About: Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases

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About: Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases Goto Sponge NotDistinct Permalink

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scientific article published on 01 May 1999

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rdf:type	Item
description	wetenschappelijk artikel (nl) bài báo khoa học (vi) наукова стаття, опублікована в травні 1999 (uk) im Mai 1999 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en mayu de 1999 (ast) scientific article published on 01 May 1999 (en)
publication date	wds:Q77726336-4F1E49C2-3177-4EE9-9CA5-395052C4DC26
publication date	1999-05-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q77726336-0310D7F3-9074-4892-8F62-823C5C285918
language of work or name	English
cites work	wds:Q77726336-15003B39-1FEF-4A99-A148-1740644FF69A wds:Q77726336-23351DAC-E39C-43FD-90A0-0AC707A9ED32 wds:Q77726336-265A96CA-5251-49C9-9F67-C2E2B1C0C7DC wds:Q77726336-315BC3CD-C099-453C-9767-BAB93CC43531 wds:Q77726336-32A2BAD2-AF54-4B1C-BB35-ECC815BF683D wds:Q77726336-3FE2B8CF-9F29-4E96-BA66-28496E2915A6 wds:Q77726336-449D2E2B-611E-4B83-9289-FB7827E6DF3F wds:Q77726336-483EDC35-A53D-48CA-B0F8-C8D8D8AC0C14 wds:Q77726336-48A5338A-1711-46FB-AC9F-FEF358802DEA wds:Q77726336-507452DC-05DC-49F9-9523-DC1F80FEF203 wds:Q77726336-59BD08B4-7F8C-4CD7-9996-7D1D66B3C26F wds:Q77726336-5CED590F-7A8E-46DE-BE15-D8E9B8F386A7 wds:Q77726336-6C43CD0F-70DD-4253-80EA-F2D443AFF995 wds:Q77726336-737B26F3-8D5C-416D-8FDA-A486CCF01A7D wds:Q77726336-95F1DB2B-7737-4BC2-BE83-FEB63B7D79EF wds:Q77726336-99AEC490-F681-4F0C-8654-C87BBF62E0BD wds:Q77726336-9B6716A7-5851-4B9A-97C3-4DA704F14D18 wds:Q77726336-A2C42F54-A464-4AD2-9A6D-6422141ABB64 wds:Q77726336-A51A52A6-C0C6-44A6-8C7D-023E2DB1A419 wds:Q77726336-AFF3CCC3-B60E-48C7-B333-33D5D585AFFD wds:Q77726336-CBBE7D5A-B383-4540-AD6F-D0579DFA1BCB wds:Q77726336-D2D815EC-9E49-4F11-B148-2F8323E38D20 wds:Q77726336-E375FED5-30FD-494B-AF76-6A30B291A7BD wds:Q77726336-EE1BB83D-DF10-4F5A-A1DF-54E6EBC716C6
cites work	Structural aspects of the gastric H,K ATPase Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Only the first and the last hydrophobic segments in the COOH-terminal third of Na,K-ATPase alpha subunit initiate and halt, respectively, membrane translocation of the newly synthesized polypeptide. Implications for the membrane topology A simple method for displaying the hydropathic character of a protein The M4M5 cytoplasmic loop of the Na,K-ATPase, overexpressed in Escherichia coli, binds nucleoside triphosphates with the same selectivity as the intact native protein. Functional consequences of mutations in the transmembrane core region for cation translocation and energy transduction in the Na+,K(+)-ATPase and the SR Ca(2+)-ATPase Organization of P-type ATPases: significance of structural diversity Membrane topology and omeprazole labeling of the gastric H+,K(+)-adenosinetriphosphatase Scanning mutagenesis reveals a similar pattern of mutation sensitivity in transmembrane sequences M4, M5, and M6, but not in M8, of the Ca2+-ATPase of sarcoplasmic reticulum (SERCA1a) Membrane disposition of the M5-M6 hairpin of Na+,K(+)-ATPase alpha subunit is ligand dependent. The nature of the accessible and buried surfaces in proteins Cation and cardiac glycoside binding sites of the Na,K-ATPase. beta-subunit assembly is essential for the correct packing and the stable membrane insertion of the H,K-ATPase alpha-subunit. Location of the carbohydrates present in the