WFRF:(Chen Zihan)
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| Fältnamn | Indikatorer | Metadata |
|---|---|---|
| 000 | 06076naa a2200589 4500 | |
| 001 | oai:DiVA.org:umu-212398 | |
| 003 | SwePub | |
| 008 | 230731s2023 | |||||||||||000 ||eng| | |
| 009 | oai:prod.swepub.kib.ki.se:153318103 | |
| 024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-2123982 URI |
| 024 | 7 | a https://doi.org/10.1002/smll.2023040312 DOI |
| 024 | 7 | a http://kipublications.ki.se/Default.aspx?queryparsed=id:1533181032 URI |
| 040 | a (SwePub)umud (SwePub)ki | |
| 041 | a engb eng | |
| 042 | 9 SwePub | |
| 072 | 7 | a ref2 swepub-contenttype |
| 072 | 7 | a art2 swepub-publicationtype |
| 100 | 1 | a Qi, Xingmeiu The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut |
| 245 | 1 0 | a Spider silk protein forms amyloid-like nanofibrils through a non-nucleation-dependent polymerization mechanism |
| 264 | 1 | b John Wiley & Sons,c 2023 |
| 338 | a electronic2 rdacarrier | |
| 520 | a Amyloid fibrils—nanoscale fibrillar aggregates with high levels of order—are pathogenic in some today incurable human diseases; however, there are also many physiologically functioning amyloids in nature. The process of amyloid formation is typically nucleation-elongation-dependent, as exemplified by the pathogenic amyloid-β peptide (Aβ) that is associated with Alzheimer's disease. Spider silk, one of the toughest biomaterials, shares characteristics with amyloid. In this study, it is shown that forming amyloid-like nanofibrils is an inherent property preserved by various spider silk proteins (spidroins). Both spidroins and Aβ capped by spidroin N- and C-terminal domains, can assemble into macroscopic spider silk-like fibers that consist of straight nanofibrils parallel to the fiber axis as observed in native spider silk. While Aβ forms amyloid nanofibrils through a nucleation-dependent pathway and exhibits strong cytotoxicity and seeding effects, spidroins spontaneously and rapidly form amyloid-like nanofibrils via a non-nucleation-dependent polymerization pathway that involves lateral packing of fibrils. Spidroin nanofibrils share amyloid-like properties but lack strong cytotoxicity and the ability to self-seed or cross-seed human amyloidogenic peptides. These results suggest that spidroins' unique primary structures have evolved to allow functional properties of amyloid, and at the same time direct their fibrillization pathways to avoid formation of cytotoxic intermediates. | |
| 650 | 7 | a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe |
| 650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng |
| 653 | a cytotoxicity | |
| 653 | a nanofibril | |
| 653 | a non-nucleation-dependent polymerization | |
| 653 | a seeding | |
| 653 | a spidroin | |
| 700 | 1 | a Wang, Yuu Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; College of Wildlife and Protected Area, Northeast Forestry University, Harbin, China4 aut |
| 700 | 1 | a Yu, Hairuiu The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut |
| 700 | 1 | a Liu, Ruifangu The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut |
| 700 | 1 | a Leppert, Axelu Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Solna, Sweden4 aut |
| 700 | 1 | a Zheng, Zihanu Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; Department of Pharmacology, Xi'an Jiaotong University, Shaanxi, China4 aut |
| 700 | 1 | a Zhong, Xueyingu School of Engineering Sciences in Chemistry, Biotechnology and Health, Department of Biomedical Engineering and Health Systems, KTH Royal Institute of Technology, Huddinge, Sweden4 aut |
| 700 | 1 | a Jin, Zhenu Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; Department of Pharmacology, Xi'an Jiaotong University, Shaanxi, China4 aut |
| 700 | 1 | a Wang, Hanu The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut |
| 700 | 1 | a Li, Xiaoliu Department of Pharmacology, College of Pharmacy, Chongqing Medical University, Chongqing, China4 aut |
| 700 | 1 | a Wang, Xiuzheu Department of Neurology, Shanghai Sixth People's Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China4 aut |
| 700 | 1 | a Landreh, Michaelu Department of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Solna, Sweden4 aut |
| 700 | 1 | a Morozova-Roche, Ludmilla A.u Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut0 (Swepub:umu)lumo0001 |
| 700 | 1 | a Johansson, Janu Karolinska Institutet4 aut |
| 700 | 1 | a Xiong, Sidongu The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, China4 aut |
| 700 | 1 | a Iashchishyn, Igoru Umeå universitet,Institutionen för medicinsk kemi och biofysik4 aut0 (Swepub:umu)igia0001 |
| 700 | 1 | a Chen, Gefeiu Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden4 aut |
| 710 | 2 | a The Jiangsu Key Laboratory of Infection and Immunity, Institutes of Biology and Medical Sciences, Soochow University, Suzhou, Chinab Department of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden; College of Wildlife and Protected Area, Northeast Forestry University, Harbin, China4 org |
| 773 | 0 | t Smalld : John Wiley & Sonsg 18:46q 18:46x 1613-6810x 1613-6829 |
| 856 | 4 | u https://doi.org/10.1002/smll.202304031y Fulltext |
| 856 | 4 | u https://umu.diva-portal.org/smash/get/diva2:1784762/FULLTEXT02.pdfx primaryx Raw objecty fulltext:print |
| 856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-212398 |
| 856 | 4 8 | u https://doi.org/10.1002/smll.202304031 |
| 856 | 4 8 | u http://kipublications.ki.se/Default.aspx?queryparsed=id:153318103 |
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