MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH

Md Amjad Beg; Mustafa Sevindik; Shahid Haider; Preeti Soni; Priya Bhatia; Shahzul Hasan; Richa Yadav; Fareeda Athar

doi:10.33483/jfpau.866876

Research Article

RV1463 OLASI KORUNMUŞ ATP BAĞLAYICI PROTEİNİN HESAPLAMALI YAKLAŞIMLA MOLEKÜLER TEMEL BÜTÜNLEŞTİRİCİ ANALİZİ

Year 2021, Volume: 45 Issue: 2, 212 - 226, 31.05.2021

Md Amjad Beg Mustafa Sevindik , Shahid Haider Preeti Soni Priya Bhatia Shahzul Hasan Richa Yadav Fareeda Athar

https://doi.org/10.33483/jfpau.866876

Cited By: 1

Abstract

Amaç: Tüberküloz, patojeni olan Mycobacterium tuberculosis H37Rv'nin (M. tuberculosis) şiddetle değişen dinamiği nedeniyle yıllardan beri küresel bir salgın olmuştur. Bu patojenin durumu daha da kötüleşmektedir ve üstesinden gelmek zorlaşmaktadır. Bu yazıda, metal iyonunun plazma membranları boyunca taşınmasına yardımcı olan ve sonuçta bir elektrokimyasal gradyan oluşturan Mycobacterium tuberculosis H37Rv'nin (M. tuberculosis) ATP bağlayıcı proteini için hesaplama yaklaşımlarını kullandı. Rv1463, ATP bağlama motifi (WalkerA) (GXXXXGKS / T) ve (Walkera) (DEXXXXXD) içeren varsayımsal bir protein ve bu motiflerin ATP bağlama ve hidrolizleme aktivitelerindeki önemi üzerinde duruldu. ATP bağlanma özelliğini, transkripsiyonel düzenleyici protein ile etkileşime girerek ve etkileşimli bileşikler magnezyum (Mg) ve Adenosin di fosfat (ADP) ile gösterir.

Gereç ve Yöntem: Rv1463'ün yapısı SwissModel web sunucusu tarafından oluşturuldu ve AutoDock kullanılarak moleküler yerleştirme yapıldı.

Sonuç ve Tartışma: Mutasyonel analizde, D175 kalıntılarının protein yapısını değiştirebilecek tüm etkileşimlerde ortak olduğunu doğrulandı. Bu hesaplama yaklaşımları, bu hastalığın tedavisinde yeni stratejiler geliştirmede yardımcı olabilir.

Keywords

Moleküler kenetlenme , Mycobacterium tuberculosis , rv1463 , tüberküloz

References

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2. Brennan, P.J. (2003). Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis. Tuberculosis (Edinb), 83(1‒3), 91‒97.
3. Beg, M.A., Shivangi Thakur S.C., Meena, L.S. (2018). Structural Prediction and Mutational Analysis of Rv3906c Gene of Mycobacterium tuberculosis H37Rv to Determine Its Essentiality in Survival. Adv Bioinformatics, 6152014.
4. Glaziou, P., Floyd, K., Raviglione, M.C. (2018). Global Epidemiology of Tuberculosis. Semin Respir Crit Care Med, 39(3), 271-285.
5. Ndlovu, H., Marakalala, M.J. (2016). Granulomas and Inflammation: Host-Directed Therapies for Tuberculosis. Front Immunol. 7, 434.
6. Silva Miranda, M., Breiman, A., Allain, S., Deknuydt, F., Altare, F. (2012). The tuberculous granuloma: an unsuccessful host defence mechanism providing a safety shelter for the bacteria? Clin Dev Immunol, 139127.
7. Russell, D.G., Cardona, P.J., Kim, M.J., Allain, S., Altare, F. (2009). Foamy macrophages and the progression of the human tuberculosis granuloma. Nat Immunol, 10(9), 943‒948.
8. Gandhi, N.R., Nunn, P., Dheda, K., Schaaf, H.S., Zignol, M., van Soolingen, D., Jensen, P., Bayona, J. (2010). Multidrug-resistant and extensively drug-resistant tuberculosis: a threat to global control of tuberculosis. Lancet, 375(9728),1830-1843.
9. Shivangi, Beg, A., Meena, S., Meena, L.S. (2017). To Find out the Essentiality of Rv0526 Gene in Virulence of Mycobacterium Tuberculosis by using in silico Approaches. Open J Bac, 1(1),013‒015.
10. Qiu, W., Liesa, M., Carpenter, E.P., Shirihai, O.S. (2015). ATP Binding and Hydrolysis Properties of ABCB10 and Their Regulation by Glutathione. PLoS One, 10(6),e0129772.
11. Braibant, M., Gilot, P., Content, J. (2000). The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis. FEMS Microbiol Rev, 24(4),449-467.
12. Cassio Barreto de Oliveira, M., Balan, A. (2020). The ATP-Binding Cassette (ABC) Transport Systems in Mycobacterium tuberculosis: Structure, Function, and Possible Targets for Therapeutics. Biology (Basel), 9(12),E443.
13. Soni, D.K., Dubey, S.K., Bhatnagar, R. (2020). ATP-binding cassette (ABC) import systems of Mycobacterium tuberculosis: target for drug and vaccine development. Emerg Microbes Infect, 27;9(1),207-220.
14. Balakrishnan, L., Venter, H., Shilling, R.A., van Veen, H.W. (2004). Reversible transport by the ATP-binding cassette multidrug export pump LmrA: ATP synthesis at the expense of downhill ethidium uptake. J Biol Chem, 279(12),11273-11280.
15. Ambudkar, S.V., Kim, I.W., Xia, D., Sauna, Z.E. (2006). The A-loop, a novel conserved aromatic acid subdomain upstream of the Walker A motif in ABC transporters, is critical for ATP binding. FEBS Lett, 580(4),1049-1055.
16. Orelle, C., Dalmas, O., Gros, P., Di Pietro, A., Jault, J.M. (2003). The conserved glutamate residue adjacent to the Walker-B motif is the catalytic base for ATP hydrolysis in the ATP-binding cassette transporter BmrA. J Biol Chem, 278(47),47002-47008.
17. Chen, M., Abele, R., Tampé, R. (2004). Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP). J Biol Chem, 279(44),46073-46081.
18. Vinothkumar, K.R., Henderson, R. (2010). Structures of membrane proteins. Q Rev Biophys, 43(1),65-158.
19. Marinko, J.T., Huang, H., Penn, W.D., Capra, J.A., Schlebach, J.P., Sanders, C.R. (2019). Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis. Chem Rev, 119(9),5537-5606.
20. Hung, L.W., Wang, I.X., Nikaido, K., Liu, P.Q., Ames, G.F., Kim, S.H. (1998). Crystal structure of the ATP-binding subunit of an ABC transporter. Nature, 396(6712),703-707.
21. Kapopoulou, A., Lew, J.M., Cole, S.T. (2011). The MycoBrowser portal: a comprehensive and manually annotated resource for mycobacterial genomes. Tuberculosis (Edinb), 91(1),8-13.
22. Shivangi, Beg, M.A., Meena, L.S. (2018). Insights of Rv2921c (Ftsy) Gene of Mycobacterium tuberculosis H37Rv To Prove Its Significance by Computational Approach. Biomed J Sci & Tech Res, 12(2),9147‒9157.
