About: 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

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About: 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 Goto Sponge NotDistinct Permalink

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scientific article published on 01 December 2000

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в грудні 2000 (uk) مقالة علمية تنشرت ف 1 دجنبر 2000 (ary) article scientifique publié en 2000 (fr) im Dezember 2000 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'avientu de 2000 (ast) scientific article published on 01 December 2000 (en)
publication date	wds:Q74338949-DA3DDB87-DD95-44C6-B0DE-90B8AB14B766
publication date	2000-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q74338949-36A558A8-3EC6-46BD-AE9E-81D582B001A6
language of work or name	English
cites work	wds:Q74338949-039B66FD-BC40-4166-A181-459042199ACD wds:Q74338949-157FA44B-1B5F-44F6-9A8D-B17C820F236B wds:Q74338949-2F09C231-05A3-4B1E-BA5E-209443B311DF wds:Q74338949-2FCC021A-A41A-41DB-BACF-5DED541A3D5E wds:Q74338949-3FC250EA-19C7-4DF9-B05A-DBDDB3A4B79C wds:Q74338949-40DF3A90-5E9F-46D8-9EB7-772AECB855B9 wds:Q74338949-42AEB38B-D060-4B55-8536-76989C954EFA wds:Q74338949-43BAA554-B6B1-4372-8F45-442265A55F52 wds:Q74338949-4DA97CE3-0E89-4F80-A772-C714A482A1A1 wds:Q74338949-4DAF0E6F-81AA-40C4-82CA-5DE68357C1B4 wds:Q74338949-5E6BF31E-AB37-44CD-A298-BE175158DEC8 wds:Q74338949-5F14C111-8B43-4AD0-8FE3-CF419E94AED7 wds:Q74338949-601F63F4-95E0-490C-851F-BFB6E55DE1E4 wds:Q74338949-6432DFE5-E664-4E34-8042-D78F42255070 wds:Q74338949-67DF104D-5B16-4299-A52C-8C47E0541766 wds:Q74338949-6F9071F6-4D7D-4668-B0E5-8EB1AB7BE646 wds:Q74338949-70CDE936-8EED-4CF3-A43D-BC57CF758F4A wds:Q74338949-72A82BAE-1640-458B-896F-01933CD34020 wds:Q74338949-8055A6E6-D103-4B5B-BD02-FD5027E80691 wds:Q74338949-8471E08B-2A90-4BCC-8863-E5E1F0F81735 wds:Q74338949-8B87484E-4DAA-48D5-88A3-1B5278D3AC78 wds:Q74338949-8BCA6DFA-CFD3-43BE-9ECA-CCE68A4F5DCD wds:Q74338949-90064C7D-A047-4E2D-913E-325934D4CC7D wds:Q74338949-9E5772F6-1F05-41FF-B2C5-E2071DBFFE6E wds:Q74338949-9F37D22B-2FCD-4E27-8001-B518211DF1DA wds:Q74338949-AE324FC8-E130-478B-8776-965525A38336 wds:Q74338949-C5B195A3-C3F3-4AB6-A0A3-DE67443DA8A8 wds:Q74338949-C81DA021-9EEF-4E22-81FA-3102F5FCFEC6 wds:Q74338949-CA8F5B94-6EC6-4BD9-B7E2-A17079F33108 wds:Q74338949-D29D192D-18F2-49A4-87EA-1864CEC6FA7F wds:Q74338949-D3CF66ED-678C-425B-8A2D-4FED0C23D3C4 wds:Q74338949-DAC78289-0F00-4203-8CBB-E6CBFAA7B664 wds:Q74338949-E6397671-A8A8-462C-8D38-3583D40F1B24
cites work	Structural basis for E1-E2 conformational transitions in Na,K-pump and Ca-pump proteins Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution Peptide and protein molecular weight determination by electrophoresis using a high-molarity tris buffer system without urea. 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. Site-directed mutagenesis by overlap extension using the polymerase chain reaction Site-directed mutagenesis of the Na,K-ATPase: consequences of substitutions of negatively-charged amino acids localized in the transmembrane domains. Structure of the calcium pump from sarcoplasmic reticulum at 8-Å resolution Leucine 332 at the boundary between the fourth transmembrane segment and the cytoplasmic domain of Na+,K+-ATPase plays a pivotal role in the ion translocating conformational changes Importance of intramembrane carboxylic acids for occlusion of K+ ions at equilibrium in renal Na,K-ATPase Three-dimensional map of the plasma membrane H+-ATPase in the open conformation. Evolution of substrate specificities in the P-type ATPase superfamily. