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Results: 1 to 20 of 127

Similar articles for PubMed (Select 23603391)

1.

NMR characterization of the interaction of GroEL with amyloid β as a model ligand.

Yagi-Utsumi M, Kunihara T, Nakamura T, Uekusa Y, Makabe K, Kuwajima K, Kato K.

FEBS Lett. 2013 Jun 5;587(11):1605-9. doi: 10.1016/j.febslet.2013.04.007. Epub 2013 Apr 18.

2.

Factors governing the substrate recognition by GroEL chaperone: a sequence correlation approach.

Chaudhuri TK, Gupta P.

Cell Stress Chaperones. 2005 Spring;10(1):24-36.

3.

NMR analysis of the binding of a rhodanese peptide to a minichaperone in solution.

Kobayashi N, Freund SM, Chatellier J, Zahn R, Fersht AR.

J Mol Biol. 1999 Sep 10;292(1):181-90.

PMID:
10493867
4.

GroEL Recognizes an Amphipathic Helix and Binds to the Hydrophobic Side.

Li Y, Gao X, Chen L.

J Biol Chem. 2009 Feb 13;284(7):4324-31. doi: 10.1074/jbc.M804818200. Epub 2008 Dec 12.

5.
6.

Molecular dynamics simulations to investigate the aggregation behaviors of the Abeta(17-42) oligomers.

Zhao JH, Liu HL, Liu YF, Lin HY, Fang HW, Ho Y, Tsai WB.

J Biomol Struct Dyn. 2009 Feb;26(4):481-90.

PMID:
19108587
7.

Structural origin of polymorphism of Alzheimer's amyloid β-fibrils.

Agopian A, Guo Z.

Biochem J. 2012 Oct 1;447(1):43-50. doi: 10.1042/BJ20120034.

PMID:
22823461
8.

Interaction between amyloid beta peptide and an aggregation blocker peptide mimicking islet amyloid polypeptide.

Rezaei-Ghaleh N, Andreetto E, Yan LM, Kapurniotu A, Zweckstetter M.

PLoS One. 2011;6(5):e20289. doi: 10.1371/journal.pone.0020289. Epub 2011 May 25.

9.

N-terminal domain of myelin basic protein inhibits amyloid beta-protein fibril assembly.

Liao MC, Hoos MD, Aucoin D, Ahmed M, Davis J, Smith SO, Van Nostrand WE.

J Biol Chem. 2010 Nov 12;285(46):35590-8. doi: 10.1074/jbc.M110.169599. Epub 2010 Aug 31.

10.

Effect of introducing a short amyloidogenic sequence from the Aβ peptide at the N-terminus of 18-residue amphipathic helical peptides.

SivakamaSundari C, Rukmani S, Nagaraj R.

J Pept Sci. 2012 Feb;18(2):122-8. doi: 10.1002/psc.1424. Epub 2011 Nov 3.

PMID:
22052825
11.
12.

Mechanism of substrate recognition by the chaperonin GroEL.

Houry WA.

Biochem Cell Biol. 2001;79(5):569-77. Review.

PMID:
11716298
13.
14.

Interplay of structure and disorder in cochaperonin mobile loops.

Landry SJ, Taher A, Georgopoulos C, van der Vies SM.

Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11622-7.

15.

Induced beta-barrel formation of the Alzheimer's Abeta25-35 oligomers on carbon nanotube surfaces: implication for amyloid fibril inhibition.

Fu Z, Luo Y, Derreumaux P, Wei G.

Biophys J. 2009 Sep 16;97(6):1795-803. doi: 10.1016/j.bpj.2009.07.014.

16.
17.

Specific binding of a β-cyclodextrin dimer to the amyloid β peptide modulates the peptide aggregation process.

Wahlström A, Cukalevski R, Danielsson J, Jarvet J, Onagi H, Rebek J Jr, Linse S, Gräslund A.

Biochemistry. 2012 May 29;51(21):4280-9. doi: 10.1021/bi300341j. Epub 2012 May 17.

PMID:
22554145
18.

Residues in substrate proteins that interact with GroEL in the capture process are buried in the native state.

Stan G, Brooks BR, Lorimer GH, Thirumalai D.

Proc Natl Acad Sci U S A. 2006 Mar 21;103(12):4433-8. Epub 2006 Mar 14.

19.

Mechanism of the chaperone-like and antichaperone activities of amyloid fibrils of peptides from αA-crystallin.

Fukuhara S, Nishigaki T, Miyata K, Tsuchiya N, Waku T, Tanaka N.

Biochemistry. 2012 Jul 10;51(27):5394-401. Epub 2012 Jun 25.

PMID:
22694216
20.

What drives amyloid molecules to assemble into oligomers and fibrils?

Schmit JD, Ghosh K, Dill K.

Biophys J. 2011 Jan 19;100(2):450-8. doi: 10.1016/j.bpj.2010.11.041.

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