The mitochondrial ATPase. Selective modification of a nitrogen residue in the beta subunit

The mitochondrial ATPase. Selective modification of a nitrogen residue in the beta subunit

Item
http://www.wikidata.org/entity/Q28323315
Significance of αThr-349 in the catalytic sites of Escherichia coli ATP synthase.Structural studies of the vacuolar membrane ATPase from Neurospora crassa and comparison with the tonoplast membrane ATPase from Zea maysATP synthase and the actions of inhibitors utilized to study its roles in human health, disease, and other scientific areas.Development of selective colorimetric probes for hydrogen sulfide based on nucleophilic aromatic substitution.A method for determining the adenosine triphosphatase content of energy-transducing membranes. reaction of 4-chloro-7-nitrobenzofurazan with the adenosine triphosphatase of bovine heart submitochondrial particles.Mitochondrial adenosine triphosphatase of the fission yeast Schizosaccharomyces pombe 972h-. Changes in inhibitor sensitivities during the cell cycle indicate similarities and differences in binding sites.Interaction of azidonitrophenylaminobutyryl--ADP, a photoaffinity ADP analog, with mitochondrial adenosine triphosphatase. Identification of the labeled subunits.The interaction of mitochondrial ATPase with an alkylating ATP-analog.Adenine nucleotide binding sites in chemically modified F1-ATPase: inhibitory effect of 4-chloro-7-nitrobenzofurazan on photolabeling by arylazido nucleotides.A common topology of proteins catalyzing ATP-triggered reactions.Interaction of ox heart mitochondrial F1-ATPase with immobilized ADP and ATP.Role of {alpha}-subunit VISIT-DG sequence residues Ser-347 and Gly-351 in the catalytic sites of Escherichia coli ATP synthase.Mutagenesis of residue betaArg-246 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F1-ATPase.Role of betaAsn-243 in the phosphate-binding subdomain of catalytic sites of Escherichia coli F(1)-ATPase.Inhibition of monoamine oxidase by 7-chloro-4-nitrobenzofurazan.Functional importance of αIle-346 and αIle-348 in the catalytic sites of Escherichia coli ATP synthase.Modulation of charge in the phosphate binding site of Escherichia coli ATP synthase.
P2860

The mitochondrial ATPase. Selective modification of a nitrogen residue in the beta subunit

Item
http://www.wikidata.org/entity/Q28323315
description
1975 nî lūn-bûn
@nan
1975 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
1975 թվականի մայիսին հրատարակված գիտական հոդված
@hy
1975年の論文
@ja
1975年論文
@yue
1975年論文
@zh-hant
1975年論文
@zh-hk
1975年論文
@zh-mo
1975年論文
@zh-tw
1975年论文
@wuu
name
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@ast
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@en
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@nl
type
label
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@ast
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@en
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@nl
prefLabel
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@ast
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@en
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P356
P1433
P1476
The mitochondrial ATPase. Sele ...... en residue in the beta subunit
@en
P2093
P304
P31
P356
10.1111/J.1432-1033.1975.TB04121.X
P407
P433
P478
P577
P5875
P698