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Structural organization, ion transport, and energy transduction of P-type ATPases Location of high affinity Ca2+-binding sites within the predicted transmembrane domain of the sarcoplasmic reticulum Ca2+-ATPase 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. Stabilization of the H,K-ATPase M5M6 membrane hairpin by K+ ions. Mechanistic significance for p2-type atpases Yeast/E. coli shuttle vectors with multiple unique restriction sites Metabolic modulation of transport coupling ratio in yeast plasma membrane H(+)-ATPase Molecular dissection of the C-terminal regulatory domain of the plant plasma membrane H+-ATPase AHA2: mapping of residues that when altered give rise to an activated enzyme Substitution of glutamic 779 with alanine in the Na,K-ATPase alpha subunit removes voltage dependence of ion transport. Evidence for a salt bridge between transmembrane segments 5 and 6 of the yeast plasma-membrane H+-ATPase Purification of a histidine-tagged plant plasma membrane H+-ATPase expressed in yeast Asp804 and Asp808 in the transmembrane domain of the Na,K-ATPase alpha subunit are cation coordinating residues Mutation Lys758 --> Ile of the sarcoplasmic reticulum Ca2+-ATPase enhances dephosphorylation of E2P and inhibits the E2 to E1Ca2 transition The 14-3-3 protein interacts directly with the C-terminal region of the plant plasma membrane H(+)-ATPase Role of negatively charged residues in the fifth and sixth transmembrane domains of the catalytic subunit of gastric H+,K+-ATPase Identification of Asp804 and Asp808 as Na+ and K+ coordinating residues in alpha-subunit of renal Na,K-ATPase The plant plasma membrane H(+)-ATPase: structure, function and regulation Structure-function relationships in membrane segment 5 of the yeast Pma1 H+-ATPase. Stalk segment 4 of the yeast plasma membrane H+-ATPase. Mutational evidence for a role in the E1-E2 conformational change. Critical effects on catalytic function produced by amino acid substitutions at Asp804 and Asp808 of the alpha1 isoform of Na,K-ATPase Two residues that may ligate Ca2+ in transmembrane domain six of the plasma membrane Ca(2+)-ATPase
author name string	wds:Q74338949-1DA019FA-E0B6-430C-98F2-439AE957FB7B wds:Q74338949-291920DD-84AD-4A72-B321-AC6E6C327ABB
author name string	Serrano R Buch-Pedersen MJ
rdfs:label	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 (en) 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 (nl)
skos:prefLabel	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 (en) 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 (nl)
name	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 (en) 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 (nl)
author	wds:Q74338949-74E49D49-59F0-4198-8941-4B86ABDACC77 wds:Q74338949-FFD79DC6-737D-4BAC-A6CD-F4D8F6E83F49
author	Kees Venema Michael Broberg Palmgren
title	wds:Q74338949-284C3A81-580C-426D-9E06-3A2E8731BD34
title	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 (en)
page(s)	wds:Q74338949-207BA8D1-ACB7-4836-B154-FFD4765A5ADC
page(s)	39167-39173
instance of	wds:Q74338949-0DF9DAB7-381F-45B9-B0D5-535F3963D5C0
instance of	scholarly article
PubMed ID	wds:Q74338949-FAD6F339-103C-4E52-9948-74402BBD64F7
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10995773

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