Jack H Kaplan
Jack H Kaplan
Professor of Biochemistry & Molecular Genetics, University of illinois at Chicago
Dirección de correo verificada de
Citado por
Citado por
Biochemistry of na, K-ATPase
JH Kaplan
Annual review of biochemistry 71 (1), 511-535, 2002
Rapid photolytic release of adenosine 5'-triphosphate from a protected analog: utilization by the sodium: potassium pump of human red blood cell ghosts
JH Kaplan, B Forbush III, JF Hoffman
Biochemistry 17 (10), 1929-1935, 1978
Organization of P-type ATPases: significance of structural diversity
S Lutsenko, JH Kaplan
Biochemistry 34 (48), 15607-15613, 1995
Rapid Adaptation of Cardiac Ryanodine Receptors: Modulation by Mg2+ and Phosphorylation
HH Valdivia, JH Kaplan, GCR Ellis-Davies, WJ Lederer
Science 267 (5206), 1997-2000, 1995
Characterization of the Wilson disease gene encoding a P-type copper transporting ATPase: genomic organization, alternative splicing, and structure/function predictions
K Petrukhin, S Lutsenko, I Chernov, BM Ross, JH Kaplan, TC Gilliam
Human Molecular Genetics 3 (9), 1647-1656, 1994
Photolabile chelators for the rapid photorelease of divalent cations.
JH Kaplan, GC Ellis-Davies
Proceedings of the National Academy of Sciences 85 (17), 6571-6575, 1988
Characterization of a new photoaffinity derivative of ouabain: labeling of the large polypeptide and of a proteolipid component of the (sodium-potassium ion)-dependent ATPase
B Forbush III, JH Kaplan, JF Hoffman
Biochemistry 17 (17), 3667-3676, 1978
Nitrophenyl-EGTA, a photolabile chelator that selectively binds Ca2+ with high affinity and releases it rapidly upon photolysis.
GC Ellis-Davies, JH Kaplan
Proceedings of the National Academy of Sciences 91 (1), 187-191, 1994
N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes disease proteins) bind copper selectively in vivo and in vitro with …
S Lutsenko, K Petrukhin, MJ Cooper, CT Gilliam, JH Kaplan
Journal of Biological Chemistry 272 (30), 18939-18944, 1997
Molecular characterization of hCTR1, the human copper uptake protein
JF Eisses, JH Kaplan
Journal of Biological Chemistry 277 (32), 29162-29171, 2002
An essential role for the extracellular domain of the sodium-potassium-ATPase. beta.-subunit in cation occlusion
S Lutsenko, JH Kaplan
Biochemistry 32 (26), 6737-6743, 1993
Na+/Ca2+ exchange and Na+/K+‐ATPase in the heart
MJ Shattock, M Ottolia, DM Bers, MP Blaustein, A Boguslavskyi, J Bossuyt, ...
The Journal of physiology 593 (6), 1361-1382, 2015
Cellular glutathione plays a key role in copper uptake mediated by human copper transporter 1
EB Maryon, SA Molloy, JH Kaplan
American Journal of Physiology-Cell Physiology 304 (8), C768-C779, 2013
Copper transport in mammalian cells: special care for a metal with special needs
JH Kaplan, S Lutsenko
Journal of Biological Chemistry 284 (38), 25461-25465, 2009
The mechanism of copper uptake mediated by human CTR1: a mutational analysis
JF Eisses, JH Kaplan
Journal of Biological Chemistry 280 (44), 37159-37168, 2005
How mammalian cells acquire copper: an essential but potentially toxic metal
JH Kaplan, EB Maryon
Biophysical journal 110 (1), 7-13, 2016
Chemical modification as an approach to elucidation of sodium pump structure-function relations
CH Pedemonte, JH Kaplan
American Journal of Physiology-Cell Physiology 258 (1), C1-C23, 1990
Laser photolysis of caged calcium: rates of calcium release by nitrophenyl-EGTA and DM-nitrophen
GC Ellis-Davies, JH Kaplan, RJ Barsotti
Biophysical Journal 70 (2), 1006-1016, 1996
Flash photolysis of caged compounds: new tools for cellular physiology
JH Kaplan, AP Somlyo
Trends in neurosciences 12 (2), 54-59, 1989
A new class of photolabile chelators for the rapid release of divalent cations: generation of caged calcium and caged magnesium
GCR Ellis-Davies, JH Kaplan
The Journal of Organic Chemistry 53 (9), 1966-1969, 1988
El sistema no puede realizar la operación en estos momentos. Inténtalo de nuevo más tarde.
Artículos 1–20