John T. Penniston spends much of his time researching Biochemistry, ATPase, Calcium pump, Calmodulin and Calcium. John T. Penniston conducts interdisciplinary study in the fields of Biochemistry and Diaphragm pump through his research. His study in ATPase is interdisciplinary in nature, drawing from both Molecular biology and Cyclic nucleotide phosphodiesterase.
His studies deal with areas such as Epithelial polarity and Cell biology as well as Calcium pump. The concepts of his Calmodulin study are interwoven with issues in Liposome, Serine, Vesicle, Aspartic acid and Stereochemistry. His study looks at the relationship between Calcium and fields such as Endocrinology, as well as how they intersect with chemical problems.
His main research concerns Biochemistry, Calmodulin, ATPase, Membrane and Cell biology. His Biochemistry study incorporates themes from Molecular biology and Calcium. His Calcium research incorporates themes from Endocrinology, Ion transporter and Calcium pump.
His Calmodulin research includes elements of Biophysics, Mutant, Binding site and Peptide. His work carried out in the field of ATPase brings together such families of science as Chromatography, Liposome and Nucleotide. His Membrane research is multidisciplinary, incorporating elements of Affinity chromatography and Ca2 pump.
His primary areas of study are Cell biology, Calmodulin, Plasma membrane Ca2+ ATPase, Gene isoform and Biochemistry. His research in Cell biology focuses on subjects like Cytosol, which are connected to Homeostasis, Function, Signal peptide and STIM1. John T. Penniston interconnects Protein structure, Cell, Plasma protein binding and Peptide in the investigation of issues within Calmodulin.
His study on Plasma membrane Ca2+ ATPase is covered under ATPase. His biological study deals with issues like Cleavage, which deal with fields such as Alanine, Calpain, Proteolysis and Proteases. His work in the fields of Membrane and Dissociation constant overlaps with other areas such as Plasma.
John T. Penniston mainly focuses on Plasma membrane Ca2+ ATPase, Cell biology, Calcium pump, Calcium signaling and Cell membrane. His Plasma membrane Ca2+ ATPase research is under the purview of ATPase. The study incorporates disciplines such as Plasma Membrane Calcium-Transporting ATPases and Calcium-Transporting ATPases in addition to Cell biology.
His Calcium-Transporting ATPases research is multidisciplinary, relying on both Calcium and Stereocilia, Hair cell, Endolymph, Cochlea. John T. Penniston combines subjects such as Internal medicine and Endocrinology with his study of Hair cell. The Calcium pump study combines topics in areas such as Epithelial polarity, Calmodulin, Apical membrane, Protein structure and Gene isoform.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Purified (Ca2+-Mg2+)-ATPase of the erythrocyte membrane. Reconstitution and effect of calmodulin and phospholipids.
V Niggli;E S Adunyah;J T Penniston;E Carafoli.
Journal of Biological Chemistry (1981)
Partial purification of the Ca2+-Mg2+ ATPase activator from human erythrocytes: its similarity to the activator of 3':5' - cyclic nucleotide phosphodiesterase.
Harry W. Jarrett;John T. Penniston.
Biochemical and Biophysical Research Communications (1977)
Purification of the (Ca2+-Mg2+)-ATPase from human erythrocyte membranes using a calmodulin affinity column.
V Niggli;J T Penniston;E Carafoli.
Journal of Biological Chemistry (1979)
Mutations in the Na+/K+-ATPase α3 Gene ATP1A3 Are Associated with Rapid-Onset Dystonia Parkinsonism
Patricia de Carvalho Aguiar;Patricia de Carvalho Aguiar;Kathleen J Sweadner;John T Penniston;Jacek Zaremba.
Neuron (2004)
Complete primary structure of a human plasma membrane Ca2+ pump.
A K Verma;A G Filoteo;D R Stanford;E D Wieben.
Journal of Biological Chemistry (1988)
Plasma membrane Ca2+-ATPase isoform 2a is the PMCA of hair bundles.
Rachel A. Dumont;Ulysses Lins;Adelaida G. Filoteo;John T. Penniston.
The Journal of Neuroscience (2001)
Modification of Human Hearing Loss by Plasma-Membrane Calcium Pump PMCA2
Julie M. Schultz;Yandan Yang;Ariel J. Caride;Adelaida G. Filoteo.
The New England Journal of Medicine (2005)
The calmodulin binding domain of the plasma membrane Ca2+ pump interacts both with calmodulin and with another part of the pump.
A Enyedi;T Vorherr;P James;D J McCormick.
Journal of Biological Chemistry (1989)
Regulation of plasma membrane Ca2+ ATPases by lipids of the phosphatidylinositol cycle.
Debra Choquette;Gabriele Hakim;Adelaida G. Filoteo;Gordon A. Plishker.
Biochemical and Biophysical Research Communications (1984)
Controlled proteolysis of the purified Ca2+-ATPase of the erythrocyte membrane. A correlation between the structure and the function of the enzyme.
M Zurini;J Krebs;J T Penniston;E Carafoli.
Journal of Biological Chemistry (1984)
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