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Items: 1 to 20 of 161

1.

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.

2.

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.

3.

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.

4.

Molecular properties of TAR DNA binding protein-43 fragments are dependent upon its cleavage site.

Furukawa Y, Kaneko K, Nukina N.

Biochim Biophys Acta. 2011 Dec;1812(12):1577-83. doi: 10.1016/j.bbadis.2011.09.005. Epub 2011 Sep 16.

5.

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.

6.

The truncated C-terminal RNA recognition motif of TDP-43 protein plays a key role in forming proteinaceous aggregates.

Wang YT, Kuo PH, Chiang CH, Liang JR, Chen YR, Wang S, Shen JC, Yuan HS.

J Biol Chem. 2013 Mar 29;288(13):9049-57. doi: 10.1074/jbc.M112.438564. Epub 2013 Jan 31.

7.

Structural insights into TDP-43 in nucleic-acid binding and domain interactions.

Kuo PH, Doudeva LG, Wang YT, Shen CK, Yuan HS.

Nucleic Acids Res. 2009 Apr;37(6):1799-808. doi: 10.1093/nar/gkp013. Epub 2009 Jan 27.

8.

Low molecular weight species of TDP-43 generated by abnormal splicing form inclusions in amyotrophic lateral sclerosis and result in motor neuron death.

Xiao S, Sanelli T, Chiang H, Sun Y, Chakrabartty A, Keith J, Rogaeva E, Zinman L, Robertson J.

Acta Neuropathol. 2015 Jul;130(1):49-61. doi: 10.1007/s00401-015-1412-5. Epub 2015 Mar 19.

9.

Point mutations in the N-terminal domain of transactive response DNA-binding protein 43 kDa (TDP-43) compromise its stability, dimerization, and functions.

Mompeán M, Romano V, Pantoja-Uceda D, Stuani C, Baralle FE, Buratti E, Laurents DV.

J Biol Chem. 2017 Jul 14;292(28):11992-12006. doi: 10.1074/jbc.M117.775965. Epub 2017 May 31.

PMID:
28566288
10.

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.

11.

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.

12.

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.

13.

Aggregation of the 35-kDa fragment of TDP-43 causes formation of cytoplasmic inclusions and alteration of RNA processing.

Che MX, Jiang YJ, Xie YY, Jiang LL, Hu HY.

FASEB J. 2011 Jul;25(7):2344-53. doi: 10.1096/fj.10-174482. Epub 2011 Mar 30.

PMID:
21450909
14.

Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis.

Igaz LM, Kwong LK, Xu Y, Truax AC, Uryu K, Neumann M, Clark CM, Elman LB, Miller BL, Grossman M, McCluskey LF, Trojanowski JQ, Lee VM.

Am J Pathol. 2008 Jul;173(1):182-94. doi: 10.2353/ajpath.2008.080003. Epub 2008 Jun 5.

15.

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.

16.

Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43.

Morgan BR, Zitzewitz JA, Massi F.

Biophys J. 2017 Aug 8;113(3):540-549. doi: 10.1016/j.bpj.2017.06.049.

PMID:
28793209
17.

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.

PMID:
19815002
18.

TDP-43 transgenic mice develop spastic paralysis and neuronal inclusions characteristic of ALS and frontotemporal lobar degeneration.

Wils H, Kleinberger G, Janssens J, Pereson S, Joris G, Cuijt I, Smits V, Ceuterick-de Groote C, Van Broeckhoven C, Kumar-Singh S.

Proc Natl Acad Sci U S A. 2010 Feb 23;107(8):3858-63. doi: 10.1073/pnas.0912417107. Epub 2010 Feb 3.

19.

Dysregulation of the ALS-associated gene TDP-43 leads to neuronal death and degeneration in mice.

Igaz LM, Kwong LK, Lee EB, Chen-Plotkin A, Swanson E, Unger T, Malunda J, Xu Y, Winton MJ, Trojanowski JQ, Lee VM.

J Clin Invest. 2011 Feb;121(2):726-38. doi: 10.1172/JCI44867. Epub 2011 Jan 4.

20.

Epitope mapping of antibodies against TDP-43 and detection of protease-resistant fragments of pathological TDP-43 in amyotrophic lateral sclerosis and frontotemporal lobar degeneration.

Tsuji H, Nonaka T, Yamashita M, Masuda-Suzukake M, Kametani F, Akiyama H, Mann DM, Tamaoka A, Hasegawa M.

Biochem Biophys Res Commun. 2012 Jan 6;417(1):116-21. doi: 10.1016/j.bbrc.2011.11.066. Epub 2011 Nov 22.

PMID:
22133678

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