Srihari Shankar
Principal Scientific Associate
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Biography and Research Information
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Srihari Shankar's research focuses on understanding the molecular mechanisms underlying cellular processes, including replication, cargo trafficking, and protein allostery. His work investigates the molecular biology of cancer and other disease states. Shankar has published on the structural basis for the regulation of Rho inactivation by p50RhoGAP, the enzymatic activity of the HACE1 HECT-type E3 ligase, and a novel allosteric site in human kidney-type glutaminase. His recent publications also explore the regulation of CHIP E3 ligase-mediated ubiquitination and the distinct roles of specific amino acid residues in the BCH domain of yeast p50RhoGAP. Additionally, he has contributed to structural studies of the GINS tetramer from *Saccharolobus solfataricus*.
Metrics
- h-index: 4
- Publications: 8
- Citations: 43
Selected Publications
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Structure of the <i>Saccharolobus solfataricus</i> GINS tetramer (2025)
Collaboration Network
Top Collaborators
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- Structural Basis for the Enzymatic Activity of the HACE1 HECT‐Type E3 Ligase Through N‐Terminal Helix Dimerization
- A novel allosteric site employs a conserved inhibition mechanism in human kidney‐type glutaminase
- Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP
- Insights into the regulation of CHIP E3 ligase-mediated ubiquitination of neuronal protein BNIP-H
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP
- Insights into the regulation of CHIP E3 ligase-mediated ubiquitination of neuronal protein BNIP-H
- Structural Basis for the Enzymatic Activity of the HACE1 HECT‐Type E3 Ligase Through N‐Terminal Helix Dimerization
- A novel allosteric site employs a conserved inhibition mechanism in human kidney‐type glutaminase
- Insights into the regulation of CHIP E3 ligase-mediated ubiquitination of neuronal protein BNIP-H
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- Structural basis for the distinct roles of non-conserved Pro116 and conserved Tyr124 of BCH domain of yeast p50RhoGAP
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- A novel allosteric site employs a conserved inhibition mechanism in human kidney‐type glutaminase
- Structural Basis for the Enzymatic Activity of the HACE1 HECT‐Type E3 Ligase Through N‐Terminal Helix Dimerization
- Insights into the regulation of CHIP E3 ligase-mediated ubiquitination of neuronal protein BNIP-H
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- Structural basis for p50RhoGAP BCH domain–mediated regulation of Rho inactivation
- A novel allosteric site employs a conserved inhibition mechanism in human kidney‐type glutaminase
- A novel allosteric site employs a conserved inhibition mechanism in human kidney‐type glutaminase
- Structural Basis for the Enzymatic Activity of the HACE1 HECT‐Type E3 Ligase Through N‐Terminal Helix Dimerization
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