{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T13:31:03Z","timestamp":1791207063511,"version":"4.1.0"},"reference-count":50,"publisher":"Oxford University Press (OUP)","issue":"16","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2005,8,15]]},"DOI":"10.1093\/hmg\/ddi236","type":"journal-article","created":{"date-parts":[[2005,7,7]],"date-time":"2005-07-07T00:13:55Z","timestamp":1120695235000},"page":"2335-2347","source":"Crossref","is-referenced-by-count":110,"title":["Somatodendritic accumulation of misfolded SOD1-L126Z in motor neurons mediates degeneration: \u03b1B-crystallin modulates aggregation"],"prefix":"10.1093","volume":"14","author":[{"given":"Jiou","family":"Wang","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Guilian","family":"Xu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hong","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Victoria","family":"Gonzales","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Fromholt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Celeste","family":"Karch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Neal G.","family":"Copeland","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nancy A.","family":"Jenkins","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David R.","family":"Borchelt","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2005,7,13]]},"reference":[{"key":"key\n\t\t\t\t20171012153241_DDI236C1","doi-asserted-by":"crossref","unstructured":"Gurney, M.E., Pu, H., Chiu, A.Y., Dal Canto, M.C., Polchow, C.Y., Alexander, D.D., Caliendo, J., Hentati, A., Kwon, Y.W., Deng, H.-X. et\u00a0al. (1994) Motor neuron degeneration in mice that express a human Cu, Zn superoxide dismutase mutation. Science, 264, 1772\u20131775.","DOI":"10.1126\/science.8209258"},{"key":"key\n\t\t\t\t20171012153241_DDI236C2","doi-asserted-by":"crossref","unstructured":"Borchelt, D.R., Lee, M.K., Slunt, H.H., Guarnieri, M., Xu, Z.-S., Wong, P.C., Brown, R.H., Jr., Price, D.L., Sisodia, S.S. and Cleveland, D.W. (1994) Superoxide dismutase 1 with mutations linked to familial amyotrophic lateral sclerosis possesses significant activity. Proc. Natl. Acad. Sci. USA, 91, 8292\u20138296.","DOI":"10.1073\/pnas.91.17.8292"},{"key":"key\n\t\t\t\t20171012153241_DDI236C3","doi-asserted-by":"crossref","unstructured":"Borchelt, D.R., Guarnieri, M., Wong, P.C., Lee, M.K., Slunt, H.S., Xu, Z.-S., Sisodia, S.S., Price, D.L. and Cleveland, D.W. (1995) Superoxide dismutase 1 subunits with mutations linked to familial amyotrophic lateral sclerosis do not affect wild-type subunit function. J. Biol. Chem., 270, 3234\u20133238.","DOI":"10.1074\/jbc.270.7.3234"},{"key":"key\n\t\t\t\t20171012153241_DDI236C4","doi-asserted-by":"crossref","unstructured":"Wong, P.C., Pardo, C.A., Borchelt, D.R., Lee, M.K., Copeland, N.G., Jenkins, N.A., Sisodia, S.S., Cleveland, D.W., Price, D.L. (1995) An adverse property of a familial ALS-linked SOD1 mutation causes motor neuron disease characterized by vacuolar degeneration of mitochondria. Neuron, 14, 1105\u20131116.","DOI":"10.1016\/0896-6273(95)90259-7"},{"key":"key\n\t\t\t\t20171012153241_DDI236C5","doi-asserted-by":"crossref","unstructured":"Reaume, A.G., Elliott, J.L., Hoffman, E.K., Kowall, N.W., Ferrante, R.J., Siwek, D.F., Wilcox, H.M., Flood, D.G., Beal, M.F., Brown, R.H., Jr. et\u00a0al. (1996) Motor neurons