A 19-kDa C-terminal tryptic fragment of the alpha chain of Na/K-ATPase is essential for occlusion and transport of cations.
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Inhibition of K+ transport through Na+, K+-ATPase by capsazepine: role of membrane span 10 of the α-subunit in the modulation of ion gatingThermal denaturation of the Na,K-ATPase provides evidence for alpha-alpha oligomeric interaction and gamma subunit association with the C-terminal domain.Membrane disposition of the M5-M6 hairpin of Na+,K(+)-ATPase alpha subunit is ligand dependent.Replacement of glycine 232 by aspartic acid in the KdpA subunit broadens the ion specificity of the K(+)-translocating KdpFABC complexIdentification of electric-field-dependent steps in the Na(+),K(+)-pump cycle.Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum.Tissue-specific distribution and modulatory role of the gamma subunit of the Na,K-ATPase.Constraints on models for the folding of the Na,K-ATPase.The amino-terminal segment of the catalytic subunit of kidney Na,K-ATPase regulates the potassium deocclusion pathway of the reaction cycle.Equilibrium of phosphointermediates of sodium and potassium ion transport adenosine triphosphatase: action of sodium ion and Hofmeister effectThe role of Na,K-ATPase alpha subunit serine 775 and glutamate 779 in determining the extracellular K+ and membrane potential-dependent properties of the Na,K-pumpFe-catalyzed cleavage of the alpha subunit of Na/K-ATPase: evidence for conformation-sensitive interactions between cytoplasmic domainsChemical modification of Glu-953 of the alpha chain of Na+,K(+)-ATPase associated with inactivation of cation occlusion.Site-directed chemical labeling of extracellular loops in a membrane protein. The topology of the Na,K-ATPase alpha-subunit.Protein kinase C phosphorylation of purified Na,K-ATPase: C-terminal phosphorylation sites at the alpha- and gamma-subunits close to the inner face of the plasma membrane.Direct activation of gastric H,K-ATPase by N-terminal protein kinase C phosphorylation. Comparison of the acute regulation mechanisms of H,K-ATPase and Na,K-ATPase.Characterization of disulfide cross-links between fragments of proteolyzed Na,K-ATPase. Implications for spatial organization of trans-membrane helices.Asp804 and Asp808 in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues.Functional consequences of alterations to Pro328 and Leu332 located in the 4th transmembrane segment of the alpha-subunit of the rat kidney Na+,K(+)-ATPase.K+ congeners that do not compromise Na+ activation of the Na+,K+-ATPase: hydration of the ion binding cavity likely controls ion selectivity.Role of the self-association of beta subunits in the oligomeric structure of Na+/K+-ATPase.Probing of the membrane topology of sarcoplasmic reticulum Ca2+-ATPase with sequence-specific antibodies. Evidence for plasticity of the c-terminal domain.Curcumin modulation of Na,K-ATPase: phosphoenzyme accumulation, decreased K+ occlusion, and inhibition of hydrolytic activity.Covalent cross-links between the gamma subunit (FXYD2) and alpha and beta subunits of Na,K-ATPase: modeling the alpha-gamma interaction.The role of loop 6/7 in folding and functional performance of Na,K-ATPase.Photoinactivation of fluorescein isothiocyanate-modified Na,K-ATPase by 2'(3')-O-(2,4,6-trinitrophenyl)8-azidoadenosine 5'-diphosphate. Abolition of E1 and E2 partial reactions by sequential block of high and low