Research Areas
Biomedical Subjects
Links
Biography and Research Information
OverviewAI-generated summary
Sibes Bera's research investigates molecular mechanisms underlying viral integration and protein structure-function relationships. His work has focused on the structural basis of host protein hijacking in human T-cell leukemia virus integration and the molecular interactions within the human immunodeficiency virus type 1 (HIV-1) concerted integration complex. Bera has also studied the role of specific amino acid mutations in protein structure and function, particularly concerning alpha-crystallin, a protein involved in maintaining lens clarity and acting as a molecular chaperone. This includes examining how mutations like R116C affect oligomerization, structure, and chaperone activity. His publications also include work on DNA repair proteins, such as RecO from Deinococcus radiodurans. Bera's research has generated 37 publications with 737 citations and an h-index of 15.
Metrics
- h-index: 15
- Publications: 37
- Citations: 737
Positions
-
Scientist 2024–presentUniversity of Arkansas for Medical Sciences Biochemistry and Molecular Biology ORCID
Selected Publications
-
Delineation of a novel assembly intermediate in retