Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Magnus Brändén"'
Autor:
Julia Hedlund, Hans Elwing, Angelika Kunze, Magnus Brändén, Olof Andersson, Anders Lundgren, Fredrik Höök
Publikováno v:
Analytical Chemistry. 83:7800-7806
A single-chip electrochemical method based on impedance measurements in resonance mode has been employed to study lipid monolayer and bilayer formation on hydrophobic alkanethiolate and SiO(2) substrates, respectively. The processes were monitored by
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::814aecc55559896c02d948a07d9c31dd
https://doi.org/10.1021/ac201273t
https://doi.org/10.1021/ac201273t
Publikováno v:
Biophysical Journal; Vol 99
Numerous membrane-transport proteins are major drug targets, and therefore a key ingredient in pharmaceutical development is the availability of reliable, efficient tools for membrane transport characterization and inhibition. Here, we present the us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::094633dbc52e44effd415b70265fdb7e
Publikováno v:
Journal of Structural Biology. 168:200-206
Inspired by natural cell-cell junctions, where membrane-residing proteins control the separation between two or more membranes without interfering with their integrity, we report a new self-assembly route for formation of multiple highly fluid tether
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::042e91982029ac6789db1a87e272627a
https://doi.org/10.1016/j.jsb.2009.07.008
https://doi.org/10.1016/j.jsb.2009.07.008
Publikováno v:
ChemPhysChem. 9:2480-2485
Pucker up! A novel approach enabling direct measurements of biomolecular transfer across lipid bilayer membranes, using surface plasmon resonance, is demonstrated. The figure shows the transfer of sucrose (S) through melittin pores formed in surface-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cb4b680a168255380b5eb435d5978e1
https://doi.org/10.1002/cphc.200800614
https://doi.org/10.1002/cphc.200800614
Autor:
Magnus Brändén, Audrius Jasaitis, Håkan Lepp, Peter Brzezinski, Andreas Namslauer, Michael I. Verkhovsky
Publikováno v:
Journal of Biological Chemistry. 282:15148-15158
Cytochrome c oxidase (CytcO) is a redox-driven, membrane-bound proton pump. One of the proton transfer pathways of the enzyme, the D pathway, used for the transfer of both substrate and pumped protons, accommodates a network of hydrogen-bonded water
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1e34c89d6f93ad6839afc94c2f8d9826
https://doi.org/10.1074/jbc.m700348200
https://doi.org/10.1074/jbc.m700348200
Publikováno v:
Proceedings of the National Academy of Sciences. 103:19766-19770
Cellular processes such as nerve conduction, energy metabolism, and import of nutrients into cells all depend on transport of ions across biological membranes through specialized membrane-spanning proteins. Understanding these processes at a molecula
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edc98c099301d674fa488fc0b91652a9
https://doi.org/10.1073/pnas.0605909103
https://doi.org/10.1073/pnas.0605909103
Autor:
Gisela Brändén, Magnus Brändén, Peter Brzezinski, Denise A. Mills, Bryan Schmidt, Shelagh Ferguson-Miller
Publikováno v:
Biochemistry. 44:10466-10474
In cytochrome c oxidase (CcO), exergonic electron transfer reactions from cytochrome c to oxygen drive proton pumping across the membrane. Elucidation of the proton pumping mechanism requires identification of the molecular components involved in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0fa0294cf4a1066f24ebf5cb13808686
https://doi.org/10.1021/bi0502745
https://doi.org/10.1021/bi0502745
Publikováno v:
Biochemistry. 41:10794-10798
Cytochrome c oxidase is a redox-driven proton pump. The enzyme has two proton input pathways, leading from the solution on the N-side to the binuclear center. One of these pathways, the K-pathway, is used for proton uptake upon reduction of the binuc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e6f28ee91fdbe405a52fef1476146dc
https://doi.org/10.1021/bi026093+
https://doi.org/10.1021/bi026093+
Publikováno v:
Journal of Inorganic Biochemistry. 88:335-342
We have investigated the CO-recombination kinetics after flash photolysis of CO from the "half-reduced" cytochrome c oxidase as a function of pH. In addition, the reaction was investigated in mutant enzymes in which Lys(I-362) and Ser(I-299), located
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1704afd110dac2f502a68ae528155968
https://doi.org/10.1016/s0162-0134(01)00348-8
https://doi.org/10.1016/s0162-0134(01)00348-8
Autor:
Pia Ädelroth, Magnus Brändén, Andreas Namslauer, Robert B. Gennis, Peter Brzezinski, Håkan Sigurdson
Publikováno v:
Proceedings of the National Academy of Sciences. 98:5013-5018
Cytochrome c oxidase is a membrane-bound enzyme that catalyzes the four-electron reduction of oxygen to water. This highly exergonic reaction drives proton pumping across the membrane. One of the key questions associated with the function of cytochro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b1c04d6d3ef28c58b404bb4afc1b4d94
https://doi.org/10.1073/pnas.081088398
https://doi.org/10.1073/pnas.081088398