Zobrazeno 1 - 10
of 60
pro vyhledávání: '"Membrane Proteins/chemistry"'
Autor:
Andrew P. Carpenter, Patricia Khuu, Tobias Weidner, Colin P. Johnson, Steven J. Roeters, Joe E. Baio
Publikováno v:
Carpenter, A P, Khuu, P, Weidner, T, Johnson, C P, Roeters, S J & Baio, J E 2023, ' Orientation of the Dysferlin C2A Domain is Responsive to the Composition of Lipid Membranes ', The journal of physical chemistry. B, vol. 127, no. 2, pp. 577-589 . https://doi.org/10.1021/acs.jpcb.2c06716
Dysferlin is a 230 kD protein that plays a critical function in the active resealing of micron-sized injuries to the muscle sarcolemma by recruiting vesicles to patch the injured site via vesicle fusion. Muscular dystrophy is observed in humans when
Autor:
Aniruddha Panda, Fabian Giska, Anna L. Duncan, Alexander J. Welch, Caroline Brown, Rachel McAllister, Parameswaran Hariharan, Jean N. D. Goder, Jeff Coleman, Sathish Ramakrishnan, Frédéric Pincet, Lan Guan, Shyam Krishnakumar, James E. Rothman, Kallol Gupta
Publikováno v:
Panda, A, Giska, F, Duncan, A L, Welch, A J, Brown, C, McAllister, R, Hariharan, P, Goder, J N D, Coleman, J, Ramakrishnan, S, Pincet, F, Guan, L, Krishnakumar, S, Rothman, J E & Gupta, K 2023, ' Direct determination of oligomeric organization of integral membrane proteins and lipids from intact customizable bilayer ', Nature Methods, vol. 20, no. 6, pp. 891-897 . https://doi.org/10.1038/s41592-023-01864-5
Hierarchical organization of integral membrane proteins (IMP) and lipids at the membrane is essential for regulating myriad downstream signaling. A quantitative understanding of these processes requires both detections of oligomeric organization of I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::32353ac527de672db3b090c2e035a260
https://doi.org/10.1101/2023.03.12.532274
https://doi.org/10.1101/2023.03.12.532274
Autor:
Cheol Jeong, Ryan Franklin, Karen J. Edler, Kenno Vanommeslaeghe, Susan Krueger, Joseph E. Curtis
Lipid nanodiscs can be used to solubilize functional membrane proteins (MPs) in nativelike environments. Thus, they are promising reagents that have been proven useful to characterize MPs. Both protein and non-protein molecular belts have shown promi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9b506e7d40e6fe57d475db8cd5d31002
https://doi.org/10.1021/acs.jpcb.1c05050
https://doi.org/10.1021/acs.jpcb.1c05050
Autor:
Pearce, Nicholas M, Gros, Piet, Sub Materials Chemistry and Catalysis, Sub Structural Biochemistry, Materials Chemistry and Catalysis, Structural Biochemistry
Publikováno v:
Pearce, N M & Gros, P 2021, ' A method for intuitively extracting macromolecular dynamics from structural disorder ', Nature Communications, vol. 12, no. 1, 5493, pp. 1-11 . https://doi.org/10.1038/s41467-021-25814-x
Nature Communications, 12(1), 1. Nature Publishing Group
Nature Communications, 12(1):5493, 1-11. Nature Publishing Group
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Nature Communications, 12(1), 1. Nature Publishing Group
Nature Communications, 12(1):5493, 1-11. Nature Publishing Group
Nature Communications
Nature Communications, Vol 12, Iss 1, Pp 1-11 (2021)
Macromolecular dynamics manifest as disorder in structure determination, which is subsequently accounted for by displacement parameters (also called temperature factors, or B-factors) or alternate conformations. Though B-factors contain detailed info
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::948a58ce9f9ef77058c38e8c5aeb52dd
https://dspace.library.uu.nl/handle/1874/425306
https://dspace.library.uu.nl/handle/1874/425306
Autor:
Wim Annaert, Katleen Dillen, Randy Schekman, Ragna Sannerud, Bertrand Kleizen, Rosanne Wouters, David Demedts, Christine Michiels, Abril Escamilla Ayala, Wendy Vermeire
Publikováno v:
Journal of Cell Biology, 220(9), 1. Rockefeller University Press
γ-Secretase affects many physiological processes through targeting >100 substrates; malfunctioning links γ-secretase to cancer and Alzheimer's disease. The spatiotemporal regulation of its stoichiometric assembly remains unresolved. Fractionation,
Autor:
Wouters, Rosanne, Michiels, Christine, Sannerud, Ragna, Kleizen, Bertrand, Dillen, Katleen, Vermeire, Wendy, Ayala, Abril, Demedts, David, Annaert, Wim, SCHEKMAN, Randy W
Publikováno v:
The Journal of Cell Biology, vol 220, iss 9
