Innovative Research Award
Aritra Bej
University of California, Davis, United States
Aritra Bej is a researcher affiliated with the University of California, Davis, whose published work spans structural biology, biophysical chemistry, nuclear magnetic resonance spectroscopy, calcium-dependent signaling, and ion-channel regulation. His research includes investigations of calmodulin interactions with retinal cyclic nucleotide-gated channels and NMDA receptors, as well as structural studies of voltage-gated calcium-channel regulatory mechanisms.[1][2] His publication record also includes earlier research in protein dynamics and structural biology, providing a broad scientific foundation for evaluating his research contributions.[3]
Abstract
Aritra Bej’s research profile is characterized by experimental and structural investigations of protein–protein interactions and regulatory mechanisms involving calcium-sensitive signaling proteins and ion channels. His work at the University of California, Davis includes studies using nuclear magnetic resonance approaches to characterize calmodulin interactions with retinal cyclic nucleotide-gated channels and receptor-associated domains, alongside broader investigations of ion-channel regulation.[1][2] Recent publications extend this research to NMDA receptor regulation by calmodulin and structural mechanisms associated with L-type voltage-gated calcium channels.[4][5]
Keywords
Aritra Bej; structural biology; biophysical chemistry; nuclear magnetic resonance; NMR spectroscopy; calmodulin; ion channels; NMDA receptors; calcium signaling; retinal cyclic nucleotide-gated channels; voltage-gated calcium channels; protein dynamics; molecular structure; protein–protein interactions; research innovation.
Introduction
Research in structural and molecular biology frequently requires the integration of biochemical, spectroscopic, and structural approaches to explain how proteins interact and how those interactions influence cellular signaling. Bej’s published work addresses this problem through studies of calmodulin and its regulatory relationships with membrane-associated proteins and ion channels. His research at the University of California, Davis has included NMR-based structural characterization of regulatory domains and molecular recognition processes.[1][2]
The research record also demonstrates continuity across different biological systems. Earlier work investigated protein conformational dynamics and structural interfaces, while subsequent studies examined calmodulin-mediated regulation of retinal cyclic nucleotide-gated channels, NMDA receptors, and voltage-gated calcium channels.[3][6] This progression provides a basis for assessing the researcher in terms of methodological development, subject-matter breadth, and contribution to molecular-level understanding of signaling proteins.
Research Profile
Bej’s documented research activities center on structural characterization of proteins and protein complexes, particularly systems in which calcium-dependent regulation influences ion-channel activity. His work combines NMR spectroscopy with biochemical and structural analyses to investigate molecular interactions and conformational states. For example, his publications have characterized calmodulin bound to specific regulatory regions of retinal cyclic nucleotide-gated channels and NMDA receptor subunits.[1][2][7]
| Research Dimension |
Documented Focus |
| Structural Biology |
Protein structure, conformational dynamics, and molecular interfaces |
| NMR Spectroscopy |
Chemical-shift assignments and structural characterization of protein complexes |
| Calmodulin Biology |
Calmodulin interactions with receptor and ion-channel regulatory regions |
| Ion-Channel Regulation |
Retinal CNG channels, NMDA receptors, and L-type voltage-gated calcium channels |
Research Contributions
A significant component of Bej’s research concerns the molecular basis of calmodulin recognition. His work on retinal cyclic nucleotide-gated channels examined calmodulin-binding regions within the cytosolic domains of CNGB1 and contributed structural information relevant to calcium-dependent channel regulation.[1] Related studies characterized calmodulin interactions with different regulatory regions of NMDA receptor subunits, creating a set of experimentally defined structural observations across related signaling systems.[7][8]
More recent work has addressed functional and structural mechanisms in ion-channel regulation. A 2026 Journal of Biological Chemistry study examined NMDA receptor regulation by calmodulin, while a 2026 Biochemistry publication investigated structural insights into CaBP1-mediated activation of the CaV1.2 L-type voltage-gated calcium channel.[4][5] Together, these studies illustrate a research trajectory connecting molecular structure with mechanisms of channel regulation.
His earlier publication record also includes work on protein dynamics and molecular interfaces, including studies involving the p53 core domain and NOD2-associated CARD interactions.[3][9] These contributions provide additional evidence of experience with structural and biophysical approaches to biologically important protein systems.
