• Publications
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Funnel-like Hexameric Assembly of the Periplasmic Adapter Protein in the Tripartite Multidrug Efflux Pump in Gram-negative Bacteria*
  • Y. Xu, M. Lee, +6 authors N. Ha
  • Chemistry, Medicine
  • The Journal of Biological Chemistry
  • 29 March 2011
Gram-negative bacteria expel diverse toxic chemicals through the tripartite efflux pumps spanning both the inner and outer membranes. The Escherichia coli AcrAB-TolC pump is the principal multidrugExpand
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Membrane Fusion Proteins of Type I Secretion System and Tripartite Efflux Pumps Share a Binding Motif for TolC in Gram-Negative Bacteria
The Hly translocator complex of Escherichia coli catalyzes type I secretion of the toxin hemolysin A (HlyA). In this complex, HlyB is an inner membrane ABC (ATP Binding Cassette)-type transporter,Expand
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Interruption of progerin-lamin A/C binding ameliorates Hutchinson-Gilford progeria syndrome phenotype.
Hutchinson-Gilford progeria syndrome (HGPS) is a rare autosomal dominant genetic disease that is caused by a silent mutation of the LMNA gene encoding lamins A and C (lamin A/C). The G608G mutationExpand
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Inhibitory effects of arbutin-β-glycosides synthesized from enzymatic transglycosylation for melanogenesis
To develop a new skin whitening agent, arbutin-β-glycosides were synthesized and evaluated for their melanogenesis inhibitory activities. Three active compounds were synthesized via theExpand
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Assembly and Channel Opening of Outer Membrane Protein in Tripartite Drug Efflux Pumps of Gram-negative Bacteria*
  • Y. Xu, A. Moeller, +5 authors N. Ha
  • Biology, Medicine
  • The Journal of Biological Chemistry
  • 3 February 2012
Background: Pseudomonas aeruginosa mainly achieves multidrug resistance by use of the MexAB-OprM pump. Results: We determined the crystal structure of MexA. Electron microscopy work using MexA andExpand
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Characterization of an exo-acting intracellular α-amylase from the hyperthermophilic bacterium Thermotoga neapolitana
We cloned and expressed the gene for an intracellular α-amylase, designated AmyB, from the hyperthermophilic bacterium Thermotoga neapolitana in Escherichia coli. The putative intracellularExpand
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Modulation of the regioselectivity of a Thermotoga neapolitana beta-glucosidase by site-directed mutagenesis.
Thermotoga neapolitana beta-glucosidase (BglA) was subjected to site-directed mutagenesis in an effort to increase its ability to synthesize arbutin derivatives by transglycosylation. TheExpand
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Crystal structure and thermostability of a putative α-glucosidase from Thermotoga neapolitana.
Glycoside hydrolase family 4 (GH4) represents an unusual group of glucosidases with a requirement for NAD(+), Mn(2+), and reducing conditions. We found a putative α-glucosidase belonging to GH4 inExpand
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Structure of a novel α-amylase AmyB from Thermotoga neapolitana that produces maltose from the nonreducing end of polysaccharides.
An intracellular α-amylase, AmyB, has been cloned from the hyperthermophilic bacterium Thermotoga neapolitana. AmyB belongs to glycoside hydrolase family 13 and liberates maltose from diverseExpand
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