The hairpin conformation of the amyloid beta peptide is an important structural motif along the aggregation pathway

↓ Direkt till sidans innehåll
↓ Direkt till sidans sekundära innehåll (sidomenyn)

Sökning: WFRF:(Abelein Axel) > The hairpin conform...

LIBRIS Formathandbok (Information om MARC21)

Fältnamn	Indikatorer	Metadata
000		04080naa a2200445 4500
001		oai:DiVA.org:su-105411
003		SwePub
008		140624s2014 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-1054112 URI
024	7	a https://doi.org/10.1007/s00775-014-1131-82 DOI
040		a (SwePub)su
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a for2 swepub-publicationtype
100	1	a Abelein, Axelu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)axab0026
245	1 0	a The hairpin conformation of the amyloid beta peptide is an important structural motif along the aggregation pathway
264		c 2014-04-16
264	1	b Springer Science and Business Media LLC,c 2014
338		a print2 rdacarrier
500		a AuthorCount:8;
520		a The amyloid beta (A beta) peptides are 39-42 residue-long peptides found in the senile plaques in the brains of Alzheimer's disease (AD) patients. These peptides self-aggregate in aqueous solution, going from soluble and mainly unstructured monomers to insoluble ordered fibrils. The aggregation process(es) are strongly influenced by environmental conditions. Several lines of evidence indicate that the neurotoxic species are the intermediate oligomeric states appearing along the aggregation pathways. This minireview summarizes recent findings, mainly based on solution and solid-state NMR experiments and electron microscopy, which investigate the molecular structures and characteristics of the A beta peptides at different stages along the aggregation pathways. We conclude that a hairpin-like conformation constitutes a common motif for the A beta peptides in most of the described structures. There are certain variations in different hairpin conformations, for example regarding H-bonding partners, which could be one reason for the molecular heterogeneity observed in the aggregated systems. Interacting hairpins are the building blocks of the insoluble fibrils, again with variations in how hairpins are organized in the cross-section of the fibril, perpendicular to the fibril axis. The secondary structure propensities can be seen already in peptide monomers in solution. Unfortunately, detailed structural information about the intermediate oligomeric states is presently not available. In the review, special attention is given to metal ion interactions, particularly the binding constants and ligand structures of A beta complexes with Cu(II) and Zn(II), since these ions affect the aggregation process(es) and are considered to be involved in the molecular mechanisms underlying AD pathology.
650	7	a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
653		a Alzheimer's disease
653		a Amyloid beta peptide
653		a Hairpin
653		a Protein aggregation
653		a Neurotoxicity
700	1	a Abrahams, Jan Pieter4 aut
700	1	a Danielsson, Jensu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)jedan
700	1	a Gräslund, Astridu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)astrid
700	1	a Jarvet, Juriu Stockholms universitet,Institutionen för biokemi och biofysik,National Institute of Chemical Physics and Biophysics, Estonia4 aut0 (Swepub:su)jyri
700	1	a Luo, Jinghui4 aut
700	1	a Tiiman, Annu Stockholms universitet,Institutionen för biokemi och biofysik4 aut0 (Swepub:su)atiim
700	1	a Wärmländer, Sebastian K. T. S.4 aut
710	2	a Stockholms universitetb Institutionen för biokemi och biofysik4 org
773	0	t Journal of Biological Inorganic Chemistryd : Springer Science and Business Media LLCg 19:4-5, s. 623-634q 19:4-5<623-634x 0949-8257x 1432-1327
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-105411
856	4 8	u https://doi.org/10.1007/s00775-014-1131-8

Hitta via bibliotek

Journal of Biological Inorganic Chemistry (Sök värdpublikationen i LIBRIS)

Till lärosätets databas

Hitta mer i SwePub

Av författaren/redakt...: Abelein, Axel; Abrahams, Jan Pi ...; Danielsson, Jens; Gräslund, Astrid; Jarvet, Juri; Luo, Jinghui; visa fler...; Tiiman, Ann; Wärmländer, Seba ...; visa färre...

Om ämnet

NATURVETENSKAP: NATURVETENSKAP; och Biologi; och Biokemi och mole ...

Artiklar i publikationen: Journal of Biolo ...

Av lärosätet: Stockholms universitet

Sök utanför SwePub

Sök vidare i:: Google; Google Book Search; Google Scholar

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

LIBRIS.kb.se