Zobrazeno 1 - 10
of 151
pro vyhledávání: '"Marcus Fändrich"'
Autor:
Sara Karimi-Farsijani, Peter Benedikt Pfeiffer, Sambhasan Banerjee, Julian Baur, Lukas Kuhn, Niklas Kupfer, Ute Hegenbart, Stefan O. Schönland, Sebastian Wiese, Christian Haupt, Matthias Schmidt, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-8 (2024)
Abstract Systemic AL amyloidosis is one of the most frequently diagnosed forms of systemic amyloidosis. It arises from mutational changes in immunoglobulin light chains. To explore whether these mutations may affect the structure of the formed fibril
Externí odkaz:
https://doaj.org/article/a8a7533f549f4f7b811b7eb83658803c
Autor:
Kartikay Sharma, Fabian Stockert, Jayakrishna Shenoy, Mélanie Berbon, Muhammed Bilal Abdul-Shukkoor, Birgit Habenstein, Antoine Loquet, Matthias Schmidt, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-8 (2024)
Abstract The transactive response DNA-binding protein-43 (TDP-43) is a multi-facet protein involved in phase separation, RNA-binding, and alternative splicing. In the context of neurodegenerative diseases, abnormal aggregation of TDP-43 has been link
Externí odkaz:
https://doaj.org/article/90078a7b880444ff872f24cf7af02b54
Autor:
Maximilian Steinebrei, Julian Baur, Anaviggha Pradhan, Niklas Kupfer, Sebastian Wiese, Ute Hegenbart, Stefan O. Schönland, Matthias Schmidt, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-8 (2023)
Abstract Systemic ATTR amyloidosis is an increasingly important protein misfolding disease that is provoked by the formation of amyloid fibrils from transthyretin protein. The pathological and clinical disease manifestations and the number of pathoge
Externí odkaz:
https://doaj.org/article/5116ea104f544636b03e07517f2cc3ed
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-8 (2023)
Abstract Amyloid fibrils have emerged as innovative tools to enhance the transduction efficiency of retroviral vectors in gene therapy strategies. In this study, we used cryo-electron microscopy to analyze the structure of a biotechnologically engine
Externí odkaz:
https://doaj.org/article/e31f43f0213d4f06865cd6238d6a6ca0
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-8 (2023)
Abstract Catalytic amyloid fibrils are novel types of bioinspired, functional materials that combine the chemical and mechanical robustness of amyloids with the ability to catalyze a certain chemical reaction. In this study we used cryo-electron micr
Externí odkaz:
https://doaj.org/article/07a71786ea894a84a03b83e572a9d05b
Autor:
Matthias Weber, Matthias Neumann, Matthias Schmidt, Peter Benedikt Pfeiffer, Akanksha Bansal, Marcus Fändrich, Volker Schmidt
Publikováno v:
Journal of Mathematics in Industry, Vol 13, Iss 1, Pp 1-11 (2023)
Abstract Fast assessment of the composition of amyloid fibril samples from cryo-EM data poses a serious challenge to existing image analysis tools. We develop a method for automated segmentation of single fibrils requiring only little user input duri
Externí odkaz:
https://doaj.org/article/f34184b1d8f04664acd7bbb827ec4d4c
Publikováno v:
Journal of Lipid Research, Vol 64, Iss 9, Pp 100429- (2023)
Serum amyloid A (SAA) is named after a life-threatening disease, yet this small evolutionarily conserved protein must have played a vital role in host defense. Most circulating SAA binds plasma lipoproteins and modulates their metabolism. However, th
Externí odkaz:
https://doaj.org/article/12c731a8521740bcbc1ee776f61a770c
Autor:
Sambhasan Banerjee, Julian Baur, Christoph Daniel, Peter Benedikt Pfeiffer, Manuel Hitzenberger, Lukas Kuhn, Sebastian Wiese, Johan Bijzet, Christian Haupt, Kerstin U. Amann, Martin Zacharias, Bouke P. C. Hazenberg, Gunilla T. Westermark, Matthias Schmidt, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-8 (2022)
This study reports the cryo-EM structures of AA amyloid fibrils from two patients with vascular AA amyloidosis. The findings imply that different disease variants in systemic amyloidosis are associated with different fibril structures.
Externí odkaz:
https://doaj.org/article/fd89d36ae1bf491c9c3cac4bac147e6d
Autor:
Thomas Heerde, Matthies Rennegarbe, Alexander Biedermann, Dilan Savran, Peter B. Pfeiffer, Manuel Hitzenberger, Julian Baur, Ioana Puscalau-Girtu, Martin Zacharias, Nadine Schwierz, Christian Haupt, Matthias Schmidt, Marcus Fändrich
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-8 (2022)
Here, the authors present the cryo-EM structure of in vitro amyloid fibrils from recombinant SAA1.1 protein that were formed by seeding with fibrils purified from systemic AA amyloidosis tissue. This in vitro fibril structure resembles the structure
Externí odkaz:
https://doaj.org/article/1dc8229b0dcb4b2fa12efbe783d6a181
Autor:
Verena Vogel, Richard Bauer, Stefanie Mauerer, Nicole Schiffelholz, Christian Haupt, Gerd M. Seibold, Marcus Fändrich, Paul Walther, Barbara Spellerberg
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-16 (2021)
Abstract As a conserved defense mechanism, many bacteria produce antimicrobial peptides, called bacteriocins, which provide a colonization advantage in a multispecies environment. Here the first bacteriocin of Streptococcus anginosus, designated Angi
Externí odkaz:
https://doaj.org/article/b730360628344a0f985b95b04ae34d00