Format
Sort by

Send to

Choose Destination

Links from PubMed

Items: 13

1.

Mechanism of C-Terminal Fragments of Amyloid β-Protein as Aβ Inhibitors: Do C-Terminal Interactions Play a Key Role in Their Inhibitory Activity?

Zheng X, Wu C, Liu D, Li H, Bitan G, Shea JE, Bowers MT.

J Phys Chem B. 2016 Mar 3;120(8):1615-23. doi: 10.1021/acs.jpcb.5b08177.

2.

Amyloid β-protein assembly: The effect of molecular tweezers CLR01 and CLR03.

Zheng X, Liu D, Klärner FG, Schrader T, Bitan G, Bowers MT.

J Phys Chem B. 2015 Apr 9;119(14):4831-41. doi: 10.1021/acs.jpcb.5b00692.

3.

Capping of aβ42 oligomers by small molecule inhibitors.

Fu Z, Aucoin D, Ahmed M, Ziliox M, Van Nostrand WE, Smith SO.

Biochemistry. 2014 Dec 23;53(50):7893-903. doi: 10.1021/bi500910b.

4.

Short Peptides as Inhibitors of Amyloid Aggregation.

Neddenriep B, Calciano A, Conti D, Sauve E, Paterson M, Bruno E, Moffet DA.

Open Biotechnol J. 2011 Dec 23;5:39-46.

5.

Impact of sequence on the molecular assembly of short amyloid peptides.

Wagoner VA, Cheon M, Chang I, Hall CK.

Proteins. 2014 Jul;82(7):1469-83. doi: 10.1002/prot.24515.

6.

Discrete molecular dynamics study of oligomer formation by N-terminally truncated amyloid β-protein.

Meral D, Urbanc B.

J Mol Biol. 2013 Jun 26;425(12):2260-75. doi: 10.1016/j.jmb.2013.03.010. Erratum in: J Mol Biol. 2015 Aug 14;427(16):2728-9.

7.

A two-step strategy for structure-activity relationship studies of N-methylated aβ42 C-terminal fragments as aβ42 toxicity inhibitors.

Li H, Zemel R, Lopes DH, Monien BH, Bitan G.

ChemMedChem. 2012 Mar 5;7(3):515-22. doi: 10.1002/cmdc.201100584.

8.

Inhibiting the nucleation of amyloid structure in a huntingtin fragment by targeting α-helix-rich oligomeric intermediates.

Mishra R, Jayaraman M, Roland BP, Landrum E, Fullam T, Kodali R, Thakur AK, Arduini I, Wetzel R.

J Mol Biol. 2012 Feb 3;415(5):900-17. doi: 10.1016/j.jmb.2011.12.011.

9.

Aβ(39-42) modulates Aβ oligomerization but not fibril formation.

Gessel MM, Wu C, Li H, Bitan G, Shea JE, Bowers MT.

Biochemistry. 2012 Jan 10;51(1):108-17. doi: 10.1021/bi201520b.

10.

C-terminal tetrapeptides inhibit Aβ42-induced neurotoxicity primarily through specific interaction at the N-terminus of Aβ42.

Li H, Du Z, Lopes DH, Fradinger EA, Wang C, Bitan G.

J Med Chem. 2011 Dec 22;54(24):8451-60. doi: 10.1021/jm200982p.

11.

Lysine-specific molecular tweezers are broad-spectrum inhibitors of assembly and toxicity of amyloid proteins.

Sinha S, Lopes DH, Du Z, Pang ES, Shanmugam A, Lomakin A, Talbiersky P, Tennstaedt A, McDaniel K, Bakshi R, Kuo PY, Ehrmann M, Benedek GB, Loo JA, Klärner FG, Schrader T, Wang C, Bitan G.

J Am Chem Soc. 2011 Oct 26;133(42):16958-69. doi: 10.1021/ja206279b.

12.

Structural basis for Aβ1–42 toxicity inhibition by Aβ C-terminal fragments: discrete molecular dynamics study.

Urbanc B, Betnel M, Cruz L, Li H, Fradinger EA, Monien BH, Bitan G.

J Mol Biol. 2011 Jul 8;410(2):316-28. doi: 10.1016/j.jmb.2011.05.021.

13.

Tissue transglutaminase-mediated glutamine deamidation of beta-amyloid peptide increases peptide solubility, whereas enzymatic cross-linking and peptide fragmentation may serve as molecular triggers for rapid peptide aggregation.

Schmid AW, Condemi E, Tuchscherer G, Chiappe D, Mutter M, Vogel H, Moniatte M, Tsybin YO.

J Biol Chem. 2011 Apr 8;286(14):12172-88. doi: 10.1074/jbc.M110.176149.

Items per page

Supplemental Content

Support Center