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Cited by 430

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Crystal Structure and Function of the Isoniazid Target of Mycobacterium tuberculosis

Dessen, Andréa, Quémard, Annaïk, Blanchard, John S., Jacobs, William R., Sacchettini, James C.·1995·Science

Abstract

Resistance to isoniazid in Mycobacterium tuberculosis can be mediated by substitution of alanine for serine 94 in the InhA protein, the drug's primary target. InhA was shown to catalyze the β-nicotinamide adenine dinucleotide (NADH)-specific reduction of 2- trans -enoyl-acyl carrier protein, an essential step in fatty acid elongation. Kinetic analyses suggested that isoniazid resistance is due to a decreased affinity of the mutant protein for NADH. The three-dimensional structures of wild-type and mutant InhA, refined to 2.2 and 2.7 angstroms, respectively, revealed that drug resistance is directly related to a perturbation in the hydrogen-bonding network that stabilizes NADH binding.

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Metadata

Authors
Dessen, A., Quémard, A., Blanchard, J. S., Jacobs, W. R., & Sacchettini, J. C.
Venue
Science
Published
1995-03-17
Volume
267
Issue
5204
Pages
1638-1641
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2117610468
Cited by
430
References
2
FWCI
26.14
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Crystal Structure and Function of the Isoniazid Target of Mycobacterium tuberculosis. https://app.cochat.ai/papers/10.1126/science.7886450
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Dessen, A., Quémard, A., Blanchard, J. S., Jacobs, W. R., & Sacchettini, J. C. (1995). Crystal Structure and Function of the Isoniazid Target of Mycobacterium tuberculosis. Science. https://doi.org/10.1126/science.7886450

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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