Lorenzen N - Search Results

1

The role of stable α-synuclein oligomers in the molecular events underlying amyloid formation.

Lorenzen N, Nielsen SB, Buell AK, Kaspersen JD, Arosio P, Vad BS, Paslawski W, Christiansen G, Valnickova-Hansen Z, Andreasen M, Enghild JJ, Pedersen JS, Dobson CM, Knowles TP, Otzen DE. Lorenzen N, et al. J Am Chem Soc. 2014 Mar 12;136(10):3859-68. doi: 10.1021/ja411577t. Epub 2014 Feb 28. J Am Chem Soc. 2014. PMID: 24527756

2

Assays for α-synuclein aggregation.

Giehm L, Lorenzen N, Otzen DE. Giehm L, et al. Among authors: lorenzen n. Methods. 2011 Mar;53(3):295-305. doi: 10.1016/j.ymeth.2010.12.008. Epub 2010 Dec 14. Methods. 2011. PMID: 21163351 Review.

3

Role of elongation and secondary pathways in S6 amyloid fibril growth.

Lorenzen N, Cohen SI, Nielsen SB, Herling TW, Christiansen G, Dobson CM, Knowles TP, Otzen D. Lorenzen N, et al. Biophys J. 2012 May 2;102(9):2167-75. doi: 10.1016/j.bpj.2012.03.047. Biophys J. 2012. PMID: 22824281 Free PMC article.

4

The neuroendocrine protein 7B2 suppresses the aggregation of neurodegenerative disease-related proteins.

Helwig M, Hoshino A, Berridge C, Lee SN, Lorenzen N, Otzen DE, Eriksen JL, Lindberg I. Helwig M, et al. Among authors: lorenzen n. J Biol Chem. 2013 Jan 11;288(2):1114-24. doi: 10.1074/jbc.M112.417071. Epub 2012 Nov 21. J Biol Chem. 2013. PMID: 23172224 Free PMC article.

5

Off-pathway aggregation can inhibit fibrillation at high protein concentrations.

Deva T, Lorenzen N, Vad BS, Petersen SV, Thørgersen I, Enghild JJ, Kristensen T, Otzen DE. Deva T, et al. Among authors: lorenzen n. Biochim Biophys Acta. 2013 Mar;1834(3):677-87. doi: 10.1016/j.bbapap.2012.12.020. Epub 2013 Jan 8. Biochim Biophys Acta. 2013. PMID: 23313095

6

Electrochemical analysis of the fibrillation of Parkinson's disease α-synuclein.

Lopes P, Dyrnesli H, Lorenzen N, Otzen D, Ferapontova EE. Lopes P, et al. Among authors: lorenzen n. Analyst. 2014 Feb 21;139(4):749-56. doi: 10.1039/c3an01616a. Analyst. 2014. PMID: 24343298

7

The N-terminus of α-synuclein is essential for both monomeric and oligomeric interactions with membranes.

Lorenzen N, Lemminger L, Pedersen JN, Nielsen SB, Otzen DE. Lorenzen N, et al. FEBS Lett. 2014 Jan 31;588(3):497-502. doi: 10.1016/j.febslet.2013.12.015. Epub 2013 Dec 25. FEBS Lett. 2014. PMID: 24374342 Free article.

8

How epigallocatechin gallate can inhibit α-synuclein oligomer toxicity in vitro.

Lorenzen N, Nielsen SB, Yoshimura Y, Vad BS, Andersen CB, Betzer C, Kaspersen JD, Christiansen G, Pedersen JS, Jensen PH, Mulder FA, Otzen DE. Lorenzen N, et al. J Biol Chem. 2014 Aug 1;289(31):21299-310. doi: 10.1074/jbc.M114.554667. Epub 2014 Jun 6. J Biol Chem. 2014. PMID: 24907278 Free PMC article.

9

Oligomers of α-synuclein: picking the culprit in the line-up.

Lorenzen N, Otzen DE. Lorenzen N, et al. Essays Biochem. 2014;56:137-48. doi: 10.1042/bse0560137. Essays Biochem. 2014. PMID: 25131592

10

High stability and cooperative unfolding of α-synuclein oligomers.

Paslawski W, Andreasen M, Nielsen SB, Lorenzen N, Thomsen K, Kaspersen JD, Pedersen JS, Otzen DE. Paslawski W, et al. Among authors: lorenzen n. Biochemistry. 2014 Oct 7;53(39):6252-63. doi: 10.1021/bi5007833. Epub 2014 Sep 24. Biochemistry. 2014. PMID: 25216651

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