Zobrazeno 1 - 10
of 117
pro vyhledávání: '"Giovanni, Maglia"'
Autor:
Nicole Stéphanie Galenkamp, Sarah Zernia, Yulan B. Van Oppen, Marco van den Noort, Andreas Milias Argeitis, Giovanni Maglia
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-13 (2024)
Abstract Enzymatic mechanisms are typically inferred from structural data. However, understanding enzymes require unravelling the intricate dynamic interplay between dynamics, conformational substates, and multiple protein structures. Here, we use si
Externí odkaz:
https://doaj.org/article/2ca5a11c0f8d47b9b521e22c2c6c2630
Autor:
Gonçalo Paulo, Ke Sun, Giovanni Di Muccio, Alberto Gubbiotti, Blasco Morozzo della Rocca, Jia Geng, Giovanni Maglia, Mauro Chinappi, Alberto Giacomello
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-9 (2023)
Abstract Signal transmission in the brain relies on voltage-gated ion channels, which exhibit the electrical behaviour of memristors, resistors with memory. State-of-the-art technologies currently employ semiconductor-based neuromorphic approaches, w
Externí odkaz:
https://doaj.org/article/2fba14ff007c46dca0f38667d83ed91c
Autor:
Florian Leonardus Rudolfus Lucas, Roderick Corstiaan Abraham Versloot, Liubov Yakovlieva, Marthe T. C. Walvoort, Giovanni Maglia
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Peptide mass fingerprinting is a traditional approach for protein identification by mass spectrometry. Here, the authors provide evidence that peptide mass fingerprinting is also feasible using FraC nanopores, demonstrating protein identification bas
Externí odkaz:
https://doaj.org/article/33975afdc6084301a4bdb1ecb96cd3c1
Autor:
Sonia Ciudad, Eduard Puig, Thomas Botzanowski, Moeen Meigooni, Andres S. Arango, Jimmy Do, Maxim Mayzel, Mariam Bayoumi, Stéphane Chaignepain, Giovanni Maglia, Sarah Cianferani, Vladislav Orekhov, Emad Tajkhorshid, Benjamin Bardiaux, Natàlia Carulla
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Formation of amyloid-beta (Aβ) oligomer pores in the membrane of neurons has been proposed to explain neurotoxicity in Alzheimer´s disease. Here authors present the 3D- structure of an Aβ oligomer formed in a membrane mimicking environment and obs
Externí odkaz:
https://doaj.org/article/2c0e9ea1270e440fb213d992e9ac74ae
Publikováno v:
iScience, Vol 24, Iss 10, Pp 103202- (2021)
Summary: The identification of proteins at the single-molecule level would open exciting new venues in biological research and disease diagnostics. Previously, we proposed a nanopore-based method for protein identification called chop-n-drop fingerpr
Externí odkaz:
https://doaj.org/article/1459d94bd34b4a7e8479868efe5620ba
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Using Fragaceatoxin C nanopores to study peptides below 1.6 kDa is challenging. Here the authors demonstrate that nanopores can be engineered to different sizes to detect a range of peptide lengths below the previous resolution limit, and show that t
Externí odkaz:
https://doaj.org/article/09dd1600d7044d409d1462d825c5945f
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-8 (2018)
Protein nanopores are emerging as sensors for a variety of biomolecules. Here the authors develop a nanopore based on the bacterial toxin ClyA, in conjunction with binding proteins for glucose and asparagine, to detect these biomolecules simultaneous
Externí odkaz:
https://doaj.org/article/f5d06fa761e34c8ab22f09254e397e18
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
Biological nanopore–based protein sequencing and recognition is challenging due to the folded structure or non-uniform charge of peptides. Here the authors show that engineered FraC nanopores can overcome these problems and recognize biomarkers in
Externí odkaz:
https://doaj.org/article/229ceae5404f44ed83b8b5d44da50e41
Autor:
Yi-Lun Ying, Zheng-Li Hu, Shengli Zhang, Yujia Qing, Alessio Fragasso, Giovanni Maglia, Amit Meller, Hagan Bayley, Cees Dekker, Yi-Tao Long
Publikováno v:
Nature Nanotechnology. 17:1136-1146
Inspired by the biological processes of molecular recognition and transportation across membranes, nanopore techniques have evolved in recent decades as ultrasensitive analytical tools for individual molecules. In particular, nanopore-based single-mo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::efd40bcbd91f24aec5745fd826b74f6f
https://doi.org/10.1038/s41565-022-01193-2
https://doi.org/10.1038/s41565-022-01193-2
Autor:
Roderick Corstiaan Abraham Versloot, Florian Leonardus Rudolfus Lucas, Liubov Yakovlieva, Matthijs Jonathan Tadema, Yurui Zhang, Thomas M. Wood, Nathaniel I. Martin, Siewert J. Marrink, Marthe T. C. Walvoort, Giovanni Maglia
Publikováno v:
Nano Letters, 22(13), 5357-5364. AMER CHEMICAL SOC
Nano Letters, 22(13):2c10338, 5357-5364. AMER CHEMICAL SOC
Nano Letters, 22(13):2c10338, 5357-5364. AMER CHEMICAL SOC
Although nanopores can be used for single-molecule sequencing of nucleic acids using low-cost portable devices, the characterization of proteins and their modifications has yet to be established. Here, we show that hydrophilic or glycosylated peptide
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::49e80f64f809e1a676f658066af5737a
https://hdl.handle.net/11370/d6debc45-1bb0-404b-a787-03da36373758
https://hdl.handle.net/11370/d6debc45-1bb0-404b-a787-03da36373758