VEGFA, B, C: Implications of the C-Terminal Sequence Variations for the Interaction with Neuropilins

Autor: Charles Eldrid, Mire Zloh, Constantina Fotinou, Tamas Yelland, Lefan Yu, Filipa Mota, David L. Selwood, Snezana Djordjevic

Publikováno v: Biomolecules, Vol 12, Iss 3, p 372 (2022)

Vascular endothelial growth factors (VEGFs) are the key regulators of blood and lymphatic vessels’ formation and function. Each of the proteins from the homologous family VEGFA, VEGFB, VEGFC and VEGFD employs a core cysteine-knot structural domain

Externí odkaz: https://doaj.org/article/60526d5f87e140dda472f99a45328337

Small Molecule Neuropilin-1 Antagonists Combine Antiangiogenic and Antitumor Activity with Immune Modulation through Reduction of Transforming Growth Factor Beta (TGFβ) Production in Regulatory T-Cells

Autor: Jonathan, Powell, Filipa, Mota, David, Steadman, Christelle, Soudy, Jeremy T, Miyauchi, Stuart, Crosby, Ashley, Jarvis, Tifelle, Reisinger, Natalie, Winfield, Graham, Evans, Aled, Finniear, Tamas, Yelland, Yi-Tai, Chou, A W Edith, Chan, Andrew, O'Leary, Lili, Cheng, Dan, Liu, Constantina, Fotinou, Carla, Milagre, John F, Martin, Haiyan, Jia, Paul, Frankel, Snezana, Djordjevic, Stella E, Tsirka, Ian C, Zachary, David L, Selwood

Publikováno v: Journal of Medicinal Chemistry

We report the design, synthesis, and biological evaluation of some potent small-molecule neuropilin-1 (NRP1) antagonists. NRP1 is implicated in the immune response to tumors, particularly in Treg cell fragility, required for PD1 checkpoint blockade.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e56ed2e21a55c2767ecc12a8b43909b2
https://pubmed.ncbi.nlm.nih.gov/29648813

Tetrameric structure of SUR2B revealed by electron microscopy of oriented single particles

Autor: Frances M. Ashcroft, Ange Polidori, Constantina Fotinou, Jussi Aittoniemi, Heidi de Wet, Mark S.P. Sansom, Catherine Vénien-Bryan, Bernard Pucci

Publikováno v: The Febs Journal
FEBS Journal
FEBS Journal, Wiley, 2013, 280 (4), pp.1051-63. ⟨10.1111/febs.12097⟩
FEBS Journal, Wiley, 2013, ⟨10.1111/febs.12097⟩
FEBS Journal, 2013, 280 (4), pp.1051-63. ⟨10.1111/febs.12097⟩

International audience; The ATP-sensitive potassium (K ATP) channel is a hetero-octameric complex that links cell metabolism to membrane electrical activity in many cells, thereby controlling physiological functions such as insulin release, muscle co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dd71a687a9c6c7367cc6e6a30ac627f
http://europepmc.org/articles/PMC3599479

SUR1: a unique ATP-binding cassette protein that functions as an ion channel regulator

Autor: Frances M. Ashcroft, Timothy J. Craig, Jussi Aittoniemi, Peter Proks, Heidi de Wet, Constantina Fotinou

Publikováno v: Philosophical Transactions of the Royal Society B: Biological Sciences; Vol 364

SUR1 is an ATP-binding cassette (ABC) transporter with a novel function. In contrast to other ABC proteins, it serves as the regulatory subunit of an ion channel. The ATP-sensitive (K ATP ) channel is an octameric complex of four pore-forming Kir6.2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eea588e785fe993bd63474cf352216c
https://doi.org/10.1098/rstb.2008.0142

The Structures of the HC Fragment of Tetanus Toxin with Carbohydrate Subunit Complexes Provide Insight into Ganglioside Binding

Autor: Eric W. Hewitt, Colin Watts, Neil W. Isaacs, Ian G. Charles, Constantina Fotinou, Isobel Black, Neil F. Fairweather, Paul Emsley

Publikováno v: Journal of Biological Chemistry. 275:8889-8894

The entry of tetanus neurotoxin into neuronal cells proceeds through the initial binding of the toxin to gangliosides on the cell surface. The carboxyl-terminal fragment of the heavy chain of tetanus neurotoxin contains the ganglioside-binding site,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f6118d1bddb3284fb9b44e9c833ecfc1
https://doi.org/10.1074/jbc.275.12.8889