Substitutions of Aspartate 378 in the Phosphorylation Domain of the Yeast PMA1 H+-ATPase Disrupt Protein Folding and Biogenesis (Q56529293)

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10 November 2019

title

Substitutions of aspartate 378 in the phosphorylation domain of the yeast PMA1 H+-ATPase disrupt protein folding and biogenesis (English)

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10 November 2019

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Sergio Verjovski Almeida

2

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10 November 2019

author name string

R K Nakamoto

1

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10 November 2019

K E Allen

3

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10 November 2019

A Ambesi

4

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10 November 2019

R Rao

5

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10 November 2019

C W Slayman

6

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10 November 2019

language of work or name

English

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publication date

1 March 1998

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Journal of Biological Chemistry

10 November 2019

published in

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10 November 2019

volume

273

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10 November 2019

issue

13

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10 November 2019

page(s)

7338-7344

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Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases

10 November 2019

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Maturation of the yeast plasma membrane [H+]ATPase involves phosphorylation during intracellular transport

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Mutation of aspartic acid-351, lysine-352, and lysine-515 alters the Ca2+ transport activity of the Ca2+-ATPase expressed in COS-1 cells

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In-frame recombination between the yeast H(+)-ATPase isogenes PMA1 and PMA2: insights into the mechanism of recombination initiated by a double-strand break

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Expression of the sarcoplasmic reticulum Ca(2+)-ATPase in yeast.

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PMR1, a Ca2+-ATPase in yeast Golgi, has properties distinct from sarco/endoplasmic reticulum and plasma membrane calcium pumps

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Site-directed mutagenesis of Asp-376, the catalytic phosphorylation site, and Lys-507, the putative ATP-binding site, of the alpha-subunit of Torpedo californica Na+/K(+)-ATPase

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Amino Acid Replacement of Asp369 in the Sheep α1 Isoform Eliminates ATP and Phosphate Stimulation of [3]H Ouabain Binding to the Na+,K+-ATPase without Altering the Cation Binding Properties of the Enzyme

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