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Items: 1 to 20 of 262

1.

Folding mechanisms steer the amyloid fibril formation propensity of highly homologous proteins.

Malgieri G, D'Abrosca G, Pirone L, Toto A, Palmieri M, Russo L, Sciacca MFM, Tatè R, Sivo V, Baglivo I, Majewska R, Coletta M, Pedone PV, Isernia C, De Stefano M, Gianni S, Pedone EM, Milardi D, Fattorusso R.

Chem Sci. 2018 Mar 1;9(13):3290-3298. doi: 10.1039/c8sc00166a. eCollection 2018 Apr 7.

2.

[PIN+]ing down the mechanism of prion appearance.

Serio TR.

FEMS Yeast Res. 2018 May 1;18(3). doi: 10.1093/femsyr/foy026.

3.

Distinct thermodynamic signatures of oligomer generation in the aggregation of the amyloid-β peptide.

Cohen SIA, Cukalevski R, Michaels TCT, Šarić A, Törnquist M, Vendruscolo M, Dobson CM, Buell AK, Knowles TPJ, Linse S.

Nat Chem. 2018 May;10(5):523-531. doi: 10.1038/s41557-018-0023-x. Epub 2018 Mar 26.

PMID:
29581486
4.

Amyloid and the origin of life: self-replicating catalytic amyloids as prebiotic informational and protometabolic entities.

Maury CPJ.

Cell Mol Life Sci. 2018 May;75(9):1499-1507. doi: 10.1007/s00018-018-2797-9. Epub 2018 Mar 17.

5.

A specific form of prefibrillar aggregates that functions as a precursor of amyloid nucleation.

Yamamoto N, Tsuhara S, Tamura A, Chatani E.

Sci Rep. 2018 Jan 8;8(1):62. doi: 10.1038/s41598-017-18390-y.

6.

Recent progress on understanding the mechanisms of amyloid nucleation.

Chatani E, Yamamoto N.

Biophys Rev. 2018 Apr;10(2):527-534. doi: 10.1007/s12551-017-0353-8. Epub 2017 Dec 6. Review.

7.

Protein-Based Inheritance: Epigenetics beyond the Chromosome.

Harvey ZH, Chen Y, Jarosz DF.

Mol Cell. 2018 Jan 18;69(2):195-202. doi: 10.1016/j.molcel.2017.10.030. Epub 2017 Nov 16. Review.

PMID:
29153393
8.

A dominant-negative mutant inhibits multiple prion variants through a common mechanism.

Pei F, DiSalvo S, Sindi SS, Serio TR.

PLoS Genet. 2017 Oct 30;13(10):e1007085. doi: 10.1371/journal.pgen.1007085. eCollection 2017 Oct.

9.

Theory of amyloid fibril nucleation from folded proteins.

Zhang L, Schmit JD.

Isr J Chem. 2017 Jul;57(7-8):738-749. doi: 10.1002/ijch.201600079. Epub 2017 Jan 30.

PMID:
28935998
10.

The physical dimensions of amyloid aggregates control their infective potential as prion particles.

Marchante R, Beal DM, Koloteva-Levine N, Purton TJ, Tuite MF, Xue WF.

Elife. 2017 Sep 7;6. pii: e27109. doi: 10.7554/eLife.27109.

11.

Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.

Dharmadana D, Reynolds NP, Conn CE, Valéry C.

Interface Focus. 2017 Aug 6;7(4):20160160. doi: 10.1098/rsfs.2016.0160. Epub 2017 Jun 16. Review.

PMID:
28630679
12.

A novel pathway for amyloids self-assembly in aggregates at nanomolar concentration mediated by the interaction with surfaces.

Banerjee S, Hashemi M, Lv Z, Maity S, Rochet JC, Lyubchenko YL.

Sci Rep. 2017 Mar 30;7:45592. doi: 10.1038/srep45592.

13.

Combining DNP NMR with segmental and specific labeling to study a yeast prion protein strain that is not parallel in-register.

Frederick KK, Michaelis VK, Caporini MA, Andreas LB, Debelouchina GT, Griffin RG, Lindquist S.

Proc Natl Acad Sci U S A. 2017 Apr 4;114(14):3642-3647. doi: 10.1073/pnas.1619051114. Epub 2017 Mar 22.

14.

Aggregation of Mod5 is affected by tRNA binding with implications for tRNA gene-mediated silencing.

Read DF, Waller TJ, Tse E, Southworth DR, Engelke DR, Smaldino PJ.

FEBS Lett. 2017 Jun;591(11):1601-1610. doi: 10.1002/1873-3468.12627. Epub 2017 May 22.

PMID:
28303570
15.

Inferring Mechanistic Parameters from Amyloid Formation Kinetics by Approximate Bayesian Computation.

Nakatani-Webster E, Nath A.

Biophys J. 2017 Mar 14;112(5):868-880. doi: 10.1016/j.bpj.2017.01.011.

16.

Proteins Containing Expanded Polyglutamine Tracts and Neurodegenerative Disease.

Adegbuyiro A, Sedighi F, Pilkington AW 4th, Groover S, Legleiter J.

Biochemistry. 2017 Mar 7;56(9):1199-1217. doi: 10.1021/acs.biochem.6b00936. Epub 2017 Feb 21. Review.

17.

The chaperonin CCT inhibits assembly of α-synuclein amyloid fibrils by a specific, conformation-dependent interaction.

Sot B, Rubio-Muñoz A, Leal-Quintero A, Martínez-Sabando J, Marcilla M, Roodveldt C, Valpuesta JM.

Sci Rep. 2017 Jan 19;7:40859. doi: 10.1038/srep40859.

18.

The Effects of Ca2+ Concentration and E200K Mutation on the Aggregation Propensity of PrPC: A Computational Study.

Marrone A, Re N, Storchi L.

PLoS One. 2016 Dec 13;11(12):e0168039. doi: 10.1371/journal.pone.0168039. eCollection 2016.

19.

Polymorphism of fibrillar structures depending on the size of assembled Aβ17-42 peptides.

Cheon M, Kang M, Chang I.

Sci Rep. 2016 Nov 30;6:38196. doi: 10.1038/srep38196.

20.

Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.

Langlois CR, Pei F, Sindi SS, Serio TR.

PLoS Genet. 2016 Nov 4;12(11):e1006417. doi: 10.1371/journal.pgen.1006417. eCollection 2016 Nov.

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