in Cu\/Zn superoxide dismutase-deficient mice develop normally but exhibit enhanced cell death after axonal injury. Nat. Genet., 13, 43\u201347.","DOI":"10.1038\/ng0596-43"},{"key":"key\n\t\t\t\t20171012153241_DDI236C6","doi-asserted-by":"crossref","unstructured":"Bruijn, L.I., Houseweart, M.K., Kato, S., Anderson, K.L., Anderson, S.D., Ohama, E., Reaume, A.G., Scott, R.W. and Cleveland, D.W. (1998) Aggregation and motor neuron toxicity of an ALS-linked SOD1 mutant independent from wild-type SOD1. Science, 281, 1851\u20131854.","DOI":"10.1126\/science.281.5384.1851"},{"key":"key\n\t\t\t\t20171012153241_DDI236C7","doi-asserted-by":"crossref","unstructured":"Ratovitski, T., Corson, L.B., Strain, J., Wong, P., Cleveland, D.W., Culotta, V.C. and Borchelt, D.R. (1999) Variation in the biochemical\/biophysical properties of mutant superoxide dismutase 1 enzymes and the rate of disease progression in familial amyotrophic lateral sclerosis kindreds. Hum. Mol. Genet., 8, 1451\u20131460.","DOI":"10.1093\/hmg\/8.8.1451"},{"key":"key\n\t\t\t\t20171012153241_DDI236C8","doi-asserted-by":"crossref","unstructured":"Valentine, J.S. and Hart, P.J. (2003) Misfolded CuZnSOD and amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA, 100, 3617\u20133622.","DOI":"10.1073\/pnas.0730423100"},{"key":"key\n\t\t\t\t20171012153241_DDI236C9","doi-asserted-by":"crossref","unstructured":"Yim, H.S., Kang, J.H., Chock, P.B., Stadtman, E.R. and Yim, M.B. (1997) A familial amyotrophic lateral sclerosis-associated A4V Cu, Zn-superoxide dismutase mutant has a lower Km for hydrogen peroxide. Correlation between clinical severity and the Km value. J. Biol. Chem., 272, 8861\u20138863.","DOI":"10.1074\/jbc.272.14.8861"},{"key":"key\n\t\t\t\t20171012153241_DDI236C10","doi-asserted-by":"crossref","unstructured":"Yim, M.B., Chock, P.B. and Stadtman, E.R. (1990) Copper, zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide. Proc. Natl. Acad. Sci. USA, 87, 5006\u20135010.","DOI":"10.1073\/pnas.87.13.5006"},{"key":"key\n\t\t\t\t20171012153241_DDI236C11","unstructured":"Yim, M.B., Chock, P.B. and Stadtman, E.R. (1993) Enzyme function of copper, zinc superoxide dismutase as a free radical generator. J. Biol. Chem., 268, 4099\u20134105."},{"key":"key\n\t\t\t\t20171012153241_DDI236C12","doi-asserted-by":"crossref","unstructured":"Yim, M.B., Kang, J.H., Yim, H.S., Kwak, H.S., Chock, P.B. and Stadtman, E.R. (1996) A gain-of-function of an amyotrophic lateral sclerosis-associated Cu, Zn-superoxide dismutase mutant: an enhancement of free radical formation due to a decrease in Km for hydrogen peroxide. Proc. Natl. Acad. Sci. USA, 93, 5709\u20135714.","DOI":"10.1073\/pnas.93.12.5709"},{"key":"key\n\t\t\t\t20171012153241_DDI236C13","doi-asserted-by":"crossref","unstructured":"Beckman, J.S., Carson, M., Smith, C.D. and Koppenol, W.H. (1993) ALS, SOD and peroxynitrite. Nature, 364, 584.","DOI":"10.1038\/364584a0"},{"key":"key\n\t\t\t\t20171012153241_DDI236C14","doi-asserted-by":"crossref","unstructured":"Crow, J.P., Ye, Y.Z., Strong, M., Kirk, M., Barnes, S. and Beckman, J.S. (1997) Superoxide dismutase catalyzes nitration of tyrosines by peroxynitrite in the rod and head domains of neurofilament-L. J. Neurochem., 69, 