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Results: 7

Related Articles by Review for PubMed (Select 23161913)

1.

Rational design of potent domain antibody inhibitors of amyloid fibril assembly.

Ladiwala AR, Bhattacharya M, Perchiacca JM, Cao P, Raleigh DP, Abedini A, Schmidt AM, Varkey J, Langen R, Tessier PM.

Proc Natl Acad Sci U S A. 2012 Dec 4;109(49):19965-70. doi: 10.1073/pnas.1208797109. Epub 2012 Nov 15. Erratum in: Proc Natl Acad Sci U S A. 2013 Jan 22;110(4):1560.

2.

Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins.

Meredith SC.

Ann N Y Acad Sci. 2005 Dec;1066:181-221. Review.

PMID:
16533927
3.

Inhibiting toxic aggregation of amyloidogenic proteins: a therapeutic strategy for protein misfolding diseases.

Cheng B, Gong H, Xiao H, Petersen RB, Zheng L, Huang K.

Biochim Biophys Acta. 2013 Oct;1830(10):4860-71. doi: 10.1016/j.bbagen.2013.06.029. Epub 2013 Jun 29. Review.

PMID:
23820032
4.

Nanobodies as structural probes of protein misfolding and fibril formation.

De Genst E, Dobson CM.

Methods Mol Biol. 2012;911:533-58. doi: 10.1007/978-1-61779-968-6_34. Review.

PMID:
22886275
5.

Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena.

Pain C, Dumont J, Dumoulin M.

Biochimie. 2015 Apr;111:82-106. doi: 10.1016/j.biochi.2015.01.012. Epub 2015 Feb 3. Review.

PMID:
25656912
7.

Small molecule protein-protein interaction inhibitors as CNS therapeutic agents: current progress and future hurdles.

Blazer LL, Neubig RR.

Neuropsychopharmacology. 2009 Jan;34(1):126-41. doi: 10.1038/npp.2008.151. Epub 2008 Sep 17. Review.

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