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  1. Article ; Online: Altering the Solubility of the Antibiotic Candidate NisinA Computational Study

    Preeti Pandey / Ulrich H. E. Hansmann / Feng Wang

    ACS Omega, Vol 5, Iss 38, Pp 24854-

    2020  Volume 24863

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2020-09-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: Effect of Lauric Acid on the Stability of Aβ42 Oligomers

    Prabir Khatua / Asis K. Jana / Ulrich H. E. Hansmann

    ACS Omega, Vol 6, Iss 8, Pp 5795-

    2021  Volume 5804

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2021-02-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Stability of the N‑Terminal Helix and Its Role in Amyloid Formation of Serum Amyloid A

    Wenhua Wang / Wenhui Xi / Ulrich H. E. Hansmann

    ACS Omega, Vol 3, Iss 11, Pp 16184-

    2018  Volume 16190

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2018-11-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Ring-like N-fold Models of Aβ42 fibrils

    Wenhui Xi / Ulrich H. E. Hansmann

    Scientific Reports, Vol 7, Iss 1, Pp 1-

    2017  Volume 14

    Abstract: 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 higher ... ...

    Abstract 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 higher toxicity. For this purpose, we develop a scalable model of ring-like assemblies of S-shaped Aβ1–42 chains and study the stability and structural properties of these assemblies through atomistic molecular dynamics simulations. We find that the proposed arrangements are in size and symmetry compatible with experimentally observed Aβ assemblies. We further show that the interior pore in our models allows for water leakage as a possible mechanism of cell toxicity of Aβ42 amyloids.
    Keywords Medicine ; R ; Science ; Q
    Language English
    Publishing date 2017-07-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Mutations Alter RNA-Mediated Conversion of Human Prions

    Erik J. Alred / Izra Lodangco / Jennifer Gallaher / Ulrich H.E. Hansmann

    ACS Omega, Vol 3, Iss 4, Pp 3936-

    2018  Volume 3944

    Keywords Chemistry ; QD1-999
    Language English
    Publishing date 2018-04-01T00:00:00Z
    Publisher American Chemical Society
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Inter-species cross-seeding

    Workalemahu M Berhanu / Ulrich H E Hansmann

    PLoS ONE, Vol 9, Iss 5, p e

    stability and assembly of rat-human amylin aggregates.

    2014  Volume 97051

    Abstract: Diseases such as type 2 diabetes, Alzheimer's and Parkinson's share as common feature the accumulation of mis-folded disease-specific protein aggregates into fibrillar structures, or plaques. These fibrils may either be toxic by themselves, or act as ... ...

    Abstract Diseases such as type 2 diabetes, Alzheimer's and Parkinson's share as common feature the accumulation of mis-folded disease-specific protein aggregates into fibrillar structures, or plaques. These fibrils may either be toxic by themselves, or act as reservoirs for smaller cytotoxic oligomers. This suggests to investigate molecules as potential therapeutics that either reduce fibril formation or increase fibril stability. One example is rat amylin, which can inhibit aggregation of human amylin, a hallmark of type 2 diabetes. In the present paper, we use molecular dynamics to compare the stability of various preformed aggregates, built out of either human amylin, rat amylin, or mixtures of both. We considered two types of fibril-like oligomers: a single-layer in-register conformation, and a double-layer conformation in which the first U-shaped layer consists of rat amylin and the second layer of human amylin. Our results explain the weak amyloid-inhibiting properties of rat amylin and suggest that membrane leakage due to pore formation is responsible for the toxicity of rat amylin observed in a recent experiment. Together, our results put in question the use of rat amylin or the similar FDA approved drug pramlintide as an inhibitor of human amylin aggregation. They also point to mixed human-rat amylin fibril-like oligomers as possible model-systems for studies of amyloid formation that involve cross-species transmission.
    Keywords Medicine ; R ; Science ; Q
    Subject code 500
    Language English
    Publishing date 2014-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Structure and dynamics of amyloid-β segmental polymorphisms.

    Workalemahu M Berhanu / Ulrich H E Hansmann

    PLoS ONE, Vol 7, Iss 7, p e

    2012  Volume 41479

    Abstract: It is believed that amyloid-beta (Aβ) aggregates play a role in the pathogenesis of Alzheimer's disease. Aβ molecules form β-sheet structures with multiple interaction sites. This polymorphism gives rise to differences in morphology, physico-chemical ... ...

    Abstract It is believed that amyloid-beta (Aβ) aggregates play a role in the pathogenesis of Alzheimer's disease. Aβ molecules form β-sheet structures with multiple interaction sites. This polymorphism gives rise to differences in morphology, physico-chemical property and level of cellular toxicity. We have investigated the conformational stability of various segmental polymorphisms using molecular dynamics simulations and find that the segmental polymorphic models of Aβ retain a U-shaped architecture. Our results demonstrate the importance of inter-sheet side chain-side chain contacts, hydrophobic contacts among the strands (β1 and β2) and of salt bridges in stabilizing the aggregates. Residues in β-sheet regions have smaller fluctuation while those at the edge and loop region are more mobile. The inter-peptide salt bridges between Asp23 and Lys28 are strong compared to intra-chain salt bridge and there is an exchange of the inter-chain salt-bridge with intra-chain salt bridge. As our results suggest that Aβ exists under physiological conditions as an ensemble of distinct segmental polymorphs, it may be necessary to account in the development of therapeutics for Alzheimer's disease the differences in structural stability and aggregation behavior of the various Aβ polymorphic forms.
    Keywords Medicine ; R ; Science ; Q
    Subject code 612
    Language English
    Publishing date 2012-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Structural transitions in biomolecules - a numerical comparison of two approaches for the study of phase transitions in small systems

    Yong Peng / Ulrich H.E. Hansmann / Nelson A. Alves

    International Journal of Molecular Sciences, Vol 3, Iss 1, Pp 17-

    2002  Volume 29

    Abstract: Abstract: We compare two recently proposed methods for the characterization of phase transitions in small systems. The usefulness of these techniques is evaluated for the case of structural transition in alanine-based peptides. ...

    Abstract Abstract: We compare two recently proposed methods for the characterization of phase transitions in small systems. The usefulness of these techniques is evaluated for the case of structural transition in alanine-based peptides.
    Keywords Phase transitions ; Critical exponents ; Partition function zeros ; Helix-coil transition ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
    Language English
    Publishing date 2002-01-01T00:00:00Z
    Publisher MDPI AG
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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