HK-ATPase vesicles isolated from hog gastric mucosa Sites of reaction of the gastric H,K-ATPase with extracytoplasmic thiol reagents. A 19-kDa C-terminal tryptic fragment of the alpha chain of Na/K-ATPase is essential for occlusion and transport of cations Occluded cations in active transport The membrane topology of the rat sarcoplasmic and endoplasmic reticulum calcium ATPases by in vitro translation scanning Identification of the site of inhibition by omeprazole of a alpha-beta fusion protein of the H,K-ATPase using site-directed mutagenesis. Role of negatively charged residues in the fifth and sixth transmembrane domains of the catalytic subunit of gastric H+,K+-ATPase Structural domains implicated in ER degradation of alpha subunits of Na,K-ATPase. Identification of two conformationally sensitive cysteine residues at the extracellular surface of the Na,K-ATPase alpha-subunit Soluble and active renal Na,K-ATPase with maximum protein molecular mass 170,000 ± 9,000 daltons; formation of larger units by secondary aggregation Ligand-induced conformational changes in the Na,K-ATPase alpha subunit
author name string	wds:Q77726336-10AC08C9-6654-43A4-93BD-91F7942960ED wds:Q77726336-1E47E464-89DD-4B7A-9BCD-88B6084902CD wds:Q77726336-8D247F3C-87D7-499F-B227-2E9779DD8A64 wds:Q77726336-CB8FEF27-1965-46EA-A09D-B1560D74E21E
author name string	G Sachs J M Shin S Lutsenko C Gatto
rdfs:label	Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases (en) Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases (nl)
skos:prefLabel	Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases (en) Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases (nl)
name	Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases (en) Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases (nl)
author	wds:Q77726336-A9C0A1BF-E593-4CAE-AD6E-55678CDD9186
author	Jack H. Kaplan
title	wds:Q77726336-99398654-FD4A-4716-9B03-64F5C0641212
title	Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases (en)
page(s)	wds:Q77726336-1D1F093C-237E-40CB-AA04-F5B81486E491
page(s)	13737-13740
instance of	wds:Q77726336-CE08AE55-ABA8-495C-8A1F-E33C09602A46
instance of	scholarly article
PubMed ID	wds:Q77726336-3D733069-EE63-4EF2-9A5F-33F932A44A1E
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10318774
PubMed ID	10318774
published in	wds:Q77726336-BED5A5E4-2C7E-4A49-8262-D8580C9C6682
published in	Journal of Biological Chemistry
issue	wds:Q77726336-200A0921-A18F-4101-929E-8F39928135F2
volume	wds:Q77726336-4193E803-6740-4AF1-AA12-95AD1C96424E
issue	20
volume	274
DOI	wds:Q77726336-388087CD-0F73-4B86-BADE-78AE0A328919
DOI	http://dx.doi.org/10.1074/JBC.274.20.13737
DOI	10.1074/JBC.274.20.13737
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q77726336
is cites work of	Structural changes in the calcium pump accompanying the dissociation of calcium Structural similarities of Na,K-ATPase and SERCA, the Ca(2+)-ATPase of the sarcoplasmic reticulum Abolishment of proton pumping and accumulation in the E1P conformational state of a plant plasma membrane H+-ATPase by substitution of a conserved aspartyl residue in transmembrane segment 6 Conformational dynamics of the Na+/K+-ATPase probed by voltage clamp fluorometry Conserved Asp684 in transmembrane segment M6 of the plant plasma membrane P-type proton pump AHA2 is a molecular determinant of proton translocation High-affinity ouabain binding by a chimeric gastric H+,K+-ATPase containing transmembrane hairpins M3-M4 and M5-M6 of the alpha 1-subunit of rat Na+,K+-ATPase

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