Zobrazeno 1 - 10
of 422
pro vyhledávání: '"Sansom, MSP"'
Publikováno v:
Annual Review of Pharmacology and Toxicology. 60:31-50
Ion channels and G protein–coupled receptors (GPCRs) are regulated by lipids in their membrane environment. Structural studies combined with biophysical and molecular simulation investigations reveal interaction sites for specific lipids on membran
Autor:
Lanz, A-L, Masi, G, Porciello, N, Cohnen, A, Cipria, D, Prakaash, D, Bálint, Š, Raggiaschi, R, Galgano, D, Cole, DK, Lepore, M, Dushek, O, Dustin, ML, Sansom, MSP, Kalli, AC, Acuto, O
The mechanism of T cell antigen receptor (TCR-CD3) signaling remains elusive. Here, we identify mutations in the transmembrane region of TCRβ or CD3ζ that augment peptide T cell antigen receptor (pMHC)-induced signaling not explicable by enhanced l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::9e007c1516b18e255258b729d06cc430
https://eprints.whiterose.ac.uk/176171/1/1-s2.0-S2211124721007737-main.pdf
https://eprints.whiterose.ac.uk/176171/1/1-s2.0-S2211124721007737-main.pdf
Autor:
Tanadet Pipatpolkai, Wanling Song, Suzanne C. Letham, Phillip J. Stansfeld, Sansom Msp., Robin A. Corey, Michael R. Horrell, L Curran, Christian Siebold, T B Ansell
Publikováno v:
Journal of Chemical Theory and Computation
Specific interactions of lipids with membrane proteins contribute to protein stability and function. Multiple lipid interactions surrounding a membrane protein are often identified in molecular dynamics (MD) simulations and are, increasingly, resolve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea4fb4d7315db2baa44f25c5a745d35d
https://doi.org/10.1101/2021.06.02.446704
https://doi.org/10.1101/2021.06.02.446704
A biomembrane sample system where millimolar changes of cations induce reversible large scale (≥ 200 Å) changes in the membrane-to-surface distance is described. The system composes of a free-floating bilayer (FFB), formed adjacent to a self-assem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bbc8ceee1e6aa034465ee86bf219053c
https://doi.org/10.26434/chemrxiv.13603325.v2
https://doi.org/10.26434/chemrxiv.13603325.v2
Nanoscale membrane curvature is a common feature in cell biology required for functions such as endocytosis, exocytosis and cell migration. These processes require the cytoskeleton to exert forces on the membrane to deform it. Cytosolic proteins cont
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1032::124f43fd3f05e889924da407f98d85a1
http://hdl.handle.net/10044/1/85877
http://hdl.handle.net/10044/1/85877
Autor:
Ni, T, Kalli, AC, Naughton, FB, Yates, LA, Naneh, O, Kozorog, M, Anderluh, G, Sansom, MSP, Gilbert, RJC
Publikováno v:
Biochemical Journal
Kindlins co-activate integrins alongside talin. They possess, like talin, a FERM domain (4.1-erythrin–radixin–moiesin domain) comprising F0–F3 subdomains, but with a pleckstrin homology (PH) domain inserted in the F2 subdomain that enables memb
Ion channels and GPCRs are regulated by lipids in their membrane environment. Structural studies combined with biophysical and molecular simulation investigations reveal interaction sites for specific lipids on membrane protein structures. For K chan
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od______1064::2de0557b242a8c5c48614f0b11003499
https://ora.ox.ac.uk/objects/uuid:02734590-44f8-48f2-b4b6-617e53fc38cf
https://ora.ox.ac.uk/objects/uuid:02734590-44f8-48f2-b4b6-617e53fc38cf
Autor:
Posner, MG, Upadhyay, A, Ishima, R, Kalli, AC, Harris, G, Kremerskothen, J, Sansom, MSP, Crennell, SJ, Bagby, S
Kidney- and brain-expressed protein (KIBRA), a multifunctional scaffold protein with around 20 known binding partners, is involved in memory and cognition, organ size control via the Hippo pathway, cell polarity, and membrane trafficking. KIBRA inclu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::75d78202e3268a2e513788335a9033ed
https://eprints.whiterose.ac.uk/131014/8/9335.full.pdf
https://eprints.whiterose.ac.uk/131014/8/9335.full.pdf
Atomistic simulations have recently been shown to be sufficiently accurate to reversibly fold globular proteins and have provided insights into folding mechanisms. Gaining similar understanding from simulations of membrane protein folding and associa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::4bf06a127a0086156508f7c8779e593f
https://doi.org/10.1021/acs.jctc.7b00983
https://doi.org/10.1021/acs.jctc.7b00983