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Items: 1 to 20 of 160


Aberrant assembly of RNA recognition motif 1 links to pathogenic conversion of TAR DNA-binding protein of 43 kDa (TDP-43).

Shodai A, Morimura T, Ido A, Uchida T, Ayaki T, Takahashi R, Kitazawa S, Suzuki S, Shirouzu M, Kigawa T, Muto Y, Yokoyama S, Takahashi R, Kitahara R, Ito H, Fujiwara N, Urushitani M.

J Biol Chem. 2013 May 24;288(21):14886-905. doi: 10.1074/jbc.M113.451849. Epub 2013 Apr 4.


Conserved acidic amino acid residues in a second RNA recognition motif regulate assembly and function of TDP-43.

Shodai A, Ido A, Fujiwara N, Ayaki T, Morimura T, Oono M, Uchida T, Takahashi R, Ito H, Urushitani M.

PLoS One. 2012;7(12):e52776. doi: 10.1371/journal.pone.0052776. Epub 2012 Dec 26.


Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate state.

Mackness BC, Tran MT, McClain SP, Matthews CR, Zitzewitz JA.

J Biol Chem. 2014 Mar 21;289(12):8264-76. doi: 10.1074/jbc.M113.542779. Epub 2014 Feb 4.


RNP2 of RNA recognition motif 1 plays a central role in the aberrant modification of TDP-43.

Takagi S, Iguchi Y, Katsuno M, Ishigaki S, Ikenaka K, Fujioka Y, Honda D, Niwa J, Tanaka F, Watanabe H, Adachi H, Sobue G.

PLoS One. 2013 Jun 28;8(6):e66966. doi: 10.1371/journal.pone.0066966. Print 2013.


TDP-43 is intrinsically aggregation-prone, and amyotrophic lateral sclerosis-linked mutations accelerate aggregation and increase toxicity.

Johnson BS, Snead D, Lee JJ, McCaffery JM, Shorter J, Gitler AD.

J Biol Chem. 2009 Jul 24;284(30):20329-39. doi: 10.1074/jbc.M109.010264. Epub 2009 May 22. Erratum in: J Biol Chem. 2009 Sep 11;284(37):25459.


Requirements for stress granule recruitment of fused in sarcoma (FUS) and TAR DNA-binding protein of 43 kDa (TDP-43).

Bentmann E, Neumann M, Tahirovic S, Rodde R, Dormann D, Haass C.

J Biol Chem. 2012 Jun 29;287(27):23079-94. doi: 10.1074/jbc.M111.328757. Epub 2012 May 4.


A seeding reaction recapitulates intracellular formation of Sarkosyl-insoluble transactivation response element (TAR) DNA-binding protein-43 inclusions.

Furukawa Y, Kaneko K, Watanabe S, Yamanaka K, Nukina N.

J Biol Chem. 2011 May 27;286(21):18664-72. doi: 10.1074/jbc.M111.231209. Epub 2011 Mar 24.


The molecular link between inefficient GluA2 Q/R site-RNA editing and TDP-43 pathology in motor neurons of sporadic amyotrophic lateral sclerosis patients.

Yamashita T, Kwak S.

Brain Res. 2014 Oct 10;1584:28-38. doi: 10.1016/j.brainres.2013.12.011. Epub 2013 Dec 16. Review.


Developmentally Regulated RNA-binding Protein 1 (Drb1)/RNA-binding Motif Protein 45 (RBM45), a Nuclear-Cytoplasmic Trafficking Protein, Forms TAR DNA-binding Protein 43 (TDP-43)-mediated Cytoplasmic Aggregates.

Mashiko T, Sakashita E, Kasashima K, Tominaga K, Kuroiwa K, Nozaki Y, Matsuura T, Hamamoto T, Endo H.

J Biol Chem. 2016 Jul 15;291(29):14996-5007. doi: 10.1074/jbc.M115.712232. Epub 2016 May 12.


Tar DNA binding protein of 43 kDa (TDP-43), 14-3-3 proteins and copper/zinc superoxide dismutase (SOD1) interact to modulate NFL mRNA stability. Implications for altered RNA processing in amyotrophic lateral sclerosis (ALS).

Volkening K, Leystra-Lantz C, Yang W, Jaffee H, Strong MJ.

