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drug development
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due to developed resistance against the existing anti-tubercular drugs by Mycobacteriumm tuberculosis, the enzyme is a target for drug development. Targeting uridyltranferase activity of Mtu GlmU would be a better choice for therapeutic intervention, since at low metabolite concentrations, inhibition of either of the GlmU reactions cause significant decrement in the overall GlmU rate, but at higher metabolite concentrations, uridyltransferase inhibition shows higher decrement, overview
drug development
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GlmU is a target for drug development against Mycobacteria
drug development
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GlmU is a target for inhibitor design
drug development
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GlmU is a target for inhibitor design
drug development
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GlmU is a target for inhibitor design
drug development
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GlmU is a target for inhibitor design
drug development
the enzyme is a target for inhibitor development in treatment of tuberculosis
drug development
the enzyme GlmU is a target for development of antibacterial drugs
drug development
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GlmU is a target for inhibitor design
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drug development
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GlmU is a target for inhibitor design
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drug development
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GlmU is a target for inhibitor design
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drug development
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GlmU is a target for inhibitor design
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medicine
GlmU is a potential antituberculosis drug target, a microtiter plate assay for GlmU activity as read out is developed
medicine
arylsulphatase AtsG , bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyl transferase GlmU and S-adenosyl-L-homocysteine hydrolase SahH are the Mycobacterium tuberculosis proteins that bind to human IL-8. The interactions with IL-8 are characterized by high binding affinity with KD values of 6.83x10-6 M, 5.24x10-6 M and 7.14x10-10 M, respectively. Strains overproducing the enzymes show a significantly increased number of intracellularly located bacilli compared with those of wild-type
medicine
GlmUMtb is a strong candidate for intervention measures against established tuberculosis infections
medicine
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GlmU is a potential antituberculosis drug target, a microtiter plate assay for GlmU activity as read out is developed
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medicine
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arylsulphatase AtsG , bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyl transferase GlmU and S-adenosyl-L-homocysteine hydrolase SahH are the Mycobacterium tuberculosis proteins that bind to human IL-8. The interactions with IL-8 are characterized by high binding affinity with KD values of 6.83x10-6 M, 5.24x10-6 M and 7.14x10-10 M, respectively. Strains overproducing the enzymes show a significantly increased number of intracellularly located bacilli compared with those of wild-type
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medicine
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GlmUMtb is a strong candidate for intervention measures against established tuberculosis infections
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medicine
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arylsulphatase AtsG , bifunctional glucosamine-1-phosphate acetyltransferase and N-acetylglucosamine-1-phosphate uridyl transferase GlmU and S-adenosyl-L-homocysteine hydrolase SahH are the Mycobacterium tuberculosis proteins that bind to human IL-8. The interactions with IL-8 are characterized by high binding affinity with KD values of 6.83x10-6 M, 5.24x10-6 M and 7.14x10-10 M, respectively. Strains overproducing the enzymes show a significantly increased number of intracellularly located bacilli compared with those of wild-type
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medicine
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GlmUMtb is a strong candidate for intervention measures against established tuberculosis infections
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additional information
the increase in activity induced by some substitutions and truncations may be a useful feature that can be exploited for commercial application of this enzyme
additional information
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the increase in activity induced by some substitutions and truncations may be a useful feature that can be exploited for commercial application of this enzyme
additional information
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the increase in activity induced by some substitutions and truncations may be a useful feature that can be exploited for commercial application of this enzyme
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additional information
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the increase in activity induced by some substitutions and truncations may be a useful feature that can be exploited for commercial application of this enzyme
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