Zobrazeno 1 - 10
of 32
pro vyhledávání: '"Larry D. Faller"'
Publikováno v:
Journal of Biological Chemistry. 280:7435-7443
Calcium pump-catalyzed (18)O exchange between inorganic phosphate and water was studied to test the hypothesis that all P-type pumps bind Mg(2+) before P(i) and validate utilization of the rate equation for ordered binding to interpret differences be
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aecdf4d4ea900a24b85d8782b85eb62d
https://doi.org/10.1074/jbc.m412319200
https://doi.org/10.1074/jbc.m412319200
Publikováno v:
Annals of the New York Academy of Sciences. 986:96-100
The loop between transmembrane helices 6 and 7 (L6/7) of P-type ATPases has been suggested to be important for the functional linkage of ion binding and enzyme phosphorylation or to be a site of initial cation binding. To investigate the role of L6/7
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cd051169f073357bb4f9636b923fed73
https://doi.org/10.1111/j.1749-6632.2003.tb07144.x
https://doi.org/10.1111/j.1749-6632.2003.tb07144.x
Autor:
Emad Elquza, Vladimir N. Kasho, Jochen Müller-Ehmsen, Robert A. Farley, Agnes K. Nagy, Larry D. Faller, David J. Kane
Publikováno v:
Biochemistry. 40:6361-6370
We have proposed a model for part of the catalytic site of P-type pumps in which arginine in a signature sequence functions like lysine in P-loop-containing enzymes that catalyze adenosine 5'-triphosphate hydrolysis [Smirnova, I. N., Kasho, V. N., an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::83dd0f7f8a6506ed7c8280bb3484d77a
https://doi.org/10.1021/bi010270+
https://doi.org/10.1021/bi010270+
Autor:
Larry D. Faller, Shwu-Hwa Lin
Publikováno v:
Analytical Biochemistry. 287:303-312
Specific labeling is required for energy transfer measurements and to avoid artifacts in the use of fluorophores as reporter groups. Therefore, a method for specific modification by one of the most popular reagents for P-type ATPases (fluorescein 5'-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::caf1ab884ea590b4c1a0be557a0c6bbf
https://doi.org/10.1006/abio.2000.4828
https://doi.org/10.1006/abio.2000.4828
Publikováno v:
FEBS Letters. 431:309-314
The machinery to catalyze elementary reactions is conserved, and the number of solved enzyme structures is increasing exponentially. Therefore, structures of enzymes that catalyze phosphate transfer are reviewed, and a supersecondary structure connec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::484243576eecb1903efad39f086f0c5a
https://doi.org/10.1016/s0014-5793(98)00760-1
https://doi.org/10.1016/s0014-5793(98)00760-1
Publikováno v:
Biochemistry. 36:8045-8052
Mutations of D586 in the DPPR sequence of sodium pump decrease the enzyme's affinity for inorganic phosphate [Farley R. A., Heart, E., Kabalin, M., Putnam, D., Wang, K., Kasho, V. N., and Faller, L. D. (1997) Biochemistry 36, 941-951]. Therefore, it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa16f5242c33f80af3f2541b01691b12
https://doi.org/10.1021/bi970472z
https://doi.org/10.1021/bi970472z
Autor:
Shwu-Hwa Lin, Larry D. Faller
Publikováno v:
Biochemistry. 35:8419-8428
The first indication of the size of a conformational change implicated in ion transport by sodium pump has been obtained by measuring the change in efficiency of fluorescence energy transfer betwee...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::333c22757660c8d859d080f02c9cd36d
https://doi.org/10.1021/bi960407+
https://doi.org/10.1021/bi960407+
Publikováno v:
Annals of the New York Academy of Sciences. 986:275-277
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::390457c2acbf8d4285703ccf638d2481
https://doi.org/10.1111/j.1749-6632.2003.tb07184.x
https://doi.org/10.1111/j.1749-6632.2003.tb07184.x
Autor:
Larry D. Faller, Shwu-Hwa Lin
Publikováno v:
Biochemistry. 32:13917-13924
Equilibrium fluorometric titrations of fluorescein 5'-isothiocyanate-modified Na,K-ATPase with cations have usually been interpreted by assuming that an enhancement reports the conformational change from E2 to E1. We report time resolution of the flu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea90f834b6e0f448519cedde36fff921
https://doi.org/10.1021/bi00213a022
https://doi.org/10.1021/bi00213a022
Autor:
Irina Smirnova, Larry D. Faller
Publikováno v:
Biochemistry. 32:5967-5977
The role of Mg2+ in the conformational change reported by fluorescein 5'-isothiocyanate modification of Na,K-ATPase has been studied by stopped-flow fluorometry. K+ causes a fluorescence quench that is reversed by Na+. The principal experimental obse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::79f19182502c2f384c952a715f466a06
https://doi.org/10.1021/bi00074a007
https://doi.org/10.1021/bi00074a007