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Items: 1 to 20 of 46

1.

Mercury and Alzheimer's Disease: Hg(II) Ions Display Specific Binding to the Amyloid-β Peptide and Hinder Its Fibrillization.

Wallin C, Friedemann M, Sholts SB, Noormägi A, Svantesson T, Jarvet J, Roos PM, Palumaa P, Gräslund A, Wärmländer SKTS.

Biomolecules. 2019 Dec 27;10(1). pii: E44. doi: 10.3390/biom10010044.

2.

Toxicity of Amyloid-β Peptides Varies Depending on Differentiation Route of SH-SY5Y Cells.

Krishtal J, Metsla K, Bragina O, Tõugu V, Palumaa P.

J Alzheimers Dis. 2019;71(3):879-887. doi: 10.3233/JAD-190705.

PMID:
31450506
3.

Redox properties of Cys2His2 and Cys4 zinc fingers determined by electrospray ionization mass spectrometry.

Smirnova J, Kabin E, Tõugu V, Palumaa P.

FEBS Open Bio. 2018 Apr 25;8(6):923-931. doi: 10.1002/2211-5463.12422. eCollection 2018 Jun.

4.

Copper(I)-binding properties of de-coppering drugs for the treatment of Wilson disease. α-Lipoic acid as a potential anti-copper agent.

Smirnova J, Kabin E, Järving I, Bragina O, Tõugu V, Plitz T, Palumaa P.

Sci Rep. 2018 Jan 23;8(1):1463. doi: 10.1038/s41598-018-19873-2.

5.

In situ fibrillizing amyloid-beta 1-42 induces neurite degeneration and apoptosis of differentiated SH-SY5Y cells.

Krishtal J, Bragina O, Metsla K, Palumaa P, Tõugu V.

PLoS One. 2017 Oct 24;12(10):e0186636. doi: 10.1371/journal.pone.0186636. eCollection 2017.

6.

Erratum to: Assessment of Blood Contamination in Biological Fluids Using MALDI-TOF MS.

Laks K, Kirsipuu T, Dmitrijeva T, Salumets A, Palumaa P.

Protein J. 2016 Jun;35(3):177-178. No abstract available.

PMID:
27101472
7.

Assessment of Blood Contamination in Biological Fluids Using MALDI-TOF MS.

Laks K, Kirsipuu T, Dmitrijeva T, Salumets A, Palumaa P.

Protein J. 2016 Jun;35(3):171-6. doi: 10.1007/s10930-016-9657-y. Erratum in: Protein J. 2016 Jun;35(3):177-8.

PMID:
27023353
8.

Insulin Fibrillization at Acidic and Physiological pH Values is Controlled by Different Molecular Mechanisms.

Noormägi A, Valmsen K, Tõugu V, Palumaa P.

Protein J. 2015 Dec;34(6):398-403.

PMID:
26493286
9.

Effect of methionine-35 oxidation on the aggregation of amyloid-β peptide.

Friedemann M, Helk E, Tiiman A, Zovo K, Palumaa P, Tõugu V.

Biochem Biophys Rep. 2015 Jul 30;3:94-99. doi: 10.1016/j.bbrep.2015.07.017. eCollection 2015 Sep.

10.

Metallothionein 2A affects the cell respiration by suppressing the expression of mitochondrial protein cytochrome c oxidase subunit II.

Bragina O, Gurjanova K, Krishtal J, Kulp M, Karro N, Tõugu V, Palumaa P.

J Bioenerg Biomembr. 2015 Jun;47(3):209-16. doi: 10.1007/s10863-015-9609-9. Epub 2015 Mar 27.

PMID:
25808318
11.

Formation of [4Fe-4S] clusters in the mitochondrial iron-sulfur cluster assembly machinery.

Brancaccio D, Gallo A, Mikolajczyk M, Zovo K, Palumaa P, Novellino E, Piccioli M, Ciofi-Baffoni S, Banci L.

J Am Chem Soc. 2014 Nov 19;136(46):16240-50. doi: 10.1021/ja507822j. Epub 2014 Nov 7.

PMID:
25347204
12.

Affinity of zinc and copper ions for insulin monomers.

Gavrilova J, Tõugu V, Palumaa P.

Metallomics. 2014 Jul;6(7):1296-300. doi: 10.1039/c4mt00059e.

PMID:
24889871
13.

The role of initial oligomers in amyloid fibril formation by human stefin B.

Taler-Verčič A, Kirsipuu T, Friedemann M, Noormägi A, Polajnar M, Smirnova J, Znidarič MT, Zganec M, Skarabot M, Vilfan A, Staniforth RA, Palumaa P, Zerovnik E.

Int J Mol Sci. 2013 Sep 5;14(9):18362-84. doi: 10.3390/ijms140918362.

14.

Copper chaperones. The concept of conformational control in the metabolism of copper.

Palumaa P.

FEBS Lett. 2013 Jun 27;587(13):1902-10. doi: 10.1016/j.febslet.2013.05.019. Epub 2013 May 16. Review.

15.

Effect of agitation on the peptide fibrillization: Alzheimer's amyloid-β peptide 1-42 but not amylin and insulin fibrils can grow under quiescent conditions.

Tiiman A, Noormägi A, Friedemann M, Krishtal J, Palumaa P, Tõugu V.

J Pept Sci. 2013 Jun;19(6):386-91. doi: 10.1002/psc.2513. Epub 2013 Apr 23.

PMID:
23609985
16.

The missing link in the amyloid cascade of Alzheimer's disease - metal ions.

Tiiman A, Palumaa P, Tõugu V.

Neurochem Int. 2013 Mar;62(4):367-78. doi: 10.1016/j.neuint.2013.01.023. Epub 2013 Feb 6. Review.

PMID:
23395747
17.

Human superoxide dismutase 1 (hSOD1) maturation through interaction with human copper chaperone for SOD1 (hCCS).

Banci L, Bertini I, Cantini F, Kozyreva T, Massagni C, Palumaa P, Rubino JT, Zovo K.

Proc Natl Acad Sci U S A. 2012 Aug 21;109(34):13555-60. doi: 10.1073/pnas.1207493109. Epub 2012 Aug 6.

18.

Redox and metal ion binding properties of human insulin-like growth factor 1 determined by electrospray ionization mass spectrometry.

Smirnova J, Muhhina J, Tõugu V, Palumaa P.

Biochemistry. 2012 Jul 24;51(29):5851-9. doi: 10.1021/bi300494s. Epub 2012 Jul 10.

PMID:
22746182
19.

Redox-active Cu(II)-Aβ causes substantial changes in axonal integrity in cultured cortical neurons in an oxidative-stress dependent manner.

Howells C, Saar K, Eaton E, Ray S, Palumaa P, Shabala L, Adlard PA, Bennett W, West AK, Guillemin GJ, Chung RS.

Exp Neurol. 2012 Oct;237(2):499-506. doi: 10.1016/j.expneurol.2012.06.002. Epub 2012 Jun 9.

PMID:
22691462
20.

Interference of low-molecular substances with the thioflavin-T fluorescence assay of amyloid fibrils.

Noormägi A, Primar K, Tõugu V, Palumaa P.

J Pept Sci. 2012 Jan;18(1):59-64. doi: 10.1002/psc.1416. Epub 2011 Nov 14.

PMID:
22083646

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