Glutamate 779, an intramembrane carboxyl, is essential for monovalent cation binding by the Na,K-ATPase (original) (raw)

Chemical modification of Glu-953 of the alpha chain of Na+,K(+)-ATPase associated with inactivation of cation occlusion

Proceedings of the National Academy of Sciences, 1992

Binding of Na+ ions to the Na,K-ATPase increases the reactivity of an essential residue in the ATP binding domain

Journal of Biological Chemistry, 1990

Modification of lysine 501 in Na,K-ATPase reveals coupling between cation occupancy and changes in the ATP binding domain

Jack Kaplan

Journal of Biological Chemistry, 1993

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Residues within Transmembrane Domains 4 and 6 of the Na,K-ATPase α Subunit Are Important for Na + Selectivity †

GLADIS GIL SANCHEZ

Biochemistry, 2004

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Molecular events in close proximity to the membrane associated with the binding of ligands to the Na,K-ATPase

S. Lutsenko

The Journal of biological chemistry, 1994

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Rapid kinetic analyses of the Na+/K+-ATPase distinguish among different criteria for conformational change

Promod Pratap

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1993

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Affinity labelling with MgATP analogues reveals coexisting Na+ and K+ forms of the alpha-subunits of Na+/K+-ATPase

Engin Serpersu

European Journal of Biochemistry, 1999

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Eight Amino Acids Form the ATP Recognition Site of Na + /K + -ATPase †

Vladimír Kopecký

Biochemistry, 2003

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Effects of competitive sodium-like antagonists on Na,K-ATPase suggest that cation occlusion from the cytoplasmic surface occurs in two steps

Alla Shainskaya

The Journal of biological chemistry, 1993

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A new variant of the gamma subunit of renal Na,K-ATPase. Identification by mass spectrometry, antibody binding, and expression in cultured cells

Alla Shainskaya

The Journal of biological chemistry, 2000

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Revealing of proteins interacting with Na,K-ATPase

Natalia Mast

Biochemistry. Biokhimii͡a, 2003

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Quaternary Benzyltriethylammonium Ion Binding to the Na,K-ATPase: A Tool to Investigate Extracellular K + Binding Reactions

Sergio Kaufman

Biochemistry, 2009

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Quaternary Benzyltriethylammonium Ion Binding to the Na,K-ATPase: A Tool to Investigate Extracellular K⁺ Binding Reactions

Sergio Kaufman

Biochemistry, 2009

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Phe475 and Glu446 but not Ser445 participate in ATP-binding to the α-subunit of Na+/K+-ATPase

Vladimír Kopecký

Biochemical and Biophysical Research Communications, 2002

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Chemical Modification with Dihydro-4,4′-diisothiocyanostilbene-2,2′-disulfonate Reveals the Distance between K480and K501in the ATP-Binding Domain of the Na,K-ATPase

Jack Kaplan

Archives of Biochemistry and Biophysics, 1997

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Effects of mono and divalent cations on total and partial reactions catalysed by pig kidney Na,K-ATPase

Luis Beaugé

The Journal of Physiology, 1986

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The intermediary complexes formed by (Na+ + K+)-dependent ATPase

Adil Shamoo

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1970

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Structure/Function Analysis of the Amino-terminal Region of the alpha 1 and alpha 2 Subunits of Na,K-ATPase

Stewart Daly

Journal of Biological Chemistry, 1996

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Na+/K+-ATPase: Activity and inhibition

Jasmina Savić, Danijela Krstić

Russian Journal of Physical Chemistry A, 2009

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Interactions between Na,K-ATPase alpha -Subunit ATP-binding Domains

Jack Kaplan

Journal of Biological Chemistry, 2003

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Isolation and cloning of the K +-independent, ouabain-insensitive Na +ATPase

Luz_Eduviges Thomas R

Biochimica Et Biophysica Acta-biomembranes, 2011

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Preparation of Na + ,K + -ATPase with Near Maximal Specific Activity and Phosphorylation Capacity: Evidence That the Reaction Mechanism Involves All of the Sites †

Dwight Martin

Biochemistry, 1999

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Inactivation of Rb+ and Na+ occlusion on (Na+,K+)-ATPase by modification of carboxyl groups

Daniel Tal

Journal of Biological Chemistry, 1988

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Microenvironment of the high affinity ATP-binding site of Na+/K+-ATPase is slightly acidic

Tomáš Obšil

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Membrane disposition of the M5-M6 hairpin of Na+,K(+)-ATPase alpha subunit is ligand dependent

S. Lutsenko

Proceedings of the National Academy of Sciences, 1995

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K + Congeners That Do Not Compromise Na + Activation of the Na + ,K + -ATPase

Yasser Mahmmoud, Wojciech Kopec

Journal of Biological Chemistry, 2014

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Cys577 Is a Conformationally Mobile Residue in the ATP-binding Domain of the Na,K-ATPase alpha -Subunit

Jack Kaplan

Journal of Biological Chemistry, 1999

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Functional Consequences of Various Leucine Mutations in the M3/M4 Loop of the Na+,K+-ATPase α-Subunit

yukichi hara

Journal of Membrane Biology, 2008

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The Fourth Transmembrane Segment of the Na,K-ATPase ␣ Subunit A SYSTEMATIC MUTAGENESIS STUDY* Received for publication

Saida Guennoun Lehmann

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Extracellular Domains, Transmembrane Segments, and Intracellular Domains Interact To Determine the Cation Selectivity of Na,K- and Gastric H,K-ATPase †

Martin Mense

Biochemistry, 2002

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Identification of the amino acid region involved in the intercellular interaction between the 1 subunits of Na+/K+-ATPase

Olga Vagin

Journal of Cell Science, 2012

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STUDIES ON THE TWO PHOSPHOENZYME CONFORMATIONS OF Na⁺+ K⁺-ATPase

Tai Akera

Annals of the New York Academy of Sciences, 1974

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A new variant of the γ subunit of renal Na, K-ATPase

Alla Shainskaya

Journal of Biological …, 2000

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Identification of intact ATP bound to (Na+ + K+)-ATPase

Adil Shamoo

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1971

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Identification of Two Conformationally Sensitive Cysteine Residues at the Extracellular Surface of the Na,K-ATPase alpha -Subunit

S. Lutsenko

Journal of Biological Chemistry, 1997

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Glutamate 779, an intramembrane carboxyl, is essential for monovalent cation binding by the Na,K-ATPase (original) (raw)

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