Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Steven. P. D. Harborne"'
Autor:
Jessica C. Boakes, Steven. P. D. Harborne, Jessie T. S. Ngo, Christos Pliotas, Adrian Goldman
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Human equilibrative nucleoside transporters represent a major pharmaceutical target for cardiac, cancer and viral therapies. Understanding the molecular basis for transport is crucial for the development of improved therapeutics through structure-bas
Externí odkaz:
https://doaj.org/article/f96b77b34352440880f14624b689e698
Autor:
Nita R. Shah, Craig Wilkinson, Steven P. D. Harborne, Ainoleena Turku, Kun-Mou Li, Yuh-Ju Sun, Sarah Harris, Adrian Goldman
Publikováno v:
Structural Dynamics, Vol 4, Iss 3, Pp 032105-032105-12 (2017)
Membrane-integral pyrophosphatases (mPPases) couple the hydrolysis of pyrophosphate (PPi) to the pumping of Na+, H+, or both these ions across a membrane. Recently solved structures of the Na+-pumping Thermotoga maritima mPPase (TmPPase) and H+-pumpi
Externí odkaz:
https://doaj.org/article/317fe7dc8b6547d3aeee4f1e62d4d008
Autor:
Jessica C. Boakes, Danielle L. Wright, Steven P. D. Harborne, Jannik Strauss, Jacques Boivineau, Veli-Pekka Jaakola, James G. Henderson, Adrian Goldman
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-18 (2020)
Scientific Reports
Scientific Reports
Identifying stabilising variants of membrane protein targets is often required for structure determination. Our new computational pipeline, the Integral Membrane Protein Stability Selector (IMPROvER) provides a rational approach to variant selection
Publikováno v:
IUBMB Life. 70:1222-1232
The mitochondrial ATP-Mg/Pi carrier is responsible for the calcium-dependent regulation of adenosine nucleotide concentrations in the mitochondrial matrix, which allows mitochondria to respond to changing energy requirements of the cell. The carrier
Publikováno v:
Methods in molecular biology (Clifton, N.J.). 2168
There are very few generic methods to assess the stability and functional properties of membrane proteins solubilized in detergent. For this purpose, a thiol-reactive fluorochrome N-[4-(7-diethylamino-4-methyl-3-coumarinyl)phenyl]maleimide (CPM) can
Publikováno v:
Methods in Molecular Biology ISBN: 9781071607237
There are very few generic methods to assess the stability and functional properties of membrane proteins solubilized in detergent. For this purpose, a thiol-reactive fluorochrome N-[4-(7-diethylamino-4-methyl-3-coumarinyl)phenyl]maleimide (CPM) can
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6561f67ab54eb12568ea0ead077b0813
https://www.repository.cam.ac.uk/handle/1810/319193
https://www.repository.cam.ac.uk/handle/1810/319193
Publikováno v:
Biochimica et Biophysica Acta
The mitochondrial ATP-Mg/Pi carrier imports adenine nucleotides from the cytosol into the mitochondrial matrix and exports phosphate. The carrier is regulated by the concentration of cytosolic calcium, altering the size of the adenine nucleotide pool
Publikováno v:
Methods in enzymology. 607
Membrane-bound pyrophosphatases (mPPases) couple pyrophosphate hydrolysis to H
Autor:
Steven P D, Harborne, Jannik, Strauss, Ainoleena, Turku, Matthew A, Watson, Roman, Tuma, Sarah A, Harris, Adrian, Goldman
Publikováno v:
Methods in enzymology. 607
Membrane-bound pyrophosphatases couple the hydrolysis of inorganic pyrophosphate to the pumping of ions (sodium or protons) across a membrane in order to generate an electrochemical gradient. This class of membrane protein is widely conserved across
Autor:
Jessica Michie, Steven P. D. Harborne, Alasdair McComb, Tommi Kotila, Adrian Goldman, Steven G. Gilmour, Duncan Wotherspoon
Protein engineering is one of the foundations of biotechnology, used to increase protein stability, re-assign the catalytic properties of enzymes or increase the interaction affinity between antibody and target. To date, strategies for protein engine
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3a107f6ca28d7cd8c9c53512796a9244
https://doi.org/10.1101/298273
https://doi.org/10.1101/298273