Indexed keywords
ADENOSINE TRIPHOSPHATE;
DRUG DERIVATIVE;
INSECT PROTEIN;
PRIMER DNA;
PROTEIN SUBUNIT;
PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;
AEDES;
ANIMAL;
ARTICLE;
ENZYME ACTIVE SITE;
ENZYMOLOGY;
GENE;
GENE EXPRESSION;
GENETICS;
IN VITRO STUDY;
ISOLATION AND PURIFICATION;
MASS SPECTROMETRY;
METABOLISM;
MOLECULAR CLONING;
NUCLEOTIDE SEQUENCE;
SPECTROFLUOROMETRY;
ADENOSINE TRIPHOSPHATE;
AEDES;
ANIMALS;
BASE SEQUENCE;
CATALYTIC DOMAIN;
CLONING, MOLECULAR;
DNA PRIMERS;
GENE EXPRESSION;
GENES, INSECT;
INSECT PROTEINS;
PROTEIN SUBUNITS;
SPECTROMETRY, FLUORESCENCE;
SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;
VACUOLAR PROTON-TRANSLOCATING ATPASES;
AEDES ALBOPICTUS;
ASCOGREGARINA TAIWANENSIS;
ESCHERICHIA COLI;
EUKARYOTA;
1
0032946360
Vacuolar and plasma membrane proton-adenosine triphosphatases
Nelson N., and Harvey W.R. Vacuolar and plasma membrane proton-adenosine triphosphatases. Physiol. Rev. 79 (1999) 361-385
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Nelson, N.1
Harvey, W.R.2
3
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Subunit composition, structure, and distribution of bacterial V-Type ATPase
Lolkema J.S., Chaban Y., and Boekema E.J. Subunit composition, structure, and distribution of bacterial V-Type ATPase. J. Bioenerg. Biomembr. 35 (2003) 323-336
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J. Bioenerg. Biomembr.
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Lolkema, J.S.1
Chaban, Y.2
Boekema, E.J.3
4
0142057284
Subunit structure, function, and arrangement in the yeast and coated vesicle V-ATPases
Inoue T., Wilkens S., and Forgac M. Subunit structure, function, and arrangement in the yeast and coated vesicle V-ATPases. J. Bioenerg. Biomembr. 35 (2000) 291-300
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J. Bioenerg. Biomembr.
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Inoue, T.1
Wilkens, S.2
Forgac, M.3
5
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ATP syntases: structure, function and evolution of unique energy converters
Müller V., and Grüber G. ATP syntases: structure, function and evolution of unique energy converters. Cell Mol. Life Sci. 60 (2003) 474-494
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Cell Mol. Life Sci.
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Müller, V.1
Grüber, G.2
6
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An expanded and flexible form of the vacuolar ATPase membrane sector
Clare D.K., et al. An expanded and flexible form of the vacuolar ATPase membrane sector. Structure 14 (2006) 1149-1156
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Structure
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Clare, D.K.1
7
0027319652
+-ATPase membrane sector
+-ATPase membrane sector. J. Biol. Chem. 268 (1993) 12749-12757
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J. Biol. Chem.
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Bauerle, C.1
9
0344875467
1-ATPase: affinity purification and structural features by electron microscopy
1-ATPase: affinity purification and structural features by electron microscopy. J. Biol. Chem. 278 (2003) 47299-47306
(2003)
J. Biol. Chem.
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Zhang, Z.1
10
0033766435
The structure of the central stalk in bovine F(1)-ATPase at 2.4 Å resolution
Gibbons C., et al. The structure of the central stalk in bovine F(1)-ATPase at 2.4 Å resolution. Nat. Struct. Biol. 7 (2000) 1055-1061
(2000)
Nat. Struct. Biol.
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, pp. 1055-1061
Gibbons, C.1
11
33644828691
+ V-ATPase in the mosquito Aedes albopictus is tightly associated with gregarine infection
+ V-ATPase in the mosquito Aedes albopictus is tightly associated with gregarine infection. J. Eukaryot. Microbiol. 53 (2006) 127-135
(2006)
J. Eukaryot. Microbiol.
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Huang, C.-G.1
12
0014949207
Cleavage of structural proteins during the assembly of the head of bacteriophage T4
Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
(1970)
Nature
, vol.227
, pp. 680-685
Laemmli, U.K.1
13
0009482260
Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76 (1979) 4350-4354
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Proc. Natl. Acad. Sci. USA
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Towbin, H.1
Staehelin, T.2
Gordon, J.3
15
0031002520
Detailed peptide characterization using PEPTIDEMASS - a World-Wide-Web-accessible tool
Wilkins M.R., et al. Detailed peptide characterization using PEPTIDEMASS - a World-Wide-Web-accessible tool. Electrophoresis 18 (1979) 403-408
(1979)
Electrophoresis
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Wilkins, M.R.1
16
0034810614
8-N(3)-3′-biotinyl-ATP, a novel monofunctional reagent: differences in the F(1)- and V(1)-ATPases by means of the ATP analogue
Schäfer H.-J., et al. 8-N(3)-3′-biotinyl-ATP, a novel monofunctional reagent: differences in the F(1)- and V(1)-ATPases by means of the ATP analogue. Biochem. Biophys. Res. Commun. 286 (2001) 1218-1227
(2001)
Biochem. Biophys. Res. Commun.
, vol.286
, pp. 1218-1227
Schäfer, H.-J.1
17
0024669473
2+-ATPase of sarcoplasmic reticulum with the disulfide of 3′(2′)-O-biotinyl-thioinosine triphosphate
2+-ATPase of sarcoplasmic reticulum with the disulfide of 3′(2′)-O-biotinyl-thioinosine triphosphate. Eur. J. Biochem. 181 (1989) 503-511
(1989)
Eur. J. Biochem.
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Kison, R.1
Meyer, H.E.2
Schoner, W.3