γ-Secretase affects many physiological processes through targeting >100 substrates; malfunctioning links γ-secretase to cancer and Alzheimers disease. The spatiotemporal regulation of its stoichiometric assembly remains unresolved. Fractionation, b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::f2ae0199a715d64c89f2a0ccb4aace5c
https://dspace.library.uu.nl/handle/1874/414000
https://dspace.library.uu.nl/handle/1874/414000
Publikováno v:
Ladefoged, L K, Zeppelin, T & Schiøtt, B 2019, ' Molecular modeling of neurological membrane proteins − from binding sites to synapses ', Neuroscience Letters, vol. 700, pp. 38-49 . https://doi.org/10.1016/j.neulet.2018.05.034
The field of molecular mechanics studies of proteins has developed enormously since its origin in the 1970’s, and many applications and methodologies have branched from the original idea of the force field. The applications of such methodologies ar
Autor:
Vincent Olieric, Valentina Cecatiello, Silvia Monzani, Julien Colombani, Valentina Palmerini, Ditte S. Andersen, Sara Mari, Rihab Loudhaief, Marina Mapelli, Quentin Laurichesse, Sebastiano Pasqualato
Publikováno v:
Nature Communications
Palmerini, V, Monzani, S, Laurichesse, Q, Loudhaief, R, Mari, S, Cecatiello, V, Olieric, V, Pasqualato, S, Colombani, J, Andersen, D S & Mapelli, M 2021, ' Drosophila TNFRs Grindelwald and Wengen bind Eiger with different affinities and promote distinct cellular functions ', Nature Communications, vol. 12, 2070 . https://doi.org/10.1038/s41467-021-22080-9
'Nature Communications ', vol: 12, pages: 2070-1-2070-12 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Palmerini, V, Monzani, S, Laurichesse, Q, Loudhaief, R, Mari, S, Cecatiello, V, Olieric, V, Pasqualato, S, Colombani, J, Andersen, D S & Mapelli, M 2021, ' Drosophila TNFRs Grindelwald and Wengen bind Eiger with different affinities and promote distinct cellular functions ', Nature Communications, vol. 12, 2070 . https://doi.org/10.1038/s41467-021-22080-9
'Nature Communications ', vol: 12, pages: 2070-1-2070-12 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
The Drosophila tumour necrosis factor (TNF) ligand-receptor system consists of a unique ligand, Eiger (Egr), and two receptors, Grindelwald (Grnd) and Wengen (Wgn), and therefore provides a simple system for exploring the interplay between ligand and
Publikováno v:
Ji, J & Day, A 2020, ' Construction of a highly error-prone DNA polymerase for developing organelle mutation systems ', Nucleic Acids Res, vol. 48, no. 21, DOI: gkaa929, pp. 11868-11879 . https://doi.org/10.1093/nar/gkaa929
Nucleic Acids Research
Nucleic Acids Research
A novel family of DNA polymerases replicates organelle genomes in a wide distribution of taxa encompassing plants and protozoans. Making error-prone mutator versions of gamma DNA polymerases revolutionised our understanding of animal mitochondrial ge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cf2dfc0f7a24dd32b9eaaa993c0d7130
http://www.narbreakthrough.com/2020/11/03/construction-of-a-highly-error-prone-dna-polymerase-for-developing-organelle-mutation-systems/
http://www.narbreakthrough.com/2020/11/03/construction-of-a-highly-error-prone-dna-polymerase-for-developing-organelle-mutation-systems/
Autor:
Mrinal Shekhar, Eamonn Reading, Chloe Martens, Emad Tajkhorshid, Argyris Politis, Antoni J. Borysik, Andy M. Lau, Paula J. Booth
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Nature Communications
Martens, C, Shekhar, M, Borysik, A, Lau, A M C, Tajkhorshid, E, Reading, E, Booth, P J & Politis, A 2018, ' Direct protein-lipid interactions shape the conformational landscape of secondary transporters ', Nature Communications, vol. 9, 4151 . https://doi.org/10.1038/s41467-018-06704-1
Nature communications, 9 (1
Nature Communications
Martens, C, Shekhar, M, Borysik, A, Lau, A M C, Tajkhorshid, E, Reading, E, Booth, P J & Politis, A 2018, ' Direct protein-lipid interactions shape the conformational landscape of secondary transporters ', Nature Communications, vol. 9, 4151 . https://doi.org/10.1038/s41467-018-06704-1
Nature communications, 9 (1
Secondary transporters undergo structural rearrangements to catalyze substrate translocation across the cell membrane - yet how such conformational changes happen within a lipid environment remains poorly understood. Here, we combine hydrogen-deuteri