Publications
- Bej, A., & Ames, J. B. (2022). Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1). Journal of Biomolecular NMR, 76, 147–151. DOI: 10.1007/s12104-022-10072-9.[1]
- Bej, A., & Ames, J. B. (2022). NMR Structures of Calmodulin Bound to Two Separate Regulatory Sites in the Retinal Cyclic Nucleotide-Gated Channel. Biochemistry, 61(18), 1955–1965. DOI: 10.1021/acs.biochem.2c00378.[2]
- Rasquinha, J. A., Bej, A., Dutta, S., & Mukherjee, S. (2017). Intrinsic Differences in Backbone Dynamics between Wild Type and DNA-Contact Mutants of the p53 DNA Binding Domain Revealed by Nuclear Magnetic Resonance Spectroscopy. Biochemistry, 56(37), 4962–4971. DOI: 10.1021/acs.biochem.7b00514.[3]
- Bej, A., Erickson-Oberg, M. Q., Nigam, A., Yu, I., Hell, J. W., Johnson, J. W., & Ames, J. B. (2026). Structural basis and functional analysis of NMDA receptor regulation by calmodulin. Journal of Biological Chemistry, 302(2), 111131. DOI: 10.1016/j.jbc.2026.111131.[4]
- Salveson, I., Anderson, D. E., Bej, A., Nieves-Cintron, M., Navedo, M., Hell, J. W., & Ames, J. B. (2026). Structural Insights into L-Type Voltage-Gated Ca2+ Channel (CaV1.2) Activation by CaBP1. Biochemistry, 65(10), 1668–1676. DOI: 10.1021/acs.biochem.6c00032.[5]
- Bej, A., & Ames, J. B. (2022). Chemical shift assignments of calmodulin under standard conditions at neutral pH. Journal of Biomolecular NMR, 76, 213–218. DOI: 10.1007/s12104-022-10082-7.[6]
- Bej, A., & Ames, J. B. (2023). Chemical shift assignments of calmodulin bound to the GluN1 C0 domain (residues 841–865) of the NMDA receptor. Journal of Biomolecular NMR, 77, 61–65. DOI: 10.1007/s12104-023-10121-x.[7]
- Bej, A., & Ames, J. B. (2023). Chemical shift assignments of calmodulin bound to a cytosolic domain of GluN2A (residues 1004–1024) from the NMDA receptor. Journal of Biomolecular NMR, 77, 89–93. DOI: 10.1007/s12104-023-10125-7.[8]
- Bej, A., Sahoo, B. R., et al. (2021). Structural Elucidation of Inter-CARD Interfaces involved in NOD2 Tandem CARD Association and RIP2 Recognition. The Journal of Physical Chemistry B, 125(49), 13349–13365. DOI: 10.1021/acs.jpcb.1c06176.[9]
Research Impact
The supplied research metrics report 28 documents, 327 citations, citations by 284 documents, and an h-index of 9. These quantitative indicators provide one measure of the visibility of the research record. They should, however, be interpreted alongside publication quality, methodological contribution, collaboration, scientific relevance, and the substantive influence of individual studies.
The publication record demonstrates sustained engagement with molecular mechanisms of protein regulation. Studies of calmodulin–channel interactions have generated experimentally characterized structural information, while later work has extended these approaches to NMDA receptors and voltage-gated calcium channels.[2][4][5] Such continuity is relevant to evaluating research development and the capacity to apply specialized structural methods across biologically significant systems.
Award Suitability
Based on the supplied bibliometric information and publicly documented publications, Aritra Bej presents a research profile that can be considered relevant to an Innovative Research Award. The principal basis for this assessment is the combination of specialized experimental methodology, a coherent body of structural and biophysical research, and publications addressing mechanisms of protein regulation and ion-channel function.[1][4]
Particular strengths include the use of NMR spectroscopy to resolve molecular interactions, the investigation of multiple channel and receptor systems, and continued publication in peer-reviewed journals. Recent studies involving NMDA receptor regulation and CaV1.2 activation indicate an ongoing focus on structural mechanisms with potential relevance to understanding cellular signaling.[4][5] Final award decisions should additionally incorporate the official award criteria, independently verified bibliometric records, originality assessments, and peer-review evidence.
Conclusion
Aritra Bej’s documented research profile reflects sustained work in structural biology, NMR spectroscopy, calmodulin-mediated regulation, and ion-channel biology. His publications range from studies of protein dynamics and molecular interfaces to detailed investigations of calmodulin interactions with retinal CNG channels and NMDA receptor components, followed by recent work on NMDA receptor regulation and CaV1.2 channel activation.[3][4][5]
With the supplied record of 28 documents, 327 citations, and an h-index of 9, the profile provides measurable evidence of scholarly activity and visibility. Considered together with the documented methodological focus and peer-reviewed publication record, these characteristics provide a reasonable scholarly basis for consideration within an innovative research recognition framework.
External Links
References
- Bej, A., & Ames, J. B. (2022). Chemical shift assignments of calmodulin bound to the β-subunit of a retinal cyclic nucleotide-gated channel (CNGB1). Journal of Biomolecular NMR, 76, 147–151. DOI: https://doi.org/10.1007/s12104-022-10072-9
PubMed Central article
- Bej, A., & Ames, J. B. (2022). NMR Structures of Calmodulin Bound to Two Separate Regulatory Sites in the Retinal Cyclic Nucleotide-Gated Channel. Biochemistry, 61(18), 1955–1965. DOI: https://doi.org/10.1021/acs.biochem.2c00378
ACS Publications article
- Rasquinha, J. A., Bej, A., Dutta, S., & Mukherjee, S. (2017). Intrinsic Differences in Backbone Dynamics between Wild Type and DNA-Contact Mutants of the p53 DNA Binding Domain Revealed by Nuclear Magnetic Resonance Spectroscopy. Biochemistry, 56(37), 4962–4971. DOI: https://doi.org/10.1021/acs.biochem.7b00514
PubMed record
- Bej, A., Erickson-Oberg, M. Q., Nigam, A., Yu, I., Hell, J. W., Johnson, J. W., & Ames, J. B. (2026). Structural basis and functional analysis of NMDA receptor regulation by calmodulin. Journal of Biological Chemistry, 302(2), 111131. DOI: https://doi.org/10.1016/j.jbc.2026.111131
PubMed record
- Salveson, I., Anderson, D. E., Bej, A., Nieves-Cintron, M., Navedo, M., Hell, J. W., & Ames, J. B. (2026). Structural Insights into L-Type Voltage-Gated Ca2+ Channel (CaV1.2) Activation by CaBP1. Biochemistry, 65(10), 1668–1676. DOI: https://doi.org/10.1021/acs.biochem.6c00032
PubMed record