affinity nucleotide sites.Isoform-specific monoclonal antibodies to Na,K-ATPase alpha subunits. Evidence for a tissue-specific post-translational modification of the alpha subunit.Topology of the Na,K-ATPase. Evidence for externalization of a labile transmembrane structure during heating.Do transmembrane segments in proteolyzed sarcoplasmic reticulum Ca(2+)-ATPase retain their functional Ca2+ binding properties after removal of cytoplasmic fragments by proteinase K?Interactions between fragments of trypsinized Na,K-ATPase detected by thermal inactivation of Rb+ occlusion and dissociation of the M5/M6 fragment.Substitutions of serine 775 in the alpha subunit of the Na,K-ATPase selectively disrupt K+ high affinity activation without affecting Na+ interaction.Transmembrane topology of alpha- and beta-subunits of Na+,K+-ATPase derived from beta-galactosidase fusion proteins expressed in yeast.Characterization of the Secondary Structure and Assembly of the Transmembrane Domains of Trypsinized Na,K-ATPase by Fourier Transform Infrared Spectroscopy
P2860
Q28538680-D858EBAE-3C9D-493A-BA8E-7E2BEABDBD1FQ31636906-2F541A00-8806-4906-A3DA-B702BF266670Q34018696-70860387-87D4-462C-AA03-3A7913B3E020Q34173641-21CA10C9-D213-4C31-A042-89B26E8F0A44Q34203746-5E5C50EC-5543-4B2F-9AFE-D13CD98B6D4DQ34271890-1032DD20-C589-4313-B85D-E3AA337DEC74Q34450048-B06028AD-478D-4E3D-A93A-9BE6EB86664AQ35167850-2B783E90-AAAD-4903-9996-4A1028DE9AD7Q36028005-153066AE-27FE-4E41-9A6D-E2359F106471Q36411864-6F1E5FD4-87D2-4409-8800-770F77D1CB8EQ36436731-898DBFA8-5450-441A-BDAC-37EDF379BDBEQ36569774-FE203142-E87E-43D3-83B0-EB69136BB767Q37127272-7BEE7E8B-A6CF-4974-803E-6E2409BA5EF4Q38313317-A775ECD9-21D3-40CA-91A7-DA802903CC30Q40204361-33EDD1E8-B8F2-4F8C-896C-993CCD6523EEQ40231192-48643051-AF48-45CD-9328-66BB1D0F1739Q40978877-FC1EB851-8A8F-42F9-ABC8-95D7F4667FBCQ41150449-F258B657-554D-4FCF-816E-4D49A28EEEC1Q41589191-7AAD6049-1F84-41DA-A7AB-8AE087E49733Q41657807-A7CB15A8-485F-4FF9-9830-826DB0B67493Q41898817-6F12A25C-2379-4C80-B768-12553E839105Q42666899-293E4D22-00E0-459A-9EAF-C59BD164CCB5Q43261468-1339A7C5-69DF-4C31-9004-2449FFC38D7CQ45295574-A8954FAD-AC96-467F-B9D4-D35824EBC361Q46130612-7FE104EC-244F-4961-843D-AA0F61DCA648Q48034678-5476A458-E0D7-4E4A-A706-71158ADBDD6FQ48915323-C0D5F082-9FC2-45F9-BBDF-4A449A010A84Q50113269-C2161339-9397-4240-B1E8-7C47A54725CEQ52509100-66AA18A3-F739-4438-8052-D0855F884635Q52529687-08E68B14-ACCC-4D06-A8F8-A8C82A9DAF37Q54162226-2F8220EB-0866-4F02-9750-D90D0C1CB631Q54577134-57BFA2CE-DB29-4136-9914-E78A9C548C50Q55016322-F93823DF-D074-4482-8EFC-F0044A43182C
P2860
A 19-kDa C-terminal tryptic fragment of the alpha chain of Na/K-ATPase is essential for occlusion and transport of cations.
description
1990 nî lūn-bûn
@nan
1990 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
A 19-kDa C-terminal tryptic fr ...... sion and transport of cations.
@ast
A 19-kDa C-terminal tryptic fr ...... sion and transport of cations.
@en
type
label
A 19-kDa C-terminal tryptic fr ...... sion and transport of cations.
@ast
A 19-kDa C-terminal tryptic fr ...... sion and transport of cations.
@en
prefLabel
A 19-kDa C-terminal tryptic fr ...... sion and transport of cations.
@ast
A 19-kDa C-terminal tryptic fr ...... sion and transport of cations.
@en
P2093
P2860
P356
P1476
A 19-kDa C-terminal tryptic fr ...... sion and transport of cations.
@en
P2093
Goldshleger R
Karlish SJ
P2860
P304
P356
10.1073/PNAS.87.12.4566
P407
P577
1990-06-01T00:00:00Z