23. Beg, M.A., Shivangi, Thakur, S.C., Meena, L.S. (2019). Systematical analysis to assist the significance of Rv1907c gene with the pathogenic potentials of Mycobacterium tuberculosis H37Rv. J Biotechnol Biomat, 8(4),286.
24. Sievers, F., Higgins, D.G. (2014). Clustal Omega, accurate alignment of very large numbers of sequences. Methods Mol Biol, 1079,105-116.
25. von Mering, C., Huynen, M., Jaeggi, D., Schmidt, S., Bork, P., Snel, B. (2003). STRING: a database of predicted functional associations between proteins. Nucleic Acids Res, 31(1),258-261.
26. Beg, M.A., Athar, F., Meena, L.S. (2019). Significant Aspect of Rv0378 Gene of Mycobacterium tuberculosis H37Rv Reveals the PE_PGRS like Properties by Computational Approaches. J Biotechnol Biomed, 2(1),024‒039.
27. Rashid, M., Saha, S., Raghava, G.P. (2007). Support Vector Machine-based method for predicting subcellular localization of mycobacterial proteins using evolutionary information and motifs. BMC Bioinformatics, 8,337.
28. Yu, C.S., Cheng, C.W., Su, W.C., Chang, K.C., Huang, S.W., Hwang, J.K., Lu, C.H. (2014). CELLO2GO: a web server for protein subCELlular LOcalization prediction with functional gene ontology annotation. PLoS One, 9(6),e99368.
29. Beg, M.A., Shivangi, Athar, F., Meena, L.S. (2018). Structural and Functional Annotation of Rv1514c Gene of Mycobacterium tuberculosis H37Rv As Glycosyl Transferases. J Adv Res Biotech, 3(2),1‒9.
30. Bowie, J.U., Lüthy, R., Eisenberg, D. (1991). A method to identify protein sequences that fold into a known three-dimensional structure. Science, 253(5016),164–170.
31. Buchan, D.W.A., Jones, D.T. (2019). The PSIPRED Protein Analysis Workbench: 20 years on. Nucleic Acids Res, 47(W1),W402-W407.
32. Beg, M.A., Thakur, S.C., Athar, F. (2020). Computational annotations of mycobacterial Rv3632 that confers its efficient function in cell wall biogenesis. J Bacteriol Mycol Open Access, 8(2),46‒53.
33. Ma J, Wang S, Zhao F, Xu J. Protein threading using context-specific alignment potential. Bioinformatics, 2013;29(13), 257-265.
34. Biasini, M., Bienert, S., Waterhouse, A., Arnold, K., Studer, G., Schmidt, T., Kiefer, F., Gallo Cassarino, T., Bertoni, M., Bordoli, L., Schwede, T. (2014). SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res, 42(Web Server issue),W252-8.
35. Beg, M.A., Thakur, S.C., Athar, F. (2020). Molecular modeling and in silico characterization of mycobacterial Rv3101c and Rv3102c proteins: prerequisite molecular target in cell division. Pharm Pharmacol Int J, 8(4),234‒243.
36. Ho, B.K., Brasseur, R. (2005). The Ramachandran plots of glycine and pre-proline. BMC Struct Biol, 5,14.
37. Cristobal, S., Zemla, A., Fischer, D., Rychlewski, L., Elofsson, A. (2001). A study of quality measures for protein threading models. BMC Bioinformatics, 2,5.
38. Wallner, B., Elofsson, A. (2003). Can correct protein models be identified? Protein Sci, 12(5),1073‒1086.
39. Beg, M.A., Athar, F. (2020). Anti-HIV and Anti-HCV drugs are the putative inhibitors of RNA-dependent-RNA polymerase activity of NSP12 of the SARS CoV- 2 (COVID-19). Pharm Pharmacol Int J, 8(3), 163‒172.
40. Trott, O., Olson, A.J. (2010). Auto Dock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem, 31(2), 455–461.
41. Beg, M.A., Athar, F. (2020). Pharmacokinetic and molecular docking studies of Achyranthes aspera phytocompounds to exploring potential anti-tuberculosis activity. J Bacteriol Mycol Open Access, 8(1), 18‒27.
42. Biovia, D.S. (2015). Discovery studio modelling environment. San Diego. Dassault Systems.
43. Beg, M.A., Athar, F. (2020). Computational method in COVID-19: Revelation of Preliminary mutations of RdRp of SARS CoV-2 that build new horizons for therapeutic development. J Hum Virol Retrovirolog, 8(3), 62‒72.
44. Rodrigues, C.H., Pires, D.E., Ascher, D.B. (2018). DynaMut: predicting the impact of mutations on protein conformation, flexibility and stability. Nucleic Acids Res, 46(W1), W350–W355.
45. Shivangi, Beg, M.A., Meena, L.S. (2019). Mutational effects on structural stability of SRP pathway dependent cotranslational protein ftsY of Mycobacterium tuberculosis H37Rv. Gene Reports, 15, 100395.

MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH

Year 2021, Volume: 45 Issue: 2, 212 - 226, 31.05.2021

Md Amjad Beg Mustafa Sevindik , Shahid Haider Preeti Soni Priya Bhatia Shahzul Hasan Richa Yadav Fareeda Athar

https://doi.org/10.33483/jfpau.866876

Cited By: 1

Abstract

Objective: Tuberculosis as a global epidemic since years due to vigorously changing dynamics of its causal pathogen, Mycobacterium tuberculosis H37Rv (M. tuberculosis). This pathogen has worsened the situation therefore making it so challenging and hard to overcome. In this manuscript, we have used the computational approaches for ATP-binding protein of Mycobacterium tuberculosis H37Rv (M. tuberculosis) that helps in transportation of metal ion across the plasma membranes and resultant generating an electrochemical gradient. Rv1463 a hypothetical protein possessing ATP binding motif (WalkerA) (GXXXXGKS/T), and (Walker B) (DEXXXXXD) and significance of these motifs in ATP binding and hydrolyzing activities. It shows the ATP-binding property by interacting with transcriptional regulatory protein and showing the interacted compounds as magnesium (Mg) and Adenosine di phosphate (ADP).

Material and Method: The structure of Rv1463 has been build by the Swiss Model webserver and molecular docking was done using AutoDock.

Result and Discussion: In the mutational analysis which confirms that D175 residues was common in all interactions which may change the protein conformation. These computational approaches can be helpful in developing new strategies in treatment of this disease.

Keywords

Molecular docking , Mycobacterium tuberculosis , Rv1463 , tuberculosis

Thanks

The author Md. Amjad Beg also acknowledges University Grants Commission Maulana Azad National Fellowship for the support and Jamia Millia Islamia University.