1945\u20131953.","DOI":"10.1046\/j.1471-4159.1997.69051945.x"},{"key":"key\n\t\t\t\t20171012153241_DDI236C15","doi-asserted-by":"crossref","unstructured":"Est\u00e9vez, A.G., Crow, J.P., Sampson, J.B., Reiter, C., Zhuang, Y., Richardson, G.J., Tarpey, M.M., Barbeito, L. and Beckman, J.S. (1999) Induction of nitric oxide-dependent apoptosis in motor neurons by zinc-deficient superoxide dismutase. Science, 286, 2498\u20132500.","DOI":"10.1126\/science.286.5449.2498"},{"key":"key\n\t\t\t\t20171012153241_DDI236C16","doi-asserted-by":"crossref","unstructured":"Wiedau-Pazos, M., Goto, J.J., Rabizadeh, S., Gralla, E.B., Roe, J.A., Lee, M.K., Valentine, J.S. and Bredesen, D.E. (1996) Altered reactivity of superoxide dismutase in familial amyotrophic lateral sclerosis. Science, 271, 515\u2013518.","DOI":"10.1126\/science.271.5248.515"},{"key":"key\n\t\t\t\t20171012153241_DDI236C17","doi-asserted-by":"crossref","unstructured":"Wang, J., Slunt, H., Gonzales, V., Fromholt, D., Coonfield, M., Copeland, N.G., Jenkins, N.A. and Borchelt, D.R. (2003) Copper-binding-site-null SOD1 causes ALS in transgenic mice: aggregates of non-native SOD1 delineate a common feature. Hum. Mol. Genet., 12, 2753\u20132764.","DOI":"10.1093\/hmg\/ddg312"},{"key":"key\n\t\t\t\t20171012153241_DDI236C18","doi-asserted-by":"crossref","unstructured":"Wang, J., Xu, G., Gonzales, V., Coonfield, M., Fromholt, D., Copeland, N.G., Jenkins, N.A. and Borchelt, D.R. (2002) Fibrillar inclusions and motor neuron degeneration in transgenic mice expressing superoxide dismutase 1 with a disrupted copper-binding site. Neurobiol. Dis., 10, 128\u2013138.","DOI":"10.1006\/nbdi.2002.0498"},{"key":"key\n\t\t\t\t20171012153241_DDI236C19","doi-asserted-by":"crossref","unstructured":"Subramaniam, J.R., Lyons, W.E., Liu, J., Bartnikas, T.B., Rothstein, J., Price, D.L., Cleveland, D.W., Gitlin, J.D. and Wong, P.C. (2002) Mutant SOD1 causes motor neuron disease independent of copper chaperone-mediated copper loading. Nat. Neurosci., 5, 301\u2013307.","DOI":"10.1038\/nn823"},{"key":"key\n\t\t\t\t20171012153241_DDI236C20","doi-asserted-by":"crossref","unstructured":"Liu, J., Lillo, C., Jonsson, P.A., Vande, V.C., Ward, C.M., Miller, T.M., Subramaniam, J.R., Rothstein, J.D., Marklund, S., Andersen, P.M. et\u00a0al. (2004) Toxicity of familial ALS-linked SOD1 mutants from selective recruitment to spinal mitochondria. Neuron, 43, 5\u201317.","DOI":"10.1016\/j.neuron.2004.06.016"},{"key":"key\n\t\t\t\t20171012153241_DDI236C21","doi-asserted-by":"crossref","unstructured":"Vijayvergiya, C., Beal, M.F., Buck, J. and Manfredi, G. (2005) Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice. J. Neurosci., 25, 2463\u20132470.","DOI":"10.1523\/JNEUROSCI.4385-04.2005"},{"key":"key\n\t\t\t\t20171012153241_DDI236C22","doi-asserted-by":"crossref","unstructured":"Johnston, J.A., Dalton, M.J., Gurney, M.E. and Kopito, R.R. (2000) Formation of high molecular weight complexes of mutant Cu, Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis. Proc. Natl. Acad. Sci. USA, 97, 12571\u201312576.","DOI":"10.1073\/pnas.220417997"},{"key":"key\n\t\t\t\t20171012153241_DDI236C23","doi-asserted-by":"crossref","unstructured":"Wang, J., Xu, G. and Borchelt, D.R. (2002) High molecular weight complexes of mutant superoxide dismutase 1: age-dependent and tissue-specific accumulation. Neurobiol. Dis., 9, 139\u2013148.","DOI":"10.1006\/nbdi.2001.0471"},{"key":"key\n\t\t\t\t20171012153241_DDI236C24","doi-asserted-by":"crossref","unstructured":"Zu, J.S., Deng, H.X., Lo, T.P., Mitsumoto, H., Ahmed, M.S., Hung, W.Y., Cai, Z.J., Tainer, J.A. and