Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Ulrich Matthey"'
Autor:
Nicola Franscini, Ahmed El Gedaily, Ulrich Matthey, Susanne Franitza, Man-Sun Sy, Alexander Bürkle, Martin Groschup, Ueli Braun, Ralph Zahn
Publikováno v:
PLoS ONE, Vol 1, p e71 (2006)
BACKGROUND: Prions are known to cause transmissible spongiform encephalopathies (TSE) after accumulation in the central nervous system. There is increasing evidence that prions are also present in body fluids and that prion infection by blood transmi
Externí odkaz:
https://doaj.org/article/332fa1232a7d49f582e72c6fd8bfeb8e
Autor:
Susanne Franitza, E Berli, Nicola Franscini, Ueli Braun, Ulrich Matthey, Michael Hässig, Ralph Zahn, A C Tschuor, A El Gedaily
Publikováno v:
Schweizer Archiv für Tierheilkunde. 151:433-436
The goal of the present study was to investigate whether protease-resistant prion protein (PrPres) occurs in plasma samples of offspring of cows that developed bovine spongiform encephalopathy (BSE; group A) and to compare the prevalence with that of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::37c1fbadc1c1b1bf671dd6077accefe5
https://doi.org/10.1024/0036-7281.151.9.433
https://doi.org/10.1024/0036-7281.151.9.433
Autor:
Ulrich Matthey, Gregory M. Cook, Stefanie Keis, Georg Kaim, Hugh W. Morgan, Christoph von Ballmoos, Peter Dimroth
Publikováno v:
Journal of Bacteriology. 185:4442-4449
We describe here purification and biochemical characterization of the F 1 F o -ATP synthase from the thermoalkaliphilic organism Bacillus sp. strain TA2.A1. The purified enzyme produced the typical subunit pattern of an F 1 F o -ATP synthase on a sod
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ed561321c25f685c29a28ad069d87d9
https://doi.org/10.1128/jb.185.15.4442-4449.2003
https://doi.org/10.1128/jb.185.15.4442-4449.2003
Publikováno v:
European Journal of Biochemistry. 269:1942-1946
The subunit c from the ATP synthase of Propionigenium modestum was studied by NMR in chloroform/methanol/water (4 : 4 : 1). In this solvent, subunit c consists of two helical segments, comprised of residues L5 to I26 and G29 to N82, respectively. On
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0ecc16ade91b7c93124e8ad3376d05ac
https://doi.org/10.1046/j.1432-1033.2002.02851.x
https://doi.org/10.1046/j.1432-1033.2002.02851.x
Publikováno v:
FEBS Letters. 505:353-356
The isolated rotor cylinder of the ATP synthase from Ilyobacter tartaricus was reconstituted into two-dimensional crystalline arrays. Atomic force microscopy imaging indicated a central cavity on one side of the rotor and a central plug protruding fr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9445098248c856c24eac41f7c9c4bfde
https://doi.org/10.1016/s0014-5793(01)02837-x
https://doi.org/10.1016/s0014-5793(01)02837-x
Autor:
Kitaru Suda, Peter Dimroth, Dimitrios Fotiadis, Thomas Meier, Daniel J. Müller, Henning Stahlberg, Andreas Engel, Ulrich Matthey
Publikováno v:
EMBO reports. 2:229-233
Synthesis of adenosine triphosphate (ATP) by the F(1)F(0) ATP synthase involves a membrane-embedded rotary engine, the F(0) domain, which drives the extra-membranous catalytic F(1) domain. The F(0) domain consists of subunits a(1)b(2) and a cylindric
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::355f2c93c49ad21f74b37ad5db2ced80
https://doi.org/10.1093/embo-reports/kve047
https://doi.org/10.1093/embo-reports/kve047
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1459:506-513
The mechanism of converting an electrochemical gradient of protons or Na(+) ions across the membrane into rotational torque by the F(o) motor of the ATP synthase has been described by a two-channel model or by a one-channel model. Experimental eviden
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::751501f8237f0d20a5cde14e4f51eb34
https://doi.org/10.1016/s0005-2728(00)00190-0
https://doi.org/10.1016/s0005-2728(00)00190-0
Publikováno v:
Journal of Bioenergetics and Biomembranes. 32:449-458
In Propionigenium modestum, ATP is manufactured from ADP and phosphate by the enzyme ATP synthase using the free energy of an electrochemical gradient of Na+ ions. The P. modestum ATP synthase is a clear member of the family of F-type ATP synthases a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3d2097119c97704f955c9ac091d37f40
https://doi.org/10.1023/a:1005608823087
https://doi.org/10.1023/a:1005608823087
Publikováno v:
Journal of Bacteriology. 180:3312-3316
The ATPase of Ilyobacter tartaricus was solubilized from the bacterial membranes and purified. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified enzyme revealed the usual subunit pattern of a bacterial F 1 F o ATPase. The poly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c57722790d2f5e077a51e6741bbc0290
https://doi.org/10.1128/jb.180.13.3312-3316.1998
https://doi.org/10.1128/jb.180.13.3312-3316.1998
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1365(1-2):87-92
A model is presented in which ion translocation through the F0 part of the ATP synthase drives the rotation of the ring of c subunits (rotor) versus the a subunit (stator). The coupling ion binding sites on the rotor are accessible from the cytoplasm
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87b2d624a5d0303c46eeae8e07b36662