Results 241 to 250 of about 493,727 (307)
Integrating Structural, Biochemical, and Cellular Perspectives on the TFIIH Helicases XPB and XPD. [PDF]
BiomoleculesBravo M, Fan L.
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Mechanistic elucidation of a terpenoid nano-bionematicide for the management of root-knot nematodes, Meloidogyne incognita infecting tomato. [PDF]
Sci RepArunachalam L, Lakshmanan S, Ganeshan S.
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Ionoregulatory and hematological parameters of Triportheus albus populations living in natural white- and blackwaters of the Amazon. [PDF]
J Comp Physiol BDuarte RM +6 more
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Annual Review of Biophysics, 2011
P-type ATPases form a large superfamily of cation and lipid pumps. They are remarkably simple with only a single catalytic subunit and carry out large domain motions during transport. The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by
Palmgren, Michael G., Nissen, Poul
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P-type ATPases form a large superfamily of cation and lipid pumps. They are remarkably simple with only a single catalytic subunit and carry out large domain motions during transport. The atomic structure of P-type ATPases in different conformations, together with ample mutagenesis evidence, has provided detailed insights into the pumping mechanism by
Palmgren, Michael G., Nissen, Poul
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Molecular and Cellular Biochemistry, 1981
An ecto-adenosine triphosphatase (E.C. 3.6.1.4 ATP-phosphohydrolase) is shown to be localized on the outer surface of varieties of cell membrane. The enzyme is different from the ATPase involved in biological energy transduction and ion transport mechanism.
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An ecto-adenosine triphosphatase (E.C. 3.6.1.4 ATP-phosphohydrolase) is shown to be localized on the outer surface of varieties of cell membrane. The enzyme is different from the ATPase involved in biological energy transduction and ion transport mechanism.
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Current Opinion in Nephrology and Hypertension, 1999
The H+,K+-ATPases comprise a group of integral membrane proteins that belong to the X+,K+-ATPase subfamily of P-type cation-transporting ATPases. Although these H+,K+-ATPase isoforms share approximately 60-70% amino acid identity, they exhibit discrete kinetic and pharmacological properties when expressed in heterologous systems.
T D, DuBose, J, Gitomer, J, Codina
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The H+,K+-ATPases comprise a group of integral membrane proteins that belong to the X+,K+-ATPase subfamily of P-type cation-transporting ATPases. Although these H+,K+-ATPase isoforms share approximately 60-70% amino acid identity, they exhibit discrete kinetic and pharmacological properties when expressed in heterologous systems.
T D, DuBose, J, Gitomer, J, Codina
openaire +2 more sources