Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Christos, Pliotas"'
Publikováno v:
Channels, Vol 16, Iss 1, Pp 148-158 (2022)
Mechanosensitive ion channels are integral membrane proteins ubiquitously present in bacteria, archaea, and eukarya. They act as molecular sensors of mechanical stress to serve vital functions such as touch, hearing, osmotic pressure, proprioception
Externí odkaz:
https://doaj.org/article/b87d8c8ebeee490c9911231f317b616d
Autor:
Benjamin J. Lane, Christos Pliotas
Publikováno v:
Frontiers in Chemistry, Vol 11 (2023)
MscL was the first mechanosensitive ion channel identified in bacteria. The channel opens its large pore when the turgor pressure of the cytoplasm increases close to the lytic limit of the cellular membrane. Despite their ubiquity across organisms, t
Externí odkaz:
https://doaj.org/article/b08a7cd66c204ef781159f1aa14f9a69
Autor:
Jessica C. Boakes, Steven. P. D. Harborne, Jessie T. S. Ngo, Christos Pliotas, Adrian Goldman
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Human equilibrative nucleoside transporters represent a major pharmaceutical target for cardiac, cancer and viral therapies. Understanding the molecular basis for transport is crucial for the development of improved therapeutics through structure-bas
Externí odkaz:
https://doaj.org/article/f96b77b34352440880f14624b689e698
Autor:
Benjamin J. Lane, Bolin Wang, Yue Ma, Antonio N. Calabrese, Hassane El Mkami, Christos Pliotas
Publikováno v:
STAR Protocols, Vol 3, Iss 3, Pp 101562- (2022)
Summary: Solvent accessibilities of and distances between protein residues measured by pulsed-EPR approaches provide high-resolution information on dynamic protein motions. We describe protocols for the purification and site-directed spin labeling of
Externí odkaz:
https://doaj.org/article/ad4467d6af924332936f59ebd54c7f43
Autor:
Charalampos Kapsalis, Bolin Wang, Hassane El Mkami, Samantha J. Pitt, Jason R. Schnell, Terry K. Smith, Jonathan D. Lippiat, Bela E. Bode, Christos Pliotas
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
How mechanosensitive ion channels, such as MscL, are activated by lipids and physical properties of the membrane remains unclear. Here authors use PELDOR/DEER spectroscopy and identify a single site which generated an allosteric structural response i
Externí odkaz:
https://doaj.org/article/a7be892017b649e08e44a9f92049a42a
Autor:
Samuel F. Haysom, Jonathan Machin, James M. Whitehouse, Jim E. Horne, Katherine Fenn, Yue Ma, Hassane El Mkami, Nils Böhringer, Till F. Schäberle, Neil A. Ranson, Sheena E. Radford, Christos Pliotas
Publikováno v:
Angewandte Chemie International Edition.
C.P. acknowledges the Biotechnology and Biological Sciences Research Council (BBSRC) (BB/S018069/1; BB/W019795/1) for funding. cwEPR data were collected at the Pliotas Laboratory (BB/S018069/1) and PELDOR data were collected at the University of St A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52e69222439946a0204f05ce9f413b33
https://doi.org/10.1002/anie.202218783
https://doi.org/10.1002/anie.202218783
In-Lipid Structure of Pressure-Sensitive Domains Hints Mechanosensitive Channel Functional Diversity
Publikováno v:
Biophysical Journal
Kapsalis, C, Ma, Y, Bode, B E & Pliotas, C 2020, ' In-lipid structure of pressure sensitive domains hints mechanosensitive channel functional diversity ', Biophysical Journal, vol. 119, no. 2, pp. 448-459 . https://doi.org/10.1016/j.bpj.2020.06.012
Kapsalis, C, Ma, Y, Bode, B E & Pliotas, C 2020, ' In-lipid structure of pressure sensitive domains hints mechanosensitive channel functional diversity ', Biophysical Journal, vol. 119, no. 2, pp. 448-459 . https://doi.org/10.1016/j.bpj.2020.06.012
This project was supported by a BBSRC grant (BB/S018069/1) to C.P., who was supported by the Royal Society of Edinburgh, Tenovus (T15/41) and Carnegie Trust (OS000256), at the initial stages of this project. Further C.P. acknowledges support from the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffacbb996ec44ca2959607f47f95a2b5
http://europepmc.org/articles/PMC7376121
http://europepmc.org/articles/PMC7376121
Autor:
Jonathan D. Lippiat, Charalampos Kapsalis, Terry K. Smith, Samantha J. Pitt, Christos Pliotas, Bela E. Bode, Jason R. Schnell, Bolin Wang, Hassane El Mkami
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
Nature Communications
