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1.
Int J Tuberc Lung Dis ; 26(1): 12-17, 2022 Jan 01.
Article in English | MEDLINE | ID: mdl-34969423

ABSTRACT

BACKGROUND: Tobacco and TB are the world´s two greatest public health problems. Exposure to tobacco has been shown to be associated with higher risk of acquiring TB and adverse outcomes such as relapse and TB mortality.OBJECTIVE: To assess and compare self-reported tobacco quit status and biochemically verified cotinine levels among TB patients at different time intervals among two study groups.METHODS: A cluster, randomised controlled trial was conducted on TB patients attending DOTS centres in Delhi, India, who reported using tobacco in any form. Participants were assigned into one of two treatment groups. Centres were randomly assigned to two intervention groups: 1) integrated intervention using behavioural counselling with nicotine replacement therapy (NRT) gum, and 2) intervention using behavioural counselling alone (50 each in intervention and control group). The subjects were followed at Week 1, Month 1, Month 3 and Month 6 for tobacco cessation.RESULTS: At the end of 6 months, patients who received the integrated intervention had significantly higher rate of success in quitting tobacco than those who received the conventional TB treatment alone (78.7% vs. 57.8%; P < 0.03).CONCLUSION: DOTS with tobacco use dependence treatment was successful in our study in helping TB patients to quit tobacco dependence and should therefore be offered to every tobacco user.


Subject(s)
Smoking Cessation , Tobacco Use Cessation , Tobacco Use Disorder , Humans , Cotinine , Smoking Cessation/methods , Tobacco Use Cessation Devices , Tobacco Use Disorder/complications , Tobacco Use Disorder/therapy , Tuberculosis
2.
J Protein Chem ; 19(7): 545-51, 2000 Oct.
Article in English | MEDLINE | ID: mdl-11233167

ABSTRACT

By comparing the average structures, computed using molecular dynamics, of the ras-binding domain of raf (RBD) bound to activated wild-type ras-p21 and its homologous inhibitory protein, rap-1A, we formerly identified three domains of the RBD that changed conformation between the two complexes, residues 62-76, 97-110, and 111-121. We found that one synthetic peptide, corresponding to RBD residues 97-110, selectively inhibited oncogenic ras-p21-induced oocyte maturation. In this study, we performed molecular dynamics on the Val 12-ras-p21-RBD complex and compared its average structure with that for the wild-type protein. We find that there is a large displacement of a loop involving these residues when the structures of the two complexes are compared. This result corroborates our former finding that the RBD 97-110 peptide inhibits only signal transduction by oncogenic ras-p21 and suggests that oncogenic p21 uses this loop to interact with raf in a unique manner.


Subject(s)
Oncogene Protein p21(ras)/chemistry , Proto-Oncogene Proteins c-raf/chemistry , Amino Acid Substitution , Binding Sites , Humans , Models, Molecular , Nonlinear Dynamics , Oncogene Protein p21(ras)/antagonists & inhibitors , Oncogene Protein p21(ras)/metabolism , Peptide Fragments/metabolism , Peptide Fragments/pharmacology , Protein Binding , Protein Conformation , Protein Structure, Tertiary , Proto-Oncogene Proteins c-raf/metabolism , Proto-Oncogene Proteins c-raf/pharmacology , Proto-Oncogene Proteins p21(ras)/chemistry , Proto-Oncogene Proteins p21(ras)/metabolism , Signal Transduction/drug effects , rap1 GTP-Binding Proteins/chemistry , rap1 GTP-Binding Proteins/metabolism
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