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Crystal structure of the ATP-binding subunit of an ABC transporter
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title
Crystal structure of the ATP-binding subunit of an ABC transporter
(English)
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main subject
crystal structure
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author
Sung-Hou Kim
series ordinal
6
object named as
S H Kim
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author name string
L W Hung
series ordinal
1
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I X Wang
series ordinal
2
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K Nikaido
series ordinal
3
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P Q Liu
series ordinal
4
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G F Ames
series ordinal
5
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language of work or name
English
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publication date
17 December 1998
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published in
Nature
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volume
396
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issue
6712
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page(s)
703-7
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cites work
ATP-dependent transport systems in bacteria and humans: relevance to cystic fibrosis and multidrug resistance
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Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity
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Characterization of transport through the periplasmic histidine permease using proteoliposomes reconstituted by dialysis.
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Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter).
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The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface
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In vitro disassembly and reassembly of an ABC transporter, the histidine permease
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The structure of the E. coli recA protein monomer and polymer
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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria
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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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Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation
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Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis
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Modeling of nucleotide binding domains of ABC transporter proteins based on a F1-ATPase/recA topology: structural model of the nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator (CFTR)
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Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
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Improvement of macromolecular electron-density maps by the simultaneous application of real and reciprocal space constraints.
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PROCHECK: a program to check the stereochemical quality of protein structures
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Identifiers
DOI
10.1038/25393
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Dimensions Publication ID
1009478150
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PubMed publication ID
9872322
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ResearchGate publication ID
13416768
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