The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis

Article Abstract:

Some Mycobacterium tuberculosis (M. tuberculosis) strains are becoming resistant to the anti-tuberculosis drug isoniazid. The resistant strains' lack of the gene katG encoding the enzymes catalase and peroxidase has been found to cause isoniazid's diminished therapeutic effectiveness. This finding was verified when insertion of katG in the resistant bacteria Mycobacterium smegmatis and Escherichia coli caused them to again be susceptible to isoniazid. Furthermore, removal of katG from M. tuberculosis chromosome was linked to isoniazid resistance in two patient isolates of M. tuberculosis.

Health aspects, Genetic aspects, Drug resistance in microorganisms, Microbial drug resistance, Enzymes, Mycobacterium tuberculosis, Peroxidase, Isoniazid

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NIP domain prevents N-type inactivation in voltage-gated potassium channels

Article Abstract:

It has been established that neither Kv1.4- nor Kv-beta-1.1-ball domains rapidly inactivate hetermultimeric Kv channels containing Kv1.6 subunits, even though these channels have a functional ball receptor and a conserved Kv-beta-1-binding domain. N-type inactivation was restored through deletion or mutation of the N-type inactivation-prevention domain. This research has established a new channel for the gating behaviour of heteromultimeric Kv channels.

Potassium channels

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Receptor-associated Mad homologues synergize as effectors of the TGF-beta response

Article Abstract:

The human Mad homologues hMad-3 and -4 synergize to produce strong ligand-independent transforming growth factor-beta (TGF-beta) responses. They act as dominant-negative inhibitors of the normal TGF-beta response when truncated at the carboxy terminal. The hMad-4 homolgue is identical to DPC-4 and functions as a tumour suppressor. The inactivation of DPC-4 prevents transforming TGF-beta responsiveness and the attenuation of growth.

Antineoplastic agents, Transforming growth factors

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