Please use this identifier to cite or link to this item:
http://doi.org/10.25358/openscience-4877Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Endres, Kristina | - |
| dc.date.accessioned | 2020-06-10T12:39:55Z | - |
| dc.date.available | 2020-06-10T14:39:55Z | - |
| dc.date.issued | 2020 | - |
| dc.identifier.uri | https://openscience.ub.uni-mainz.de/handle/20.500.12030/4880 | - |
| dc.description.abstract | The term “amyloid” refers to proteinaceous deposits of peptides that might be generated from larger precursor proteins e.g., by proteolysis. Common to these peptides is a stable cross-β dominated secondary structure which allows self-assembly, leading to insoluble oligomers and lastly to fibrils. These highly ordered protein aggregates have been, for a long time, mainly associated with human neurodegenerative diseases such as Alzheimer’s disease (Amyloid-β peptides). However, they also exert physiological functions such as in release of deposited hormones in human beings. In the light of the rediscovery of our microbial commensals as important companions in health and disease, the fact that microbes also possess amyloidogenic peptides is intriguing. Transmission of amyloids by iatrogenic means or by consumption of contaminated meat from diseased animals is a well-known fact. What if also our microbial commensals might drive human amyloidosis or suffer from our aggregated amyloids? Moreover, as the microbial amyloids are evolutionarily older, we might learn from these organisms how to cope with the sword of Damocles forged of endogenous, potentially toxic peptides. This review summarizes knowledge about the interplay between human amyloids involved in neurodegenerative diseases and microbial amyloids. Keywords: amyloid; Alzheimer’s disease; biofilm; neurodegeneration; microbiota; Parkinson’s disease | en_GB |
| dc.description.sponsorship | DFG, Open Access-Publizieren Universität Mainz / Universitätsmedizin | - |
| dc.language.iso | eng | - |
| dc.rights | CC BY | de_DE |
| dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | - |
| dc.subject.ddc | 610 Medizin | de_DE |
| dc.subject.ddc | 610 Medical sciences | en_GB |
| dc.title | Amyloidogenic peptides in human neuro-degenerative diseases and in microorganisms : a sorrow shared is a sorrow halved? | en_GB |
| dc.type | Zeitschriftenaufsatz | de_DE |
| dc.identifier.urn | urn:nbn:de:hebis:77-publ-598661 | - |
| dc.identifier.doi | http://doi.org/10.25358/openscience-4877 | - |
| jgu.type.dinitype | article | - |
| jgu.type.version | Published version | en_GB |
| jgu.type.resource | Text | - |
| jgu.organisation.department | FB 04 Medizin | - |
| jgu.organisation.number | 2700 | - |
| jgu.organisation.name | Johannes Gutenberg-Universität Mainz | - |
| jgu.rights.accessrights | openAccess | - |
| jgu.journal.title | Molecules | - |
| jgu.journal.volume | 25 | - |
| jgu.journal.issue | 4 | - |
| jgu.pages.alternative | Art. 925 | - |
| jgu.publisher.year | 2020 | - |
| jgu.publisher.name | MDPI | - |
| jgu.publisher.place | Basel | - |
| jgu.publisher.uri | http://dx.doi.org/10.3390/molecules25040925 | - |
| jgu.publisher.issn | 1420-3049 | - |
| jgu.organisation.place | Mainz | - |
| jgu.subject.ddccode | 610 | - |
| opus.date.accessioned | 2020-06-10T12:39:55Z | - |
| opus.date.modified | 2020-06-29T08:48:02Z | - |
| opus.date.available | 2020-06-10T14:39:55 | - |
| opus.subject.dfgcode | 00-000 | - |
| opus.organisation.string | FB 04: Medizin: Klinik für Psychiatrie und Psychotherapie | de_DE |
| opus.identifier.opusid | 59866 | - |
| opus.institute.number | 0472 | - |
| opus.metadataonly | false | - |
| opus.type.contenttype | Keine | de_DE |
| opus.type.contenttype | None | en_GB |
| opus.affiliated | Endres, Kristina | - |
| jgu.publisher.doi | 10.3390/molecules25040925 | |
| jgu.organisation.ror | https://ror.org/023b0x485 | |
| Appears in collections: | JGU-Publikationen | |