References

1. Simmons, J.D., Stein, C.M., Seshadri, C., Campo, M., Alter, G., Fortune, S., Schurr, E., Wallis, R.S., Churchyard, G., Mayanja-Kizza, H., Boom, W.H., Hawn, T.R. (2018). Immunological mechanisms of human resistance to persistent Mycobacterium tuberculosis infection. Nat Rev Immunol, 18(9), 575-589.
2. Brennan, P.J. (2003). Structure, function, and biogenesis of the cell wall of Mycobacterium tuberculosis. Tuberculosis (Edinb), 83(1‒3), 91‒97.
3. Beg, M.A., Shivangi Thakur S.C., Meena, L.S. (2018). Structural Prediction and Mutational Analysis of Rv3906c Gene of Mycobacterium tuberculosis H37Rv to Determine Its Essentiality in Survival. Adv Bioinformatics, 6152014.
4. Glaziou, P., Floyd, K., Raviglione, M.C. (2018). Global Epidemiology of Tuberculosis. Semin Respir Crit Care Med, 39(3), 271-285.
5. Ndlovu, H., Marakalala, M.J. (2016). Granulomas and Inflammation: Host-Directed Therapies for Tuberculosis. Front Immunol. 7, 434.
6. Silva Miranda, M., Breiman, A., Allain, S., Deknuydt, F., Altare, F. (2012). The tuberculous granuloma: an unsuccessful host defence mechanism providing a safety shelter for the bacteria? Clin Dev Immunol, 139127.
7. Russell, D.G., Cardona, P.J., Kim, M.J., Allain, S., Altare, F. (2009). Foamy macrophages and the progression of the human tuberculosis granuloma. Nat Immunol, 10(9), 943‒948.
8. Gandhi, N.R., Nunn, P., Dheda, K., Schaaf, H.S., Zignol, M., van Soolingen, D., Jensen, P., Bayona, J. (2010). Multidrug-resistant and extensively drug-resistant tuberculosis: a threat to global control of tuberculosis. Lancet, 375(9728),1830-1843.
9. Shivangi, Beg, A., Meena, S., Meena, L.S. (2017). To Find out the Essentiality of Rv0526 Gene in Virulence of Mycobacterium Tuberculosis by using in silico Approaches. Open J Bac, 1(1),013‒015.
10. Qiu, W., Liesa, M., Carpenter, E.P., Shirihai, O.S. (2015). ATP Binding and Hydrolysis Properties of ABCB10 and Their Regulation by Glutathione. PLoS One, 10(6),e0129772.
11. Braibant, M., Gilot, P., Content, J. (2000). The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis. FEMS Microbiol Rev, 24(4),449-467.
12. Cassio Barreto de Oliveira, M., Balan, A. (2020). The ATP-Binding Cassette (ABC) Transport Systems in Mycobacterium tuberculosis: Structure, Function, and Possible Targets for Therapeutics. Biology (Basel), 9(12),E443.
13. Soni, D.K., Dubey, S.K., Bhatnagar, R. (2020). ATP-binding cassette (ABC) import systems of Mycobacterium tuberculosis: target for drug and vaccine development. Emerg Microbes Infect, 27;9(1),207-220.
14. Balakrishnan, L., Venter, H., Shilling, R.A., van Veen, H.W. (2004). Reversible transport by the ATP-binding cassette multidrug export pump LmrA: ATP synthesis at the expense of downhill ethidium uptake. J Biol Chem, 279(12),11273-11280.
15. Ambudkar, S.V., Kim, I.W., Xia, D., Sauna, Z.E. (2006). The A-loop, a novel conserved aromatic acid subdomain upstream of the Walker A motif in ABC transporters, is critical for ATP binding. FEBS Lett, 580(4),1049-1055.
16. Orelle, C., Dalmas, O., Gros, P., Di Pietro, A., Jault, J.M. (2003). The conserved glutamate residue adjacent to the Walker-B motif is the catalytic base for ATP hydrolysis in the ATP-binding cassette transporter BmrA. J Biol Chem, 278(47),47002-47008.
17. Chen, M., Abele, R., Tampé, R. (2004). Functional non-equivalence of ATP-binding cassette signature motifs in the transporter associated with antigen processing (TAP). J Biol Chem, 279(44),46073-46081.
18. Vinothkumar, K.R., Henderson, R. (2010). Structures of membrane proteins. Q Rev Biophys, 43(1),65-158.
19. Marinko, J.T., Huang, H., Penn, W.D., Capra, J.A., Schlebach, J.P., Sanders, C.R. (2019). Folding and Misfolding of Human Membrane Proteins in Health and Disease: From Single Molecules to Cellular Proteostasis. Chem Rev, 119(9),5537-5606.
20. Hung, L.W., Wang, I.X., Nikaido, K., Liu, P.Q., Ames, G.F., Kim, S.H. (1998). Crystal structure of the ATP-binding subunit of an ABC transporter. Nature, 396(6712),703-707.
21. Kapopoulou, A., Lew, J.M., Cole, S.T. (2011). The MycoBrowser portal: a comprehensive and manually annotated resource for mycobacterial genomes. Tuberculosis (Edinb), 91(1),8-13.
