Literature DB >> 30290957

Keys to Amyloid City: Computation and NMR Reveal Potential TDP-43 ALS Intermediates.

W Michael Babinchak1, Zhenlu Li1, Matthias Buck2.   

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Year:  2018        PMID： 30290957      PMCID： PMC6225042          DOI： 10.1016/j.bpj.2018.09.012

Source DB:  PubMed          Journal:  Biophys J        ISSN： 0006-3495            Impact factor:   4.033


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  10 in total

1.  Replica-Averaged Metadynamics.

Authors:  Carlo Camilloni; Andrea Cavalli; Michele Vendruscolo
Journal:  J Chem Theory Comput       Date:  2013-11-21       Impact factor: 6.006

2.  Mutation in the RRM2 domain of TDP-43 in Amyotrophic Lateral Sclerosis with rapid progression associated with ubiquitin positive aggregates in cultured motor neurons.

Authors:  Cindy Maurel; Blandine Madji-Hounoum; Rose-Anne Thepault; Sylviane Marouillat; Céline Brulard; Véronique Danel-Brunaud; Jean-Philippe Camdessanche; Helene Blasco; Philippe Corcia; Christian R Andres; Patrick Vourc'h
Journal:  Amyotroph Lateral Scler Frontotemporal Degener       Date:  2017-07-13       Impact factor: 4.092

3.  Comparative analysis of thermal unfolding simulations of RNA recognition motifs (RRMs) of TAR DNA-binding protein 43 (TDP-43).

Authors:  Amresh Prakash; Vijay Kumar; Naveen Kumar Meena; Md Imtaiyaz Hassan; Andrew M Lynn
Journal:  J Biomol Struct Dyn       Date:  2018-01-10

4.  Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis.

Authors:  Manuela Neumann; Deepak M Sampathu; Linda K Kwong; Adam C Truax; Matthew C Micsenyi; Thomas T Chou; Jennifer Bruce; Theresa Schuck; Murray Grossman; Christopher M Clark; Leo F McCluskey; Bruce L Miller; Eliezer Masliah; Ian R Mackenzie; Howard Feldman; Wolfgang Feiden; Hans A Kretzschmar; John Q Trojanowski; Virginia M-Y Lee
Journal:  Science       Date:  2006-10-06       Impact factor: 47.728

Review 5.  Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade.

Authors:  Fabrizio Chiti; Christopher M Dobson
Journal:  Annu Rev Biochem       Date:  2017-05-12       Impact factor: 23.643

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

Authors:  Brian C Mackness; Meme T Tran; Shannan P McClain; C Robert Matthews; Jill A Zitzewitz
Journal:  J Biol Chem       Date:  2014-02-04       Impact factor: 5.157

7.  Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis.

Authors:  Davide Tavella; Jill A Zitzewitz; Francesca Massi
Journal:  Biophys J       Date:  2018-09-21       Impact factor: 4.033

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

Authors:  Pan-Hsien Kuo; Lyudmila G Doudeva; Yi-Ting Wang; Che-Kun James Shen; Hanna S Yuan
Journal:  Nucleic Acids Res       Date:  2009-01-27       Impact factor: 16.971

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

Authors:  Yi-Ting Wang; Pan-Hsien Kuo; Chien-Hao Chiang; Jhe-Ruei Liang; Yun-Ru Chen; Shuying Wang; James C K Shen; Hanna S Yuan
Journal:  J Biol Chem       Date:  2013-01-31       Impact factor: 5.157

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

Authors:  Liangzhong Lim; Yuanyuan Wei; Yimei Lu; Jianxing Song
Journal:  PLoS Biol       Date:  2016-01-06       Impact factor: 8.029
  10 in total

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