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Items: 1 to 20 of 71

1.

Interaction with polyglutamine aggregates reveals a Q/N-rich domain in TDP-43.

Fuentealba RA, Udan M, Bell S, Wegorzewska I, Shao J, Diamond MI, Weihl CC, Baloh RH.

J Biol Chem. 2010 Aug 20;285(34):26304-14. doi: 10.1074/jbc.M110.125039. Epub 2010 Jun 16.

2.

Implications of the prion-related Q/N domains in TDP-43 and FUS.

Udan M, Baloh RH.

Prion. 2011 Jan-Mar;5(1):1-5. Epub 2011 Jan 1. Review.

3.

Protein aggregates and regional disease spread in ALS is reminiscent of prion-like pathogenesis.

Verma A.

Neurol India. 2013 Mar-Apr;61(2):107-10. doi: 10.4103/0028-3886.111109. Review.

4.

TDP-43 mutant transgenic mice develop features of ALS and frontotemporal lobar degeneration.

Wegorzewska I, Bell S, Cairns NJ, Miller TM, Baloh RH.

Proc Natl Acad Sci U S A. 2009 Nov 3;106(44):18809-14. doi: 10.1073/pnas.0908767106. Epub 2009 Oct 15.

5.

Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation.

Winton MJ, Igaz LM, Wong MM, Kwong LK, Trojanowski JQ, Lee VM.

J Biol Chem. 2008 May 9;283(19):13302-9. doi: 10.1074/jbc.M800342200. Epub 2008 Feb 27.

6.

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.

7.

TDP-43 loss of cellular function through aggregation requires additional structural determinants beyond its C-terminal Q/N prion-like domain.

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

Hum Mol Genet. 2015 Jan 1;24(1):9-20. doi: 10.1093/hmg/ddu415. Epub 2014 Aug 13.

8.

Structural determinants of the cellular localization and shuttling of TDP-43.

Ayala YM, Zago P, D'Ambrogio A, Xu YF, Petrucelli L, Buratti E, Baralle FE.

J Cell Sci. 2008 Nov 15;121(Pt 22):3778-85. doi: 10.1242/jcs.038950. Epub 2008 Oct 28.

9.

Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity.

Zhang YJ, Xu YF, Cook C, Gendron TF, Roettges P, Link CD, Lin WL, Tong J, Castanedes-Casey M, Ash P, Gass J, Rangachari V, Buratti E, Baralle F, Golde TE, Dickson DW, Petrucelli L.

Proc Natl Acad Sci U S A. 2009 May 5;106(18):7607-12. doi: 10.1073/pnas.0900688106. Epub 2009 Apr 21.

10.

Mutations in TDP-43 link glycine-rich domain functions to amyotrophic lateral sclerosis.

Pesiridis GS, Lee VM, Trojanowski JQ.

Hum Mol Genet. 2009 Oct 15;18(R2):R156-62. doi: 10.1093/hmg/ddp303. Review.

11.

Hyperphosphorylation as a defense mechanism to reduce TDP-43 aggregation.

Li HY, Yeh PA, Chiu HC, Tang CY, Tu BP.

PLoS One. 2011;6(8):e23075. doi: 10.1371/journal.pone.0023075. Epub 2011 Aug 5.

12.

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.

13.

[The implications of TDP-43 mutations in pathogenesis of amyotrophic lateral sclerosis].

Ishihara T, Yokoseki A, Nishizawa M, Takahashi H, Onodera O.

Brain Nerve. 2009 Nov;61(11):1301-7. Review. Japanese.

PMID:
19938687
14.

Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy.

Arai T, Hasegawa M, Nonoka T, Kametani F, Yamashita M, Hosokawa M, Niizato K, Tsuchiya K, Kobayashi Z, Ikeda K, Yoshida M, Onaya M, Fujishiro H, Akiyama H.

Neuropathology. 2010 Apr;30(2):170-81. doi: 10.1111/j.1440-1789.2009.01089.x. Epub 2010 Jan 19. Review.

PMID:
20102522
15.

How do the RNA-binding proteins TDP-43 and FUS relate to amyotrophic lateral sclerosis and frontotemporal degeneration, and to each other?

Baloh RH.

Curr Opin Neurol. 2012 Dec;25(6):701-7. doi: 10.1097/WCO.0b013e32835a269b. Review.

PMID:
23041957
16.

Prion-like nuclear aggregation of TDP-43 during heat shock is regulated by HSP40/70 chaperones.

Udan-Johns M, Bengoechea R, Bell S, Shao J, Diamond MI, True HL, Weihl CC, Baloh RH.

Hum Mol Genet. 2014 Jan 1;23(1):157-70. doi: 10.1093/hmg/ddt408. Epub 2013 Aug 19.

17.

Expression of TDP-43 C-terminal Fragments in Vitro Recapitulates Pathological Features of TDP-43 Proteinopathies.

Igaz LM, Kwong LK, Chen-Plotkin A, Winton MJ, Unger TL, Xu Y, Neumann M, Trojanowski JQ, Lee VM.

J Biol Chem. 2009 Mar 27;284(13):8516-24. doi: 10.1074/jbc.M809462200. Epub 2009 Jan 21.

18.

[The molecular mechanisms of intracellular TDP-43 aggregates].

Nonaka T, Arai T, Hasegawa M.

Brain Nerve. 2009 Nov;61(11):1292-300. Review. Japanese.

PMID:
19938686
19.

[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.

PMID:
21921519
20.

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.

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