Zobrazeno 1 - 10
of 68
pro vyhledávání: '"J. Malcolm East"'
Autor:
Sophie J. Hesketh, Zoe Stroud, Alvin C. K. Teo, Timothy R. Dafforn, Sarah C. Lee, Corinne J. Smith, David I. Roper, Timothy J. Knowles, Corinne M. Spickett, Megha Rai, Pooja Sridhar, J. Malcolm East, Mayuriben J. Parmar, Stephen P Muench, Kailene S. Simon, Richard Collins, Vincent L. G. Postis, Saskia E. Bakker, C. Howard Barton, Naomi L. Pollock, Gregory Hurlbut
Most membrane proteins function through interactions with other proteins in the phospholipid bilayer, the cytosol or the extracellular milieu. Understanding the molecular basis of these interactions is key to understanding membrane protein function a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4184bd5543023d4d506e72952b00801a
Publikováno v:
Biochemistry
We show that interactions of fatty acids with the central cavity of potassium channel KcsA can be characterized using the fluorescence probe 11-dansylaminoundecanoic acid (Dauda). The fluorescence emission spectrum of Dauda bound to KcsA in bilayers
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4d4d3cbc7ef3b85532677814ec4b806
https://doi.org/10.1021/bi3009196
https://doi.org/10.1021/bi3009196
Publikováno v:
Biochemical Society Transactions. 39:789-797
The SERCA (sarcoplasmic/endoplasmic reticulum Ca2+-ATPase) is probably the most extensively studied membrane protein transporter. There is a vast array of diverse inhibitors for the Ca2+ pump, and many have proved significant in helping to elucidate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aaecea33b99e3472568c4f9ae4618183
https://doi.org/10.1042/bst0390789
https://doi.org/10.1042/bst0390789
Publikováno v:
Biochemistry. 47:12175-12184
We have studied the effects of lipid structure on the function of the mechanosensitive channel of large conductance (MscL) from Escherichia coli to determine whether effects follow from direct interaction between the lipids and protein or whether the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7fd04200651d94a11198592345e3badf
https://doi.org/10.1021/bi801352a
https://doi.org/10.1021/bi801352a
Publikováno v:
Basic & Clinical Pharmacology & Toxicology. 103:209-213
The aim of this study was to assess the ability of currently deployed antimalarials to inhibit mammalian sarcoendoplasmic reticulum calcium adenosine triphosphatase (SERCA). Artemisinins exert their antiplasmodial action by inhibiting parasite PfATP6
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::781746cdc1154630940c88b8c699ba2e
https://doi.org/10.1111/j.1742-7843.2008.00256.x
https://doi.org/10.1111/j.1742-7843.2008.00256.x
Publikováno v:
Biochemistry. 47:4317-4328
The mechanosensitive channel of large conductance MscL from Escherichia coli has been reconstituted into sealed vesicles, and the effects of lipid structure on the flux of the fluorescent molecule calcein through the open channel have been studied. T
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::932317ab0aeda4f5d60cd91e582fbe6f
https://doi.org/10.1021/bi702409t
https://doi.org/10.1021/bi702409t
Publikováno v:
Biochemistry. 44:5713-5721
The hydrophobic thickness of a membrane protein is an important parameter, defining how the protein sits within the hydrocarbon core of the lipid bilayer that surrounds it in a membrane. Here we show that Trp scanning mutagenesis combined with fluore
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7368120f7151282aa494798481811bd7
https://doi.org/10.1021/bi047338g
https://doi.org/10.1021/bi047338g
Publikováno v:
Biochemistry. 44:5873-5883
We have introduced single Trp residues into the mechanosensitive channel of large conductance (MscL) from Mycobacterium tuberculosis and used fluorescence quenching by brominated phospholipids to detect the presence of a binding site of high affinity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dc8c186137ef7d34992bfa1b7b67c17
https://doi.org/10.1021/bi047439e
https://doi.org/10.1021/bi047439e
Publikováno v:
Biophysical Journal. 85(6):3828-3838
Fluorescence quenching methods have been used to study interactions of anionic phospholipids with the potassium channel KcsA from Streptomyces lividans. Quenching of the Trp fluorescence of KcsA reconstituted into mixtures of dioleoylphosphatidylchol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9912eefb5949e96ab7e3d99777b48943
Publikováno v:
Biochemistry. 42:14306-14317
Trp fluorescence spectroscopy is a powerful tool to study the structures of membrane proteins and their interactions with the surrounding lipid bilayer. Many membrane proteins contain more than one Trp residue, making analysis of the fluorescence dat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d0e4d653d5c88500f34b9ae86cfe9e58
https://doi.org/10.1021/bi034995k
https://doi.org/10.1021/bi034995k