Zobrazeno 1 - 10
of 18
pro vyhledávání: '"Patricia M, Dijkman"'
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-10 (2023)
Abstract Voltage-gated sodium channels shape action potentials that propagate signals along cells. When the membrane potential reaches a certain threshold, the channels open and allow sodium ions to flow through the membrane depolarizing it, followed
Externí odkaz:
https://doaj.org/article/feadb23b05ec4f4fbbf1f4588303e3c6
Autor:
Yingyi Zhang, Patricia M. Dijkman, Rongfeng Zou, Martina Zandl-Lang, Ricardo M. Sanchez, Luise Eckhardt-Strelau, Harald Köfeler, Horst Vogel, Shuguang Yuan, Mikhail Kudryashev
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-15 (2021)
Pentameric ligand-gated ion channels (pLGICs) are key players in neurotransmission and have been shown to be modulated by the lipid environment, however the underlying mechanism is not well understood. Here, the authors report structures of the pLGIC
Externí odkaz:
https://doaj.org/article/c3dc1144479e42dfbcbc8d743307e558
Autor:
Patricia M. Dijkman, Oliver K. Castell, Alan D. Goddard, Juan C. Munoz-Garcia, Chris de Graaf, Mark I. Wallace, Anthony Watts
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Evidence suggests oligomerisation of G protein-coupled receptors in membranes, but this is controversial. Here, authors use single-molecule and ensemble FRET, and spectroscopy to show that the neurotensin receptor 1 forms multiple dimer conformations
Externí odkaz:
https://doaj.org/article/28f2d38675864c7fa3f3f5c8d36e8dc1
Autor:
Patricia M, Dijkman, Tanja, Marzluf, Yingyi, Zhang, Shih-Ying Scott, Chang, Dominic, Helm, Michael, Lanzer, Hermann, Bujard, Mikhail, Kudryashev
Publikováno v:
Science advances. 7(23)
The merozoite surface protein 1 (MSP-1) is the most abundant protein on the surface of the erythrocyte-invading
Autor:
Antonio J. Costa-Filho, Patricia M. Dijkman, Juan C. Muñoz-García, Anthony Watts, Rosana I. Reis, Steven Lavington, Daniel Yin, Phillip J. Stansfeld, Patricia S. Kumagai
Publikováno v:
Repositório Institucional da USP (Biblioteca Digital da Produção Intelectual)
Universidade de São Paulo (USP)
instacron:USP
Science Advances
Universidade de São Paulo (USP)
instacron:USP
Science Advances
Helix 8 of the GPCR neurotensin receptor 1 is stabilised by specific lipid-protein interactions.
G protein–coupled receptors (GPCRs) are the largest and pharmaceutically most important class of membrane proteins encoded in the human genome, ch
G protein–coupled receptors (GPCRs) are the largest and pharmaceutically most important class of membrane proteins encoded in the human genome, ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::483a0810dd023e844410834f47a9deb0
Autor:
Patricia M. Dijkman, Juan H. Bolivar, Anthony Watts, Phillip J. Stansfeld, Tomas Castro-Dopico, Juan C. Muñoz-García
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1858:1278-1287
Information about lipid–protein interactions for G protein-coupled receptors (GPCRs) is scarce. Here, we use electron spin resonance (ESR) and spin-labelled lipids to study lipid interactions with the rat neurotensin receptor 1 (NTS1). A fusion pro
Publikováno v:
Methods (San Diego, Calif.). 147
The cell membrane is a complex milieu of lipids and proteins. In order to understand the behaviour of individual molecules is it often desirable to examine them as purified components in in vitro systems. Here, we detail the creation and use of dropl
Autor:
Anthony Watts, Patricia M. Dijkman
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1848(11):2889-2897
Upon binding of extracellular ligands, G protein coupled-receptors (GPCRs) initiate signalling cascades by activating heterotrimeric G proteins through direct interactions with the α subunit. While the lipid dependence of ligand binding has previous
Autor:
Patricia M. Dijkman, Chris de Graaf, Juan C. Muñoz-García, Anthony Watts, Alan D. Goddard, Mark I. Wallace, Oliver Kieran Castell
Publikováno v:
Nature Communications
Nature Communications, 9(1):1710. Nature Publishing Group
Dijkman, P M, Castell, O K, Goddard, A D, Munoz-Garcia, J C, de Graaf, C, Wallace, M I & Watts, A 2018, ' Dynamic tuneable G protein-coupled receptor monomer-dimer populations ', Nature Communications, vol. 9, 1710 . https://doi.org/10.1038/s41467-018-03727-6
Dijkman, P M, Castell, O K, Goddard, A D, Munoz-Garcia, J C, De Graaf, C, Wallace, M I & Watts, A 2018, ' Dynamic tuneable G protein-coupled receptor monomer-dimer populations ', Nature Communications, vol. 9, no. 1, 1710 . https://doi.org/10.1038/s41467-018-03727-6
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
Nature Communications, 9(1):1710. Nature Publishing Group
Dijkman, P M, Castell, O K, Goddard, A D, Munoz-Garcia, J C, de Graaf, C, Wallace, M I & Watts, A 2018, ' Dynamic tuneable G protein-coupled receptor monomer-dimer populations ', Nature Communications, vol. 9, 1710 . https://doi.org/10.1038/s41467-018-03727-6
Dijkman, P M, Castell, O K, Goddard, A D, Munoz-Garcia, J C, De Graaf, C, Wallace, M I & Watts, A 2018, ' Dynamic tuneable G protein-coupled receptor monomer-dimer populations ', Nature Communications, vol. 9, no. 1, 1710 . https://doi.org/10.1038/s41467-018-03727-6
Nature Communications, Vol 9, Iss 1, Pp 1-14 (2018)
G protein-coupled receptors (GPCRs) are the largest class of membrane receptors, playing a key role in the regulation of processes as varied as neurotransmission and immune response. Evidence for GPCR oligomerisation has been accumulating that challe
Autor:
Geert van den Bogaart, Dieter Braun, Wendy A. Lea, Fernando A. Melo, Moran Jerabek-Willemsen, Patricia M. Dijkman, Stefan Duhr, Ana Lazic, Jeremiah S. Joseph, Susanne A. I. Seidel, Gideon Schreiber, Philipp Baaske, Prakash Srinivasan, Anthony Watts, John E. Ladbury, Ilia Katritch, Anton Simeonov
Publikováno v:
Methods: a Journal for Human Science, 59, 301-15
Methods: a Journal for Human Science, 59, 3, pp. 301-15
Methods: a Journal for Human Science, 59, 3, pp. 301-15
Contains fulltext : 118804.pdf (Publisher’s version ) (Open Access) Microscale thermophoresis (MST) allows for quantitative analysis of protein interactions in free solution and with low sample consumption. The technique is based on thermophoresis,