Siddique, T. (1997) Exon 5 encoded domain is not required for the toxic function of mutant SOD1 but essential for the dismutase activity: identification and characterization of two new SOD1 mutations associated with familial amyotrophic lateral sclerosis. Neurogenetics, 1, 65\u201371.","DOI":"10.1007\/s100480050010"},{"key":"key\n\t\t\t\t20171012153241_DDI236C25","doi-asserted-by":"crossref","unstructured":"Jonsson, P.A., Ernhill, K., Andersen, P.M., Bergemalm, D., Brannstrom, T., Gredal, O., Nilsson, P. and Marklund, S.L. (2004) Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis. Brain, 127, 73\u201388.","DOI":"10.1093\/brain\/awh005"},{"key":"key\n\t\t\t\t20171012153241_DDI236C26","doi-asserted-by":"crossref","unstructured":"Watanabe, Y., Yasui, K., Nakano, T., Doi, K., Fukada, Y., Kitayama, M., Ishimoto, M., Kurihara, S., Kawashima, M., Fukuda, H. et\u00a0al. (2005) Mouse motor neuron disease caused by truncated SOD1 with or without C-terminal modification. Brain Res. Mol. Brain Res., 135, 12\u201320.","DOI":"10.1016\/j.molbrainres.2004.11.019"},{"key":"key\n\t\t\t\t20171012153241_DDI236C27","doi-asserted-by":"crossref","unstructured":"Bruijn, L.I., Becher, M.W., Lee, M.K., Anderson, K.L., Jenkins, N.A., Copeland, N.G., Sisodia, S.S., Rothstein, J.D., Borchelt, D.R., Price, D.L. et\u00a0al. (1997) ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron, 18, 327\u2013338.","DOI":"10.1016\/S0896-6273(00)80272-X"},{"key":"key\n\t\t\t\t20171012153241_DDI236C28","doi-asserted-by":"crossref","unstructured":"Borchelt, D.R., Wong, P.C., Becher, M.W., Pardo, C.A., Lee, M.K., Xu, Z.S., Thinakaran, G., Jenkins, N.A., Copeland, N.G., Sisodia, S.S. et\u00a0al. (1998) Axonal transport of mutant superoxide dismutase 1 and focal axonal abnormalities in the proximal axons of transgenic mice. Neurobiol. Dis., 5, 27\u201335.","DOI":"10.1006\/nbdi.1998.0178"},{"key":"key\n\t\t\t\t20171012153241_DDI236C29","doi-asserted-by":"crossref","unstructured":"Horwitz, J. (2003) Alpha-crystallin. Exp. Eye. Res., 76, 145\u2013153.","DOI":"10.1016\/S0014-4835(02)00278-6"},{"key":"key\n\t\t\t\t20171012153241_DDI236C30","doi-asserted-by":"crossref","unstructured":"Narberhaus, F. (2002) Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network. Microbiol. Mol. Biol. Rev., 66, 64\u201393.","DOI":"10.1128\/MMBR.66.1.64-93.2002"},{"key":"key\n\t\t\t\t20171012153241_DDI236C31","doi-asserted-by":"crossref","unstructured":"Elam, J.S., Taylor, A.B., Strange, R., Antonyuk, S., Doucette, P.A., Rodriguez, J.A., Hasnain, S.S., Hayward, L.J., Valentine, J.S., Yeates, T.O. et\u00a0al. (2003) Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS. Nat. Struct. Biol., 10, 461\u2013467.","DOI":"10.1038\/nsb935"},{"key":"key\n\t\t\t\t20171012153241_DDI236C32","doi-asserted-by":"crossref","unstructured":"Watanabe, M., Dykes-Hoberg, M., Cizewski, C.V., Price, D.L., Wong, P.C. and Rothstein, J.D. (2001) Histological evidence of protein aggregation in mutant SOD1 transgenic mice and in amyotrophic lateral sclerosis neural tissues. Neurobiol. Dis., 8, 933\u2013941.","DOI":"10.1006\/nbdi.2001.0443"},{"key":"key\n\t\t\t\t20171012153241_DDI236C33","doi-asserted-by":"crossref","unstructured":"Cheroni, C., Peviani, M., Cascio, P., DeBiasi, S., Monti, C. and