2016-04-27
Volume
73
Issue
18
Pages
3433-3451
ISSN
  • 1420-682X
  • 1420-9071
Cited by
21
References
19
Language
en

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