Picture of Haribabu Arthanari

Haribabu Arthanari, Ph.D.

Associate Professor of Biological Chemistry and Molecular Pharmacology

We utilize a combination of techniques including NMR spectroscopy, NMR-based fragment and high throughput screening, and biophysical and cell-based assays to map hotspots in the interaction interface, to further understand the molecular mechanisms orchestrated by these interactions, and to identify disruptive inhibitors that may be developed into treatments for the related pathologies.

Haribabu Arthanari received his Bachelors in Chemistry from the Madras Christian College and his Masters in Chemistry from the Indian Institute of Technology (IIT)-Madras.  He did his graduate studies at Wesleyan University with Philip  Bolton and earned his PhD in 2004. He then joined the laboratory of Gerhard Wagner for his post-doctoral training. He was promoted to a lecturer in 2010 and moved to his independent position in 2016.

Research:

Protein-Protein Interactions (PPIs) is the Holy Grail of therapeutic intervention, offering a plethora of unique structural landscapes as potential targets. I use structure-guided approaches to characterize and validate these interactions in the context of disease models.  We utilize a combination of techniques including NMR spectroscopy, NMR-based fragment and high throughput screening, and biophysical and cell-based assays to map hotspots in the interaction interface, to further understand the molecular mechanisms orchestrated by these interactions, and to identify disruptive inhibitors that may be developed into treatments for the related pathologies.  Our current areas of focus are 1) the critical interactions between transcription factors and the general transcriptional machinery, including the Mediator complex, co-activators, and remodeling factors, and 2) translation initiation machinery demonstrated to be dysregulated in cancer disease states.  We are working on making use of NMR-derived metabolomics data in the identification of novel metabolite disease markers that in combination with cellular pathway analysis can be used to identify new potential therapeutic targets.  In order to facilitate our research goals, we also work on the development of new NMR methods for fragment screening, metabolite fingerprinting and protein-ligand interaction identification.  Our work on novel pulse sequences, pulse designs, labeling strategies and sampling schemes let us push the boundaries of NMR as a technique, allowing us to tackle larger systems by NMR.

Address: 

Longwood Center

LC-3311

360 Longwood Ave.

Boston, MA 02115

Publications View
Molecular Landscape of the Ribosome Pre-initiation Complex during mRNA Scanning: Structural Role for eIF3c and Its Control by eIF5.
Authors: Authors: Obayashi E, Luna RE, Nagata T, Martin-Marcos P, Hiraishi H, Singh CR, Erzberger JP, Zhang F, Arthanari H, Morris J, Pellarin R, Moore C, Harmon I, Papadopoulos E, Yoshida H, Nasr ML, Unzai S, Thompson B, Aube E, Hustak S, Stengel F, Dagraca E, Ananbandam A, Gao P, Urano T, Hinnebusch AG, Wagner G, Asano K.
Cell Rep
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Perspective: revisiting the field dependence of TROSY sensitivity.
Authors: Authors: Takeuchi K, Arthanari H, Wagner G.
J Biomol NMR
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Identification of DNA primase inhibitors via a combined fragment-based and virtual screening.
Authors: Authors: Ilic S, Akabayov SR, Arthanari H, Wagner G, Richardson CC, Akabayov B.
Sci Rep
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Analytical optimization of active bandwidth and quality factor for TOCSY experiments in NMR spectroscopy.
Authors: Authors: Coote P, Bermel W, Wagner G, Arthanari H.
J Biomol NMR
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Backbone resonance assignment of N15, N30 and D10 T cell receptor ß subunits.
Authors: Authors: Mallis RJ, Reinherz EL, Wagner G, Arthanari H.
Biomol NMR Assign
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Inhibiting fungal multidrug resistance by disrupting an activator-Mediator interaction.
Authors: Authors: Nishikawa JL, Boeszoermenyi A, Vale-Silva LA, Torelli R, Posteraro B, Sohn YJ, Ji F, Gelev V, Sanglard D, Sanguinetti M, Sadreyev RI, Mukherjee G, Bhyravabhotla J, Buhrlage SJ, Gray NS, Wagner G, Näär AM, Arthanari H.
Nature
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Nitrogen-detected TROSY yields comparable sensitivity to proton-detected TROSY for non-deuterated, large proteins under physiological salt conditions.
Authors: Authors: Takeuchi K, Arthanari H, Imai M, Wagner G, Shimada I.
J Biomol NMR
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Solution Structure of the Cuz1 AN1 Zinc Finger Domain: An Exposed LDFLP Motif Defines a Subfamily of AN1 Proteins.
Authors: Authors: Sun ZJ, Bhanu MK, Allan MG, Arthanari H, Wagner G, Hanna J.
PLoS One
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Nitrogen detected TROSY at high field yields high resolution and sensitivity for protein NMR.
Authors: Authors: Takeuchi K, Arthanari H, Shimada I, Wagner G.
J Biomol NMR
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Structure of a CGI-58 motif provides the molecular basis of lipid droplet anchoring.
Authors: Authors: Boeszoermenyi A, Nagy HM, Arthanari H, Pillip CJ, Lindermuth H, Luna RE, Wagner G, Zechner R, Zangger K, Oberer M.
J Biol Chem
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