22. Shivangi, Beg, M.A., Meena, L.S. (2018). Insights of Rv2921c (Ftsy) Gene of Mycobacterium tuberculosis H37Rv To Prove Its Significance by Computational Approach. Biomed J Sci & Tech Res, 12(2),9147‒9157.
23. Beg, M.A., Shivangi, Thakur, S.C., Meena, L.S. (2019). Systematical analysis to assist the significance of Rv1907c gene with the pathogenic potentials of Mycobacterium tuberculosis H37Rv. J Biotechnol Biomat, 8(4),286.
24. Sievers, F., Higgins, D.G. (2014). Clustal Omega, accurate alignment of very large numbers of sequences. Methods Mol Biol, 1079,105-116.
25. von Mering, C., Huynen, M., Jaeggi, D., Schmidt, S., Bork, P., Snel, B. (2003). STRING: a database of predicted functional associations between proteins. Nucleic Acids Res, 31(1),258-261.
26. Beg, M.A., Athar, F., Meena, L.S. (2019). Significant Aspect of Rv0378 Gene of Mycobacterium tuberculosis H37Rv Reveals the PE_PGRS like Properties by Computational Approaches. J Biotechnol Biomed, 2(1),024‒039.
27. Rashid, M., Saha, S., Raghava, G.P. (2007). Support Vector Machine-based method for predicting subcellular localization of mycobacterial proteins using evolutionary information and motifs. BMC Bioinformatics, 8,337.
28. Yu, C.S., Cheng, C.W., Su, W.C., Chang, K.C., Huang, S.W., Hwang, J.K., Lu, C.H. (2014). CELLO2GO: a web server for protein subCELlular LOcalization prediction with functional gene ontology annotation. PLoS One, 9(6),e99368.
29. Beg, M.A., Shivangi, Athar, F., Meena, L.S. (2018). Structural and Functional Annotation of Rv1514c Gene of Mycobacterium tuberculosis H37Rv As Glycosyl Transferases. J Adv Res Biotech, 3(2),1‒9.
30. Bowie, J.U., Lüthy, R., Eisenberg, D. (1991). A method to identify protein sequences that fold into a known three-dimensional structure. Science, 253(5016),164–170.
31. Buchan, D.W.A., Jones, D.T. (2019). The PSIPRED Protein Analysis Workbench: 20 years on. Nucleic Acids Res, 47(W1),W402-W407.
32. Beg, M.A., Thakur, S.C., Athar, F. (2020). Computational annotations of mycobacterial Rv3632 that confers its efficient function in cell wall biogenesis. J Bacteriol Mycol Open Access, 8(2),46‒53.
33. Ma J, Wang S, Zhao F, Xu J. Protein threading using context-specific alignment potential. Bioinformatics, 2013;29(13), 257-265.
34. Biasini, M., Bienert, S., Waterhouse, A., Arnold, K., Studer, G., Schmidt, T., Kiefer, F., Gallo Cassarino, T., Bertoni, M., Bordoli, L., Schwede, T. (2014). SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res, 42(Web Server issue),W252-8.
35. Beg, M.A., Thakur, S.C., Athar, F. (2020). Molecular modeling and in silico characterization of mycobacterial Rv3101c and Rv3102c proteins: prerequisite molecular target in cell division. Pharm Pharmacol Int J, 8(4),234‒243.
36. Ho, B.K., Brasseur, R. (2005). The Ramachandran plots of glycine and pre-proline. BMC Struct Biol, 5,14.
37. Cristobal, S., Zemla, A., Fischer, D., Rychlewski, L., Elofsson, A. (2001). A study of quality measures for protein threading models. BMC Bioinformatics, 2,5.
38. Wallner, B., Elofsson, A. (2003). Can correct protein models be identified? Protein Sci, 12(5),1073‒1086.
39. Beg, M.A., Athar, F. (2020). Anti-HIV and Anti-HCV drugs are the putative inhibitors of RNA-dependent-RNA polymerase activity of NSP12 of the SARS CoV- 2 (COVID-19). Pharm Pharmacol Int J, 8(3), 163‒172.
40. Trott, O., Olson, A.J. (2010). Auto Dock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comput Chem, 31(2), 455–461.
41. Beg, M.A., Athar, F. (2020). Pharmacokinetic and molecular docking studies of Achyranthes aspera phytocompounds to exploring potential anti-tuberculosis activity. J Bacteriol Mycol Open Access, 8(1), 18‒27.
42. Biovia, D.S. (2015). Discovery studio modelling environment. San Diego. Dassault Systems.
43. Beg, M.A., Athar, F. (2020). Computational method in COVID-19: Revelation of Preliminary mutations of RdRp of SARS CoV-2 that build new horizons for therapeutic development. J Hum Virol Retrovirolog, 8(3), 62‒72.
44. Rodrigues, C.H., Pires, D.E., Ascher, D.B. (2018). DynaMut: predicting the impact of mutations on protein conformation, flexibility and stability. Nucleic Acids Res, 46(W1), W350–W355.
45. Shivangi, Beg, M.A., Meena, L.S. (2019). Mutational effects on structural stability of SRP pathway dependent cotranslational protein ftsY of Mycobacterium tuberculosis H37Rv. Gene Reports, 15, 100395.

