Alexander Buntru
Overview
Explore the profile of Alexander Buntru including associated specialties, affiliations and a list of published articles.
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21
Citations
344
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Recent Articles
1.
Secker C, Motzny A, Kostova S, Buntru A, Helmecke L, Reus L, et al.
J Neurochem
. 2023 May;
166(2):294-317.
PMID: 37165774
The accumulation of amyloidogenic protein aggregates in neurons is a pathogenic hallmark of a large number of neurodegenerative diseases including Alzheimer's disease (AD). Small molecules targeting such structures and promoting...
2.
Scior A, Arnsburg K, Iburg M, Juenemann K, Pigazzini M, Mlody B, et al.
EMBO J
. 2021 Oct;
40(19):e109413.
PMID: 34605047
No abstract available.
3.
Wiglenda T, Groenke N, Hoffmann W, Manz C, Diez L, Buntru A, et al.
J Mol Biol
. 2020 Feb;
432(7):2080-2098.
PMID: 32061932
The self-assembly of the 42-residue amyloid-β peptide, Aβ42, into fibrillar aggregates is associated with neuronal dysfunction and toxicity in Alzheimer's disease (AD) patient brains, suggesting that small molecules acting on...
4.
Boeddrich A, Babila J, Wiglenda T, Diez L, Jacob M, Nietfeld W, et al.
Cell Chem Biol
. 2018 Nov;
26(1):109-120.e7.
PMID: 30472115
Self-propagating amyloid-β (Aβ) aggregates or seeds possibly drive pathogenesis of Alzheimer's disease (AD). Small molecules targeting such structures might act therapeutically in vivo. Here, a fluorescence polarization assay was established...
5.
Ast A, Buntru A, Schindler F, Hasenkopf R, Schulz A, Brusendorf L, et al.
Mol Cell
. 2018 Sep;
71(5):675-688.e6.
PMID: 30193095
Self-propagating, amyloidogenic mutant huntingtin (mHTT) aggregates may drive progression of Huntington's disease (HD). Here, we report the development of a FRET-based mHTT aggregate seeding (FRASE) assay that enables the quantification...
6.
Trepte P, Kruse S, Kostova S, Hoffmann S, Buntru A, Tempelmeier A, et al.
Mol Syst Biol
. 2018 Jul;
14(7):e8071.
PMID: 29997244
Information on protein-protein interactions (PPIs) is of critical importance for studying complex biological systems and developing therapeutic strategies. Here, we present a double-readout bioluminescence-based two-hybrid technology, termed LuTHy, which provides...
7.
Ast A, Schindler F, Buntru A, Schnoegl S, Wanker E
Methods Mol Biol
. 2018 Jun;
1780:31-40.
PMID: 29856013
N-terminal mutant huntingtin (mHTT) fragments with pathogenic polyglutamine (polyQ) tracts spontaneously form stable, amyloidogenic protein aggregates with a fibrillar morphology. Such structures are detectable in brains of Huntington's disease (HD)...
8.
Wagner A, Politi A, Ast A, Bravo-Rodriguez K, Baum K, Buntru A, et al.
J Mol Biol
. 2018 Mar;
430(12):1725-1744.
PMID: 29601786
Huntingtin (HTT) fragments with extended polyglutamine tracts self-assemble into amyloid-like fibrillar aggregates. Elucidating the fibril formation mechanism is critical for understanding Huntington's disease pathology and for developing novel therapeutic strategies....
9.
Matthes F, Hettich M, Schilling J, Flores-Dominguez D, Blank N, Wiglenda T, et al.
Cell Death Discov
. 2018 Mar;
4:4.
PMID: 29531801
Alzheimer's disease (AD) is characterized by two neuropathological hallmarks: senile plaques, which are composed of amyloid-β (Aβ) peptides, and neurofibrillary tangles, which are composed of hyperphosphorylated tau protein. Aβ peptides...
10.
Scior A, Buntru A, Arnsburg K, Ast A, Iburg M, Juenemann K, et al.
EMBO J
. 2017 Dec;
37(2):282-299.
PMID: 29212816
Huntington's disease (HD) is a neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin gene (). Molecular chaperones have been implicated in suppressing or delaying the aggregation...