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A universal system for the transport of redox proteins: early roots and latest developments
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scholarly article
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stated in
Europe PubMed Central
PubMed ID
11026678
retrieved
30 July 2017
review article
1 reference
stated in
Europe PubMed Central
title
A universal system for the transport of redox proteins: early roots and latest developments
(English)
1 reference
stated in
Europe PubMed Central
PubMed ID
11026678
retrieved
30 July 2017
author name string
Voordouw G
series ordinal
1
1 reference
stated in
Europe PubMed Central
PubMed ID
11026678
retrieved
30 July 2017
publication date
1 August 2000
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stated in
Europe PubMed Central
PubMed ID
11026678
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30 July 2017
published in
Biophysical Chemistry
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stated in
Europe PubMed Central
PubMed ID
11026678
retrieved
30 July 2017
volume
86
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stated in
Europe PubMed Central
PubMed ID
11026678
retrieved
30 July 2017
page(s)
131-140
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stated in
Europe PubMed Central
PubMed ID
11026678
retrieved
30 July 2017
issue
2-3
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Europe PubMed Central
PubMed ID
11026678
retrieved
30 July 2017
cites work
Isolation and physical studies of the intact supercoiled, the open circular and the linear forms of ColE1-plasmid DNA.
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Studies of ColE1-plasmid DNA and its interactions with histones: sedimentation velocity studies of monodisperse complexes reconstituted with calf-thymus histones
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Cloning of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough) and determination of the NH2-terminal sequence.
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Crossref
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7 January 2021
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Nucleotide sequence of the gene encoding the hydrogenase from Desulfovibrio vulgaris (Hildenborough).
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Putative signal peptide on the small subunit of the periplasmic hydrogenase from Desulfovibrio vulgaris
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Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas
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Unusual ligand structure in Ni-Fe active center and an additional Mg site in hydrogenase revealed by high resolution X-ray structure analysis
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Cloning, characterization, and sequencing of the genes encoding the large and small subunits of the periplasmic [NiFe]hydrogenase of Desulfovibrio gigas.
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Crossref
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Cloning and sequencing of the genes encoding the large and small subunits of the periplasmic (NiFeSe) hydrogenase of Desulfovibrio baculatus
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X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution
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Desulfovibrio desulfuricans iron hydrogenase: the structure shows unusual coordination to an active site Fe binuclear center
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Site-directed mutagenesis of the hydrogenase signal peptide consensus box prevents export of a beta-lactamase fusion protein
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Co-translocation of a Periplasmic Enzyme Complex by a Hitchhiker Mechanism through the Bacterial Tat Pathway
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The role of the twin-arginine motif in the signal peptide encoded by the hydA gene of the hydrogenase from wolinella succinogenes
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Cloning and nucleotide sequence of the structural genes encoding the formate dehydrogenase of Wolinella succinogenes
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Cloning, sequencing, and expression of the gene encoding the high-molecular-weight cytochrome c from Desulfovibrio vulgaris Hildenborough
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The hmc operon of Desulfovibrio vulgaris subsp. vulgaris Hildenborough encodes a potential transmembrane redox protein complex
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A common export pathway for proteins binding complex redox cofactors?
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Lack of copper insertion into unprocessed cytoplasmic nitrous oxide reductase generated by an R20D substitution in the arginine consensus motif of the signal peptide.
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Sec-independent protein translocation by the maize Hcf106 protein.
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Overlapping functions of components of a bacterial Sec-independent protein export pathway
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A novel and ubiquitous system for membrane targeting and secretion of cofactor-containing proteins.
1 reference
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Potential receptor function of three homologous components, TatA, TatB and TatE, of the twin-arginine signal sequence-dependent metalloenzyme translocation pathway in Escherichia coli
1 reference
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Sec-independent protein translocation in Escherichia coli. A distinct and pivotal role for the TatB protein.
1 reference
stated in
Crossref
reference URL
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retrieved
7 January 2021
based on heuristic
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Identifiers
DOI
10.1016/S0301-4622(00)00149-6
1 reference
stated in
Europe PubMed Central
PubMed ID
11026678
retrieved
30 July 2017
PubMed ID
11026678
1 reference
stated in
Europe PubMed Central
PubMed ID
11026678
retrieved
30 July 2017
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