There are 45 citations in total.

Details

Primary Language	English
Subjects	Pharmacology and Pharmaceutical Sciences
Journal Section	Research Article
Authors	Md Amjad Beg This is me 0000-0002-7555-1822 Mustafa Sevindik 0000-0001-7223-2220 Shahid Haider This is me 0000-0003-2661-4169 Preeti Soni This is me 0000-0002-0256-4040 Priya Bhatia This is me 0000-0002-7038-5562 Shahzul Hasan This is me 0000-0001-8677-1057 Richa Yadav This is me 0000-0002-7479-0629 Fareeda Athar This is me 0000-0001-8097-7206
Publication Date	May 31, 2021
Submission Date	January 23, 2021
Acceptance Date	March 1, 2021
Published in Issue	Year 2021 Volume: 45 Issue: 2

Cite

APA	Beg, M. A., Sevindik, M., Haider, S., … Soni, P. (2021). MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH. Journal of Faculty of Pharmacy of Ankara University, 45(2), 212-226. https://doi.org/10.33483/jfpau.866876
AMA	Beg MA, Sevindik M, Haider S, et al. MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH. J. Fac. Pharm. Ankara. May 2021;45(2):212-226. doi:10.33483/jfpau.866876
Chicago	Beg, Md Amjad, Mustafa Sevindik, Shahid Haider, Preeti Soni, Priya Bhatia, Shahzul Hasan, Richa Yadav, and Fareeda Athar. “MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH”. Journal of Faculty of Pharmacy of Ankara University 45, no. 2 (May 2021): 212-26. https://doi.org/10.33483/jfpau.866876.
EndNote	Beg MA, Sevindik M, Haider S, Soni P, Bhatia P, Hasan S, Yadav R, Athar F (May 1, 2021) MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH. Journal of Faculty of Pharmacy of Ankara University 45 2 212–226.
IEEE	M. A. Beg, M. Sevindik, S. Haider, P. Soni, P. Bhatia, S. Hasan, R. Yadav, and F. Athar, “MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH”, J. Fac. Pharm. Ankara, vol. 45, no. 2, pp. 212–226, 2021, doi: 10.33483/jfpau.866876.
ISNAD	Beg, Md Amjad et al. “MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH”. Journal of Faculty of Pharmacy of Ankara University 45/2 (May2021), 212-226. https://doi.org/10.33483/jfpau.866876.
JAMA	Beg MA, Sevindik M, Haider S, Soni P, Bhatia P, Hasan S, Yadav R, Athar F. MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH. J. Fac. Pharm. Ankara. 2021;45:212–226.
MLA	Beg, Md Amjad et al. “MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH”. Journal of Faculty of Pharmacy of Ankara University, vol. 45, no. 2, 2021, pp. 212-26, doi:10.33483/jfpau.866876.
Vancouver	Beg MA, Sevindik M, Haider S, Soni P, Bhatia P, Hasan S, et al. MOLECULAR BASIS AND INTEGRATIVE ANALYSIS OF Rv1463 AS PROBABLE CONSERVED ATP-BINDING PROTEIN BY COMPUTATIONAL APPROACH. J. Fac. Pharm. Ankara. 2021;45(2):212-26.

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The Journal of Faculty of Pharmacy of Ankara University is an international medium, an open access, peer-reviewed journal for the publication of original research reports, reviews and short communications in English or Turkish on relevant developments in pharmaceutical sciences., Proceeding of scientific meetings may be published as special issues of supplements to the journal. Additionally, it contains previous and forthcoming national and international scientific meetings with social activities in pharmaceutical areas.