Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Amy P. Guilfoyle"'
Autor:
Megan J. Maher, Amy P. Guilfoyle, Josep Font, Mika Jormakka, Aaron P. McGrath, Chandrika N. Deshpande
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69:399-404
FeoB is a transmembrane protein involved in ferrous iron uptake in prokaryotic organisms. FeoB comprises a cytoplasmic soluble domain termed NFeoB and a C-terminal polytopic transmembrane domain. Recent structures of NFeoB have revealed two structura
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c7741b6562590e56562cab0cea6b2f6
https://doi.org/10.1107/s1744309113005939
https://doi.org/10.1107/s1744309113005939
Publikováno v:
Bioscience Reports
Bioscience Reports, Vol 34, Iss 6, p e00158 (2014)
Bioscience Reports, Vol 34, Iss 6, p e00158 (2014)
GDP release from GTPases is usually extremely slow and is in general assisted by external factors, such as association with guanine exchange factors or membrane-embedded GPCRs (G protein-coupled receptors), which accelerate the release of GDP by seve
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8a9eca1d71b8c392934f4c691f1df1b
https://pubmed.ncbi.nlm.nih.gov/25374115
https://pubmed.ncbi.nlm.nih.gov/25374115
Autor:
Megan J. Maher, Amy P. Guilfoyle, Chandrika N. Deshpande, Kimberley Vincent, Marcelo Monteiro Pedroso, Mika Jormakka, Gerhard Schenk
Publikováno v:
The FEBS journal. 281(9)
GTPases (G proteins) hydrolyze the conversion of GTP to GDP and free phosphate, comprising an integral part of prokaryotic and eukaryotic signaling, protein biosynthesis and cell division, as well as membrane transport processes. The G protein cycle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ed6be7cb2a1e37235cb2821fcb39e40
https://pubmed.ncbi.nlm.nih.gov/24649829
https://pubmed.ncbi.nlm.nih.gov/24649829
Autor:
Amy P. Guilfoyle, J. Mitchell Guss, Ronald J. Clarke, Miriam-Rose Ash, Mika Jormakka, Megan J. Maher
FeoB is a prokaryotic membrane protein responsible for the import of ferrous iron (Fe(2+)). A defining feature of FeoB is that it includes an N-terminal 30-kDa soluble domain with GTPase activity, which is required for iron transport. However, the lo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76cd2539594deb118c8a352f64367191
https://europepmc.org/articles/PMC2863241/
https://europepmc.org/articles/PMC2863241/
Autor:
Mikaela Rapp, Ronald J. Clarke, Amy P. Guilfoyle, Mika Jormakka, Megan J. Maher, Stephen J. Harrop
Publikováno v:
The EMBO journal. 28(17)
G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe(2+) transport, and is unique in that the G protein is directly tet
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab440cd84e20c1c914961c6ceaa5dcc2
https://pubmed.ncbi.nlm.nih.gov/19629046
https://pubmed.ncbi.nlm.nih.gov/19629046
Autor:
Andrew, Robinson, Amy P, Guilfoyle, Visaahini, Sureshan, Michael, Howell, Stephen J, Harrop, Yan, Boucher, Hatch W, Stokes, Paul M G, Curmi, Bridget C, Mabbutt
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 426
Mobile gene cassettes collectively carry a highly diverse pool of novel genes, ostensibly for purposes of microbial adaptation. At the sequence level, putative functions can only be assigned to a minority of carried ORFs due to their inherent novelty
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::461f3d2e65763719e6101e3e0929d036
https://pubmed.ncbi.nlm.nih.gov/18542892
https://pubmed.ncbi.nlm.nih.gov/18542892
Autor:
Miriam-Rose Ash, Megan J. Maher, Amy P. Guilfoyle, Mika Jormakka, Samuel Tourle, Chandrika N. Deshpande, Gerhard Schenk, Josep Font Sadurni
Publikováno v:
Guilfoyle, A P, Deshpande, C N, Font Sadurni, J, Ash, M-R, Tourle, S, Schenk, G, Maher, M J & Jormakka, M 2014, ' A GTPase chimera illustrates an uncoupled nucleotide affinity and release rate, Providing insight into the activation mechanism ', Biophysical Journal, vol. 107, no. 12, pp. L45-L48 . https://doi.org/10.1016/j.bpj.2014.10.064
The release of GDP from GTPases signals the initiation of a GTPase cycle, where the association of GTP triggers conformational changes promoting binding of downstream effector molecules. Studies have implicated the nucleotide-binding G5 loop to be in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1039ffa6f1778fafaf4cafb805b7f998