Zobrazeno 1 - 10
of 253
pro vyhledávání: '"E. Hansmann"'
Publikováno v:
ACS Omega, Vol 6, Iss 8, Pp 5795-5804 (2021)
Externí odkaz:
https://doaj.org/article/a31ab81447a54a28b24b654a9a44045f
Publikováno v:
ACS Omega, Vol 5, Iss 38, Pp 24854-24863 (2020)
Externí odkaz:
https://doaj.org/article/9fe8ceeae6924d729e099af788571791
Publikováno v:
ACS Omega, Vol 3, Iss 11, Pp 16184-16190 (2018)
Externí odkaz:
https://doaj.org/article/d07ae291caa84f32906641dc50c46122
Autor:
Wenhui Xi, Ulrich H. E. Hansmann
Publikováno v:
Scientific Reports, Vol 7, Iss 1, Pp 1-14 (2017)
Abstract When assembling as fibrils Aβ40 peptides can only assume U-shaped conformations while Aβ42 can also arrange as S-shaped three-stranded chains. We show that this allows Aβ42 peptides to assemble pore-like structures that may explain their
Externí odkaz:
https://doaj.org/article/686e3a39388349e3b3af1e48edb6fece
Publikováno v:
bioRxiv
J Phys Chem B
J Phys Chem B
Aggregates of α-synuclein are thought to be the disease-causing agent in Parkinson's disease. Various case studies have hinted at a correlation between COVID-19 and the onset of Parkinson's disease. For this reason, we use molecular dynamics simulat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4a963b0ddae26925aee4885351e93cd
https://pubmed.ncbi.nlm.nih.gov/35233574
https://pubmed.ncbi.nlm.nih.gov/35233574
Parkinson’s Disease is accompanied by presence of amyloids in the brain formed of α-synuclein chains. Correlation between COVID-19 and the onset of Parkinson’s disease let to the idea that amyloidogenic segments in SARS-COV-2 proteins can induce
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::abcb6dc578f5643f7bd933a1ed1e2cb3
https://doi.org/10.1101/2023.05.06.539715
https://doi.org/10.1101/2023.05.06.539715
Publikováno v:
The Journal of Physical Chemistry. B
A marker for the severeness and disease progress of COVID-19 is overexpression of serum amyloid A (SAA) to levels that in other diseases are associated with a risk for SAA amyloidosis. In order to understand whether SAA amyloidosis could also be a lo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::14eb6850a5910343ee67f18025274697
https://doi.org/10.1021/acs.jpcb.1c04871
https://doi.org/10.1021/acs.jpcb.1c04871
Autor:
Ulrich H. E. Hansmann, Wenhua Wang
Publikováno v:
J Phys Chem B
In systemic amyloidosis, Serum amyloid A (SAA) fibril deposits cause widespread damages to tissues and organs that eventually may lead to death. A therapeutically intervention therefore has either to dissolve these fibrils or inhibit their formation.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bcf65c37bda9e95539ba288e979c7f17
https://doi.org/10.1021/acs.jpcb.0c08280
https://doi.org/10.1021/acs.jpcb.0c08280
Publikováno v:
ACS Omega, Vol 5, Iss 38, Pp 24854-24863 (2020)
The growing bacterial resistance to available antibiotics makes it necessary to look for new drug candidates. An example is a lanthionine-containing nisin, which has a broad spectrum of antimicrobial activity. While nisin is widely utilized as a food
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::99675425971033baf8a2a02ee4e48f75
https://doi.org/10.1021/acsomega.0c03594
https://doi.org/10.1021/acsomega.0c03594
Publikováno v:
J Chem Theory Comput
Motivated by the role that amylin aggregates play in type-II diabetes, we compare the stability of regular amylin fibrils with the stability of fibrils where l-amino acid chains are replaced by d-retro inverso (DRI) amylin, that is, peptides where th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::150a888545dbcbbd1010ec856d0af8fc
https://doi.org/10.1021/acs.jctc.0c00523
https://doi.org/10.1021/acs.jctc.0c00523