Ethayathulla Abdul Samath
Affiliation
Additional Professor
Department of
Biophysics
Contact
Email :
ethayathulla@aiims.edu
Phone :
(O) +91- 11 26594816 / 26593351
Additional Responsibility
Office Address
R.No.3006, 3rd Floor Teaching Block ,All India Institute of Medical Sciences ,Ansari Nagar, New Delhi
General OPD
Special Clinic
Surgery Days
Speciality of work
Areas of teaching
Areas of teaching
Recent employment details:
- Additional Professor,since July 2020-Till date
- Associate Professor, since July 2017-June 2020
- Assistant Professor,since June 2014-June 2017
Any additional information:
Associate Professor (2017 - till date):Biophysics, AIIMS, New Delhi, India
Assistant Professor (2014 – 2017):Biophysics, AIIMS, New Delhi, India
Research Associate (2012-2014):Texas Tech University Health Science center, Texas, USA
Post doctoral Fellow (2007 - 2012):University of California San Diego, California, USA.
Ph.D. (Biophysics, 2007):AllMS, New Delhi
Master of Science (Biophysics, 2002):University of Madras, Chennai
Bachelor of Science (Physics -2000):University of Madras, Chennai
- Senior Research Fellowship awarded by CSIR, New Delhi, India.
- Senior Research Fellowship in the project from DST, New Delhi, India.
- Junior Research Fellowship in the project from DST, New Delhi, India.
- Junior Research Fellowship in the project from DBT, New Delhi, India.
Research Interests:
The research work is focused on TP53 tumor suppressor gene plays crucial role in suppression of cancer. But the mutation in p53 leads to tumour proliferation sometimes drug resistance cancer cells. The research focused on targeting mutant p53 with structure-based drug design to restore mutant p53 to functional like wild type. We do structure-based drug design by X-ray crystallography and for drug binding and functional studies we various biophysical techniques like ITC, CD, Fluorescence and cell based functional assay in p53 mutant cell lines.
The second major project in our lab is antimicrobial drug development against drug resistant bacterial pathogen. We work on bacterial cell division proteins particularly FtsZ and its associate proteins involved forming divisome protein complex assembly. We do structure-based drug design by X-ray crystallography, In silico drug screening and for drug binding studies we various biophysical techniques like ITC, CD, Fluorescence.
Recent Publications:
- Yadav P, Kumar M, Bansal R, Kaur P, Ethayathulla AS. Structure model of ferrochelatase from Salmonella Typhi elucidating metalation mechanism. Int J Biol Macromol. 2019 Apr 15;127:585-593.
- Bansal R, Haque MA, Yadav P, Gupta D, Ethayathulla AS, Hassan MI, Kaur P. Estimation of structure and stability of MurE ligase from Salmonella enterica serovar Typhi. Int J Biol Macromol. 2018 Apr 1;109:375-382.
- Gupta D, Sachdeva E, Haque MA, Rahman S, Bansal R, Ethayathulla AS, Hassan MI, Kaur P. Effect of chemical denaturants on the conformational stability of GyrB subunit of DNA gyrase from Salmonella enterica serovar Typhi. Int J Biol Macromol. 2017 May 9;103:165-174.
- Khan MI, Gupta AK, Kumar DR, Kumar M, Ethayathulla AS, Hariprasad G. Molecular modeling of Gly80 and Ser80 variants of human group IID phospholipase A2 and their receptor complexes: potential basis for weight loss in chronic obstructive pulmonary disease. J Mol Model. 2016 Sep;22(9):232.
- Ramos A, Tse PW, Wang J, Ethayathulla AS, Viadiu H. Sequence Variation in the Response Element Determines Binding by the Transcription Factor p73. Biochemistry. 2015 Dec 1;54(47):6961-72.
- Tikhonova EB, Ethayathulla AS, Su Y, Hariharan P, Xie S, Guan L. A transcription blocker isolated from a designed repeat protein combinatorial library by in vivo functional screen. Sci Rep. 2015 Jan 28;5:8070.
- Amin A, Ethayathulla AS, Guan L. Suppression of conformation-compromised mutants of Salmonella enterica serovar Typhimurium MelB. J Bacteriol. 2014;196(17):3134-9.
- Ethayathulla AS, Yousef MS, Amin A, Leblanc G, Kaback HR, Guan L. Structure-based mechanism for Na(+)/melibiose symport by MelB. Nat Commun. 2014;5:3009.
- Ciribilli Y, Monti P, Bisio A, Nguyen T, Ethayathulla AS, Ramos A, Foggetti G, Menichini P, Menendez D, Resnick M, Viadiu H, Fronza G, Inga A. Transactivation specificity is conserved among p53 family proteins and depends on a response element sequence code. Nucleic Acids Res. 2013 Oct;41(18):8637-53.
- Ethayathulla AS, Nguyen HT, Viadiu H. Crystal Structures of the DNA-binding Domain Tetramer of the p53 Tumor Suppressor Family Member p73 Bound to Different Full-site Response Elements. J Biol Chem. 2013; 288(7):4744-54.
- Ethayathulla AS, Tse P, Monti P, Nguyen S, Inga A, Fronza G, Viadiu H. Structure of p73 DNA-Binding Domain Tetramer Modulates p73 Transactivation. Proc Natl Acad Sci U S A. 2012 Apr 17;109(16):6066-71.
- Soni BR, Hasan MI, Parmar A, Ethayathulla AS, Kumar RP, Singh NK, Sinha M, Kaur P, Yadav S, Sharma S, Madamwar D, Singh TP. Structure of the novel 14kDa fragment of alpha-subunit of phycoerythrin from the starving cyanobacterium Phormidium tenue. J Struct Biol. 2010 171(3):247-55.
- Mishra P, Prem Kumar R, Ethayathulla AS, Singh N, Sharma S, Perbandt M, Betzel C, Kaur P, Srinivasan A, Bhakuni V, Singh TP. Polysaccharide binding sites in hyaluronate lyase--crystal structures of native phage-encoded hyaluronate lyase and its complexes with ascorbic acid and lactose. FEBS J. 2009 276(12):3392-402.
- Ethayathulla AS, Bessho Y, Shinkai A, Padmanabhan B, Singh TP, Kaur P, Yokoyama S. Purification, crystallization and preliminary X-ray diffraction analysis of the putative ABC transporter ATP-binding protein from Thermotoga maritima. Acta Crystallogr Sect F. 2008 (64) 498-500.
