Zobrazeno 1 - 10
of 45
pro vyhledávání: '"Axel Abelein"'
Autor:
Rakesh Kumar, Tanguy Le Marchand, Laurène Adam, Raitis Bobrovs, Gefei Chen, Jēkabs Fridmanis, Nina Kronqvist, Henrik Biverstål, Kristaps Jaudzems, Jan Johansson, Guido Pintacuda, Axel Abelein
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-10 (2024)
Abstract Protein misfolding can generate toxic intermediates, which underlies several devastating diseases, such as Alzheimer’s disease (AD). The surface of AD-associated amyloid-β peptide (Aβ) fibrils has been suggested to act as a catalyzer for
Externí odkaz:
https://doaj.org/article/417265d7196a4cdfa85435dbb85fcbd1
Autor:
Gefei Chen, Axel Leppert, Helen Poska, Harriet E. Nilsson, Carlos Piedrafita Alvira, Xueying Zhong, Philip Koeck, Caroline Jegerschöld, Axel Abelein, Hans Hebert, Jan Johansson
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-8 (2023)
Abstract ATP-independent molecular chaperones are important for maintaining cellular fitness but the molecular determinants for preventing aggregation of partly unfolded protein substrates remain unclear, particularly regarding assembly state and bas
Externí odkaz:
https://doaj.org/article/71ccbc7cbdc84d0cba35d704c18e4cb9
Autor:
Tina Arndt, Kristaps Jaudzems, Olga Shilkova, Juanita Francis, Mathias Johansson, Peter R. Laity, Cagla Sahin, Urmimala Chatterjee, Nina Kronqvist, Edgar Barajas-Ledesma, Rakesh Kumar, Gefei Chen, Roger Strömberg, Axel Abelein, Maud Langton, Michael Landreh, Andreas Barth, Chris Holland, Jan Johansson, Anna Rising
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
Recombinant spider silks are of interest but the multimodal and aggregation-prone nature of them is a limitation. Here, the authors report on a miniature spidroin based on the N-terminal domain which forms a hydrogel at 37 °C which allows for ease o
Externí odkaz:
https://doaj.org/article/797818a67a6f4d898230e24aa54af69c
Autor:
Richeng Jiang, Una Smailovic, Hazal Haytural, Betty M. Tijms, Hao Li, Robert Mihai Haret, Ganna Shevchenko, Gefei Chen, Axel Abelein, Johan Gobom, Susanne Frykman, Misaki Sekiguchi, Ryo Fujioka, Naoto Watamura, Hiroki Sasaguri, Sofie Nyström, Per Hammarström, Takaomi C. Saido, Vesna Jelic, Stina Syvänen, Henrik Zetterberg, Bengt Winblad, Jonas Bergquist, Pieter Jelle Visser, Per Nilsson
Publikováno v:
Acta Neuropathologica Communications, Vol 10, Iss 1, Pp 1-17 (2022)
Abstract Cerebrospinal fluid (CSF) biomarkers play an important role in diagnosing Alzheimer’s disease (AD) which is characterized by amyloid-β (Aβ) amyloidosis. Here, we used two App knock-in mouse models, App NL-F/NL-F and App NL-G-F/NL-G-F , e
Externí odkaz:
https://doaj.org/article/de02c2b3c0b44a69941ed429ae504a9a
Autor:
Carmen Peña-Bautista, Rakesh Kumar, Miguel Baquero, Jan Johansson, Consuelo Cháfer-Pericás, Axel Abelein, Daniel Ferreira
Publikováno v:
Frontiers in Molecular Biosciences, Vol 10 (2023)
Introduction: Dementia with Lewy Bodies (DLB) is the second most common cause of neurodegenerative dementia after Alzheimer’s disease (AD), but the field is still lacking a specific biomarker for its core pathology: alpha synuclein (α-syn). Realti
Externí odkaz:
https://doaj.org/article/489490a372ab4021b2a8b418020cff66
Autor:
Richeng Jiang, Makoto Shimozawa, Johanna Mayer, Simone Tambaro, Rakesh Kumar, Axel Abelein, Bengt Winblad, Nenad Bogdanovic, Per Nilsson
Publikováno v:
Frontiers in Aging Neuroscience, Vol 14 (2022)
Alzheimer’s disease (AD) is characterized by impaired protein homeostasis leading to amyloid-β peptide (Aβ) amyloidosis. Amyloid precursor protein (APP) knock-in mice exhibit robust Aβ pathology, providing possibilities to determine its effect o
Externí odkaz:
https://doaj.org/article/5bdec84212d44e5484c5d22672a15608
Autor:
Henrik Biverstål, Rakesh Kumar, Anna Katharina Schellhaus, Médoune Sarr, Nico P. Dantuma, Axel Abelein, Jan Johansson
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-9 (2020)
Abstract Amyloid fibrils are mechanically robust and partly resistant to proteolytic degradation, making them potential candidates for scaffold materials in cell culture, tissue engineering, drug delivery and other applications. Such applications of
Externí odkaz:
https://doaj.org/article/b9caf7651d644f00969a609d822c2cf9
Autor:
Gefei Chen, Axel Abelein, Harriet E. Nilsson, Axel Leppert, Yuniesky Andrade-Talavera, Simone Tambaro, Lovisa Hemmingsson, Firoz Roshan, Michael Landreh, Henrik Biverstål, Philip J. B. Koeck, Jenny Presto, Hans Hebert, André Fisahn, Jan Johansson
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-14 (2017)
The BRICHOS domain is a chaperone that can act against amyloid-β peptide fibril formation and non-fibrillar protein aggregation. Here the authors use a multidisciplinary approach and show that the Bri2 BRICHOS domain has qualitatively different chap
Externí odkaz:
https://doaj.org/article/54f4eca3feec44a6b3d1e292c044e1a5
Autor:
Shaffi Manchanda, Lorena Galan-Acosta, Axel Abelein, Simone Tambaro, Gefei Chen, Per Nilsson, Jan Johansson
Publikováno v:
Molecular Therapy. 31:487-502
Attempts to treat Alzheimer's disease with immunotherapy against the β-amyloid (Aβ) peptide or with enzyme inhibitors to reduce Aβ production have not yet resulted in effective treatment, suggesting that alternative strategies may be useful. Here
Autor:
Axel Abelein, Jan Johansson
Publikováno v:
RSC Medicinal Chemistry. 14:848-857
Molecular chaperones are important components in the cellular quality-control machinery and increasing evidence points to potential new roles for them as suppressors of amyloid formation in neurodegenerative diseases, such as Alzheimers disease.