Aneel K Aggarwal, PhD
- PROFESSOR | Pharmacological Sciences
- PROFESSOR | Oncological Sciences
Research Topics:DNA Repair, DNA Replication, Structural Biology, Transcription Factors, Translation
Dr. Aggarwal is an internationally recognized structural biologist, who earned his PhD in biophysics at Kings College, University of London, in 1984. From 1985 to 1987, Dr. Aggarwal participated in a NATO research fellowship and was also a postdoctoral fellow in the Department of Biochemistry and Molecular Biology at Harvard University. He then became an Assistant Professor at Columbia University before joining the Mount Sinai Medical School. He is currently a Professor in the Department of Structural & Chemical Biology and holds an Endowed Chair as the Mount Sinai Professor in Structural Biology.
Multi-Disciplinary Training AreasBiophysics and Systems Pharmacology [BSP], Cancer Biology [CAB], Genetics and Genomic Sciences [GGS]
PhD, Kings College, University of London
Dean’s Award for Excellence in Basic Science Research
Faculty Council Award for Academic Excellence
Mount Sinai Professor in Structural Biology (Endowed Chair)
The Doctor Harold and Golden Lamport Award for Excellence in Basic Science Research
Irma T. Hirschl Career Scientist Award
Basil O'Connor Starter Scholar Research Award
The North Atlantic Treaty Organization (NATO) Research Fellowship
EMBO Long-term Fellowship (Declined)
Science and Engineering Research Council (SERC) of Great Britain Studentship
Protein-nucleic acid interactions
We use a variety of structural tools to uncover how enzymes, and transcription and translation regulators interact with nucleic acids to affect cellular development and disease outcome. We study how such proteins locate, bind, and move on their DNA or RNA sites, and, then use that knowledge to create enzymes with new specificities and obtain a molecular understanding for how genes are regulated. We are also interested in learning how cells cope with the effects of DNA damage. In particular, we investigate how a set of specialized DNA polymerases can bypass DNA damage during replication and how mutations in them can lead to cancer.
Gupta YK, Chan SH, Xu SY, Aggarwal AK. Structural basis of asymmetric DNA methylation and ATP-triggered long-range diffusion by EcoP15I. Nature communications 2015; 6.
Gómez-Llorente Y, Malik R, Jain R, Choudhury JR, Johnson RE, Prakash L, Prakash S, Ubarretxena-Belandia I, Aggarwal AK. The architecture of yeast DNA polymerase ζ. Cell reports 2013; 5: 79-86.
Ummat A, Rechkoblit O, Jain R, Roy Choudhury J, Johnson RE, Silverstein TD, Buku A, Lone S, Prakash L, Prakash S, Aggarwal AK. Structural basis for cisplatin DNA damage tolerance by human polymerase η during cancer chemotherapy. Nature Struct. & Mol. Biol. 2012; 19: 628-632.
Silverstein TD, Johnson RE, Jain R, Prakash L, Prakash S, Aggarwal AK. Structural basis for the suppression of skin cancers by DNA polymerase eta. Nature 2010; 465: 1039-1043.
Swan MK, Johnson RE, Prakash L, Prakash S, Aggarwal AK. Structural basis of high-fidelity DNA synthesis by yeast DNA polymerase delta. Nature Struct. & Mol. Biol. 2009; 16: 979-986.
Escalante CR, Nistal-Villan E, Shen L, Garcia-Sastre A, Aggarwal AK. Structure of IRF-3 bound to the PRDIII-I regulatory element of the human interferon-beta enhancer. Mol. Cell 2007; 26: 703-716.
Lone S, Townson SA, Uljon SN, Johnson RE, Brahma A, Nair DT, Prakash S, Prakash L, Aggarwal AK. Human DNA polymerase-K encircles DNA: Implications for mismatch extension and lesion bypass. Mol. Cell 2007; 25: 601-614.
Nair DT, Johnson RE, Prakash S, Prakash L, Aggarwal AK. Rev1 employs a novel mechanism of DNA synthesis using a protein template. Science 2005; 309: 2219-2222.
Nair DT, Johnson RE, Prakash S, Prakash L, Aggarwal AK. Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing. Nature 2004; 430: 377-380.
Kumar V, Carlson JE, Ohgi KA, Edwards TA, Rose DW, Escalante CR, Rosenfeld MG, Aggarwal AK. Transcription corepressor CtBP is an NAD(+)-regulated dehydrogenase. Mol. Cell 2002; 10: 1127-1131.
Escalante CR, Brass AL, Pongubala JM, Shatova E, Shen L, Singh H, Aggarwal AK. Crystal structure of PU.1/IRF-4/DNA ternary complex. Mol. Cell 2002; 10: 1097-1105.
Edwards TA, Pyle S, Wharton RP, Aggarwal AK. Structure of Pumilio reveals similarity in RNA and peptide binding motifs. Cell 2001; 105: 281-289.
Trincao J, Johnson RE, Escalante CR, Prakash S, Prakash L, Aggarwal AK. Structure of the catalytic core of S. cerevisiae DNA polymerase n: implication for translesion DNA synthesis. Mol. Cell 2001; 8: 439-488.
Scully K, Jacobson EM, Jepsen K, Lunyak V, Viadiu H, Carriere C, Rose DW, Hooshmand F, Aggarwal AK, Rosenfeld MG. Allosteric effects of Pit-1 DNA sites on long-term repression in cell-type specification. Science 2000; 290: 1127-1132.
Viadiu H, Aggarwal AK. Structure of BamHI bound to non-specific DNA: A model for DNA sliding. Mol. Cell 2000; 5: 889-895.
Dhalluin C, Carlson JE, Zeng L, He C, Aggarwal AK, Zhou MM. Structure and ligand of a histone acetyltransferase bromodomain. Nature 1999; 399: 491-496.
Passner JM, Ryoo HD, Shen L, Mann RS, Aggarwal AK. Structure of a DNA-bound Ultrabithorax-Extradenticle homeodomain complex. Nature 1999; 397: 714-719.
Escalante CR, Yie J, Thanos D, Aggarwal AK. Structure of IRF-1 with bound DNA reveals determinants of interferon regulation. Nature 1998; 391: 103-106.
Wah DA, Hirsch JA, Dorner LF, Schildkraut I, Aggarwal AK. Structure of the multimodular endonuclease FokI bound to DNA. Nature 1997; 388: 97-100.
Newman M, Strzelecka T, Dorner LF, Schildkraut I, Aggarwal AK. Structure of BamHI endonuclease bound to DNA: Partial folding and unfolding on DNA binding. Science 1995; 269: 656-663.
Newman M, Strzelecka T, Dorner LF, Schildkraut I, Aggarwal AK. Structure of restriction endonuclease BamHI and its relationship to EcoRI. Nature 1994; 368: 660-664.
Pabo CO, Aggarwal AK, Jordan SR, Beamer LJ, Obeysekare UR, Harrison SC. Conserved residues make similar contacts in two repressor-operator complexes. Science (New York, N.Y.) 1990; 247: 1210-1213.
Aggarwal AK, Rodgers DW, Drottar M, Ptashne M, Harrison SC. Recognition of a DNA operator by the repressor of phage 434: a view at high resolution. Science (New York, N.Y.) 1988; 242: 899-907.