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A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria
scientific article
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instance of
scholarly article
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title
A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria
(English)
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main subject
bacteria
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author name string
C F Higgins
series ordinal
1
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I D Hiles
series ordinal
2
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G P Salmond
series ordinal
3
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D R Gill
series ordinal
4
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J A Downie
series ordinal
5
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I J Evans
series ordinal
6
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I B Holland
series ordinal
7
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L Gray
series ordinal
8
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S D Buckel
series ordinal
9
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A W Bell
series ordinal
10
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language of work or name
English
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publication date
October 1986
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stated in
PubMed
published in
Nature
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volume
323
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page(s)
448-50
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issue
6087
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cites work
Bacterial periplasmic transport systems: structure, mechanism, and evolution
1 reference
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https://api.crossref.org/works/10.1038%2F323448A0
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7 January 2021
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Different mechanisms of energy coupling for the active transport of proline and glutamine in Escherichia coli
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7 January 2021
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ATP-binding sites in the membrane components of histidine permease, a periplasmic transport system
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1038%2F323448A0
retrieved
7 January 2021
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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
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7 January 2021
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Substrate positions and induced-fit in crystalline adenylate kinase
1 reference
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7 January 2021
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ATP-binding site of adenylate kinase: mechanistic implications of its homology with ras-encoded p21, F1-ATPase, and other nucleotide-binding proteins
1 reference
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Crossref
reference URL
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7 January 2021
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Sequences of the recA gene and protein
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7 January 2021
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The nucleotide sequence of the uvrD gene of E. coli
1 reference
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7 January 2021
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Phosphate-binding sequences in nucleotide-binding proteins
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7 January 2021
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Complete nucleotide sequence and identification of membrane components of the histidine transport operon of S. typhimurium
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F323448A0
retrieved
7 January 2021
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Genetical and functional organisation of the Escherichia coli haemolysin determinant 2001
1 reference
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7 January 2021
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Transport of hemolysin across the outer membrane of Escherichia coli requires two functions
1 reference
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Crossref
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7 January 2021
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Identification of polypeptides required for the export of haemolysin 2001 from E. coli
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7 January 2021
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Identification of a membrane protein as a histidine transport component in Salmonella typhimurium
1 reference
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Crossref
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retrieved
7 January 2021
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Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F323448A0
retrieved
7 January 2021
based on heuristic
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Transport of hemolysin by Escherichia coli
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2F323448A0
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Sulphate sequestered in the sulphate-binding protein of Salmonella typhimurium is bound solely by hydrogen bonds
1 reference
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7 January 2021
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Novel stereospecificity of the L-arabinose-binding protein
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7 January 2021
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Sequence of the malK gene in E.coli K12
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7 January 2021
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Expression and regulation of the plasmid-encoded hemolysin determinant of Escherichia coli.
1 reference
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7 January 2021
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DNA sequence of the Rhizobium leguminosarum nodulation genes nodAB and C required for root hair curling.
1 reference
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https://api.crossref.org/works/10.1038%2F323448A0
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7 January 2021
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Identifiers
DOI
10.1038/323448A0
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4912417
Dimensions Publication ID
1017689834
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OpenCitations bibliographic resource ID
4912417
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4912417
PubMed ID
3762694
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
4912417
Springer Nature article ID
10.1038/323448a0
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