Bendotti, C. (2005) Accumulation of human SOD1 and ubiquitinated deposits in the spinal cord of SOD1G93A mice during motor neuron disease progression correlates with a decrease of proteasome. Neurobiol. Dis., 18, 509\u2013522.","DOI":"10.1016\/j.nbd.2004.12.007"},{"key":"key\n\t\t\t\t20171012153241_DDI236C34","doi-asserted-by":"crossref","unstructured":"Pasinelli, P., Belford, M.E., Lennon, N., Bacskai, B.J., Hyman, B.T., Trotti, D. and Brown, R.H., Jr. (2004) Amyotrophic lateral sclerosis-associated SOD1 mutant proteins bind and aggregate with Bcl-2 in spinal cord mitochondria. Neuron, 43, 19\u201330.","DOI":"10.1016\/j.neuron.2004.06.021"},{"key":"key\n\t\t\t\t20171012153241_DDI236C35","doi-asserted-by":"crossref","unstructured":"Tummala, H., Jung, C., Tiwari, A., Higgins, C.M., Hayward, L.J. and Xu, Z. (2005) Inhibition of chaperone activity is a shared property of several Cu, Zn-superoxide dismutase mutants that cause amyotrophic lateral sclerosis. J. Biol. Chem., 280, 17725\u201317731.","DOI":"10.1074\/jbc.M501705200"},{"key":"key\n\t\t\t\t20171012153241_DDI236C36","unstructured":"McKinley, M.P., Meyer, R.K., Kenaga, L., Rahbar, F., Cotter, R., Serban, A. and Prusiner, S.B. (1991) Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol., 65, 1340\u20131351."},{"key":"key\n\t\t\t\t20171012153241_DDI236C37","doi-asserted-by":"crossref","unstructured":"Vleminckx, V., Van Damme, P., Goffin, K., Delye, H., Van Den, B.L. and Robberecht, W. (2002) Upregulation of HSP27 in a transgenic model of ALS. J. Neuropathol. Exp. Neurol., 61, 968\u2013974.","DOI":"10.1093\/jnen\/61.11.968"},{"key":"key\n\t\t\t\t20171012153241_DDI236C38","doi-asserted-by":"crossref","unstructured":"Kumar, L.V. and Rao, C.M. (2000) Domain swapping in human alpha A and alpha B crystallins affects oligomerization and enhances chaperone-like activity. J. Biol. Chem., 275, 22009\u201322013.","DOI":"10.1074\/jbc.M003307200"},{"key":"key\n\t\t\t\t20171012153241_DDI236C39","doi-asserted-by":"crossref","unstructured":"Devlin, G.L., Carver, J.A. and Bottomley, S.P. (2003) The selective inhibition of serpin aggregation by the molecular chaperone, alpha-crystallin, indicates a nucleation-dependent specificity. J. Biol. Chem., 278, 48644\u201348650.","DOI":"10.1074\/jbc.M308376200"},{"key":"key\n\t\t\t\t20171012153241_DDI236C40","doi-asserted-by":"crossref","unstructured":"Sathish, H.A., Stein, R.A., Yang, G. and Mchaourab, H.S. (2003) Mechanism of chaperone function in small heat-shock proteins. Fluorescence studies of the conformations of T4 lysozyme bound to alphaB-crystallin. J. Biol. Chem., 278, 44214\u201344221.","DOI":"10.1074\/jbc.M307578200"},{"key":"key\n\t\t\t\t20171012153241_DDI236C41","doi-asserted-by":"crossref","unstructured":"Tanksale, A., Ghatge, M. and Deshpande, V. (2002) Alpha-crystallin binds to the aggregation-prone molten-globule state of alkaline protease: implications for preventing irreversible thermal denaturation. Protein Sci, 11, 1720\u20131728.","DOI":"10.1110\/ps.0201802"},{"key":"key\n\t\t\t\t20171012153241_DDI236C42","doi-asserted-by":"crossref","unstructured":"Kumar, M.S., Kapoor, M., Sinha, S. and Reddy, G.B. (2005) Insights into hydrophobicity and the chaperone-like function of alpha A and alpha B-crystallins: an isothermal titration calorimetric study. J. Biol. Chem., 280, 