Brain Res. 2009 Dec 11;1305:168-82. doi: 10.1016/j.brainres.2009.09.105. Epub 2009 Oct 6.


The dual functions of the extreme N-terminus of TDP-43 in regulating its biological activity and inclusion formation.

Zhang YJ, Caulfield T, Xu YF, Gendron TF, Hubbard J, Stetler C, Sasaguri H, Whitelaw EC, Cai S, Lee WC, Petrucelli L.

Hum Mol Genet. 2013 Aug 1;22(15):3112-22. doi: 10.1093/hmg/ddt166. Epub 2013 Apr 10.


[Clinical and pathological spectrum of TDP-43 associated ALS].

Onodera O, Yokoseki A, Tan CF, Ishihara T, Nishiira Y, Toyoshima Y, Kakita A, Nishizawa M, Takahashi H.

Rinsho Shinkeigaku. 2010 Nov;50(11):940-2. Review. Japanese.


Induction of amyloid fibrils by the C-terminal fragments of TDP-43 in amyotrophic lateral sclerosis.

Chen AK, Lin RY, Hsieh EZ, Tu PH, Chen RP, Liao TY, Chen W, Wang CH, Huang JJ.

J Am Chem Soc. 2010 Feb 3;132(4):1186-7. doi: 10.1021/ja9066207.


Potentiation of amyotrophic lateral sclerosis (ALS)-associated TDP-43 aggregation by the proteasome-targeting factor, ubiquilin 1.

Kim SH, Shi Y, Hanson KA, Williams LM, Sakasai R, Bowler MJ, Tibbetts RS.

J Biol Chem. 2009 Mar 20;284(12):8083-92. doi: 10.1074/jbc.M808064200. Epub 2008 Dec 26.


The structural integrity of TDP-43 N-terminus is required for efficient aggregate entrapment and consequent loss of protein function.

Romano V, Quadri Z, Baralle FE, Buratti E.

Prion. 2015;9(1):1-9. doi: 10.1080/19336896.2015.1011885.


Fused in sarcoma (FUS) protein lacking nuclear localization signal (NLS) and major RNA binding motifs triggers proteinopathy and severe motor phenotype in transgenic mice.

Shelkovnikova TA, Peters OM, Deykin AV, Connor-Robson N, Robinson H, Ustyugov AA, Bachurin SO, Ermolkevich TG, Goldman IL, Sadchikova ER, Kovrazhkina EA, Skvortsova VI, Ling SC, Da Cruz S, Parone PA, Buchman VL, Ninkina NN.

J Biol Chem. 2013 Aug 30;288(35):25266-74. doi: 10.1074/jbc.M113.492017. Epub 2013 Jul 18.


The RNA-binding motif 45 (RBM45) protein accumulates in inclusion bodies in amyotrophic lateral sclerosis (ALS) and frontotemporal lobar degeneration with TDP-43 inclusions (FTLD-TDP) patients.

Collins M, Riascos D, Kovalik T, An J, Krupa K, Krupa K, Hood BL, Conrads TP, Renton AE, Traynor BJ, Bowser R.

Acta Neuropathol. 2012 Nov;124(5):717-32. doi: 10.1007/s00401-012-1045-x. Epub 2012 Sep 21.


A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity.

Johnson BS, McCaffery JM, Lindquist S, Gitler AD.

Proc Natl Acad Sci U S A. 2008 Apr 29;105(17):6439-44. doi: 10.1073/pnas.0802082105. Epub 2008 Apr 23.


ALS-Causing Mutations Significantly Perturb the Self-Assembly and Interaction with Nucleic Acid of the Intrinsically Disordered Prion-Like Domain of TDP-43.

Lim L, Wei Y, Lu Y, Song J.

PLoS Biol. 2016 Jan 6;14(1):e1002338. doi: 10.1371/journal.pbio.1002338. eCollection 2016 Jan.


CUL2-mediated clearance of misfolded TDP-43 is paradoxically affected by VHL in oligodendrocytes in ALS.

Uchida T, Tamaki Y, Ayaki T, Shodai A, Kaji S, Morimura T, Banno Y, Nishitsuji K, Sakashita N, Maki T, Yamashita H, Ito H, Takahashi R, Urushitani M.

Sci Rep. 2016 Jan 11;6:19118. doi: 10.1038/srep19118.

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