Kapsalis, C, Wang, B, Mkami, H E, Pitt, S J, Schnell, J R, Smith, T K, Lippiat, J D, Bode, B E & Pliotas, C 2019, ' Allosteric activation of an ion channel triggered by modification of mechanosensitive nano-pockets ', Nature Communications, vol. 10, 4619, pp. 1-14 . https://doi.org/10.1038/s41467-019-12591-x
Nature Communications
Kapsalis, C, Wang, B, Mkami, H E, Pitt, S J, Schnell, J R, Smith, T K, Lippiat, J D, Bode, B E & Pliotas, C 2019, ' Allosteric activation of an ion channel triggered by modification of mechanosensitive nano-pockets ', Nature Communications, vol. 10, 4619, pp. 1-14 . https://doi.org/10.1038/s41467-019-12591-x
Lipid availability within transmembrane nano-pockets of ion channels is linked with mechanosensation. However, the effect of hindering lipid-chain penetration into nano-pockets on channel structure has not been demonstrated. Here we identify nano-poc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3b4f45815654ff1d3fa5745d249d8fc0
http://link.springer.com/article/10.1038/s41467-019-12591-x
http://link.springer.com/article/10.1038/s41467-019-12591-x
Autor:
Frank Sobott, Benjamin J. Lane, Antonio N. Calabrese, Bolin Wang, Hassane El Mkami, Charalampos Kapsalis, James R. Ault, Antreas C. Kalli, Christos Pliotas
The MscL channel gates in response to membrane tension changes to allow the exchange of molecules through its pore. Lipid removal from transmembrane pockets leads to a MscL response. However, it is unknown whether there is correlation between the ten
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d5577b9f9285bfbd02243069f7d73db2
https://doi.org/10.1101/2021.04.01.438050
https://doi.org/10.1101/2021.04.01.438050
Autor:
Edward T Davis, Michael G. Tomlinson, Lisa Seipold, Murat Keles, Natalie S. Poulter, Paul Saftig, Antonia Malinova, Stephan A. Mueller, Stefan F. Lichtenthaler, Alexandra L. Matthews, Bethany Cragoe, Hanh T.H. Nguyen, Stephen J. Briddon, Nicholas D. Holliday, Christos Pliotas, Chek Ziu Koo, Eric Rubinstein, Thomas A. McFarlane, Johanna Tüshaus, Michael C. Sykes, Justyna Szyroka, Eleanor Cull, Katie Willis, Haroon Ahmed, Alessandro Di Maio, Clara Apicella, Joelle Goulding, Peter J. Noy, Neale Harrison, Hung-En Hsia, Philip R. Morrison
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2020, 295 (36), pp.12822-12839. ⟨10.1074/jbc.ra120.012601⟩
The journal of biological chemistry 295(36), 12822-12839 (2020). doi:10.1074/jbc.RA120.012601
J Biol Chem
Journal of Biological Chemistry, 2020, 295 (36), pp.12822-12839. ⟨10.1074/jbc.ra120.012601⟩
Koo, C Z, Harrison, N, Noy, P J, Szyroka, J, Matthews, A L, Hsia, H-E, Müller, S A, Tüshaus, J, Goulding, J, Willis, K, Apicella, C, Cragoe, B, Davis, E, Keles, M, Malinova, A, McFarlane, T A, Morrison, P R, Nguyen, H T H, Sykes, M C, Ahmed, H, Maio, A D, Seipold, L, Saftig, P, Cull, E, Pliotas, C, Rubinstein, E, Poulter, N S, Briddon, S J, Holliday, N D, Lichtenthaler, S F & Tomlinson, M G 2020, ' The tetraspanin Tspan15 is an essential subunit of an ADAM10 scissor complex ', Journal of Biological Chemistry, vol. 295, no. 36, pp. 12822-12839 . https://doi.org/10.1074/jbc.RA120.012601
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2020, 295 (36), pp.12822-12839. ⟨10.1074/jbc.ra120.012601⟩
The journal of biological chemistry 295(36), 12822-12839 (2020). doi:10.1074/jbc.RA120.012601
J Biol Chem
Journal of Biological Chemistry, 2020, 295 (36), pp.12822-12839. ⟨10.1074/jbc.ra120.012601⟩
Koo, C Z, Harrison, N, Noy, P J, Szyroka, J, Matthews, A L, Hsia, H-E, Müller, S A, Tüshaus, J, Goulding, J, Willis, K, Apicella, C, Cragoe, B, Davis, E, Keles, M, Malinova, A, McFarlane, T A, Morrison, P R, Nguyen, H T H, Sykes, M C, Ahmed, H, Maio, A D, Seipold, L, Saftig, P, Cull, E, Pliotas, C, Rubinstein, E, Poulter, N S, Briddon, S J, Holliday, N D, Lichtenthaler, S F & Tomlinson, M G 2020, ' The tetraspanin Tspan15 is an essential subunit of an ADAM10 scissor complex ', Journal of Biological Chemistry, vol. 295, no. 36, pp. 12822-12839 . https://doi.org/10.1074/jbc.RA120.012601
International audience; A disintegrin and metalloprotease 10 (ADAM10) is a transmembrane protein essential for embryonic development, and its dysregulation underlies disorders such as cancer, Alzheimer's disease, and inflammation. ADAM10 is a “mole
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a8eb363ab27157e6e501561ef205a029
https://hal.sorbonne-universite.fr/hal-03124330
https://hal.sorbonne-universite.fr/hal-03124330