21726\u201321730.","DOI":"10.1074\/jbc.M500405200"},{"key":"key\n\t\t\t\t20171012153241_DDI236C43","doi-asserted-by":"crossref","unstructured":"Koyama, Y. and Goldman, J.E. (1999) Formation of GFAP cytoplasmic inclusions in astrocytes and their disaggregation by alphaB-crystallin. Am. J. Pathol., 154, 1563\u20131572.","DOI":"10.1016\/S0002-9440(10)65409-0"},{"key":"key\n\t\t\t\t20171012153241_DDI236C44","doi-asserted-by":"crossref","unstructured":"Biswas, A. and Das, K.P. (2004) Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function. J. Biol. Chem., 279, 42648\u201342657.","DOI":"10.1074\/jbc.M404444200"},{"key":"key\n\t\t\t\t20171012153241_DDI236C45","doi-asserted-by":"crossref","unstructured":"Pramatarova, A., Laganiere, J., Roussel, J., Brisebois, K. and Rouleau, G.A. (2001) Neuron-specific expression of mutant superoxide dismutase 1 in transgenic mice does not lead to motor impairment. J. Neurosci., 21, 3369\u20133374.","DOI":"10.1523\/JNEUROSCI.21-10-03369.2001"},{"key":"key\n\t\t\t\t20171012153241_DDI236C46","doi-asserted-by":"crossref","unstructured":"Lino, M.M., Schneider, C. and Caroni, P. (2002) Accumulation of SOD1 mutants in postnatal motoneurons does not cause motoneuron pathology or motoneuron disease. J. Neurosci., 22, 4825\u20134832.","DOI":"10.1523\/JNEUROSCI.22-12-04825.2002"},{"key":"key\n\t\t\t\t20171012153241_DDI236C47","doi-asserted-by":"crossref","unstructured":"Clement, A.M., Nguyen, M.D., Roberts, E.A., Garcia, M.L., Boillee, S., Rule, M., McMahon, A.P., Doucette, W., Siwek, D., Ferrante et\u00a0al. (2003) Wild-type nonneuronal cells extend survival of SOD1 mutant motor neurons in ALS mice. Science, 302, 113\u2013117.","DOI":"10.1126\/science.1086071"},{"key":"key\n\t\t\t\t20171012153241_DDI236C48","doi-asserted-by":"crossref","unstructured":"Sun, X., Moriarty, P.M. and Maquat, L.E. (2000) Nonsense-mediated decay of glutathione peroxidase 1 mRNA in the cytoplasm depends on intron position. EMBO J., 19, 4734\u20134744.","DOI":"10.1093\/emboj\/19.17.4734"},{"key":"key\n\t\t\t\t20171012153241_DDI236C49","unstructured":"Maquat, L.E. (1995) When cells stop making sense: effects of nonsense codons on RNA metabolism in vertebrate cells. RNA, 1, 453\u2013465."},{"key":"key\n\t\t\t\t20171012153241_DDI236C50","doi-asserted-by":"crossref","unstructured":"Maquat, L.E. and Carmichael, G.G. (2001) Quality control of mRNA function. Cell, 104, 173\u2013176.","DOI":"10.1016\/S0092-8674(01)00202-1"}],"container-title":["Human Molecular Genetics"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/hmg\/article-pdf\/14\/16\/2335\/17241468\/ddi236.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2019,3,5]],"date-time":"2019-03-05T13:01:11Z","timestamp":1551790871000},"score":1,"resource":{"primary":{"URL":"http:\/\/academic.oup.com\/hmg\/article\/14\/16\/2335\/675656\/Somatodendritic-accumulation-of-misfolded"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2005,7,13]]},"references-count":50,"journal-issue":{"issue":"16","published-online":{"date-parts":[[2005,7,13]]},"published-print":{"date-parts":[[2005,8,15]]}},"URL":"https:\/\/doi.org\/10.1093\/hmg\/ddi236","relation":{},"ISSN":["1460-2083","0964-6906"],"issn-type":[{"value":"1460-2083","type":"electronic"},{"value":"0964-6906","type":"print"}],"subject":[],"published-other":{"date-parts":[[2005,8,15]]},"published":{"date-parts":[[2005,7,13]]}}}