(Q27930841)

P-type ATPases of eukaryotes and bacteria: sequence analyses and construction of phylogenetic trees

GOA release 2020-03-11

author

André Goffeau

series ordinal

3

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author name string

P Catty

series ordinal

1

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A de Kerchove d'Exaerde

series ordinal

2

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language of work or name

English

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publication date

16 June 1997

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1 reference

1 December 2016

409

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page(s)

325-32

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issue

3

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cites work

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Organization of P-type ATPases: significance of structural diversity

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Sequence, mapping and disruption of CCC2, a gene that cross-complements the Ca(2+)-sensitive phenotype of csg1 mutants and encodes a P-type ATPase belonging to the Cu(2+)-ATPase subfamily.

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The yeast secretory pathway is perturbed by mutations in PMR1, a member of a Ca2+ ATPase family.

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The yeast Ca(2+)-ATPase homologue, PMR1, is required for normal Golgi function and localizes in a novel Golgi-like distribution

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Identification and phylogenetic classification of eleven putative P-type calcium transport ATPase genes in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe

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A subfamily of P-type ATPases with aminophospholipid transporting activity

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A PMR2 tandem repeat with a modified C-terminus is located downstream from the KRS1 gene encoding lysyl-tRNA synthetase in Saccharomyces cerevisiae

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A novel P-type ATPase from yeast involved in sodium transport

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Differential expression of two genes encoding isoforms of the ATPase involved in sodium efflux in Saccharomyces cerevisiae

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The Wilson disease gene is a putative copper transporting P-type ATPase similar to the Menkes gene

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Automated construction and graphical presentation of protein blocks from unaligned sequences.

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A family of cation ATPase-like molecules from Plasmodium falciparum

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Molecular cloning and sequence of two novel P-type adenosinetriphosphatases from Plasmodium falciparum.

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2-D structure of the Neurospora crassa plasma membrane ATPase as determined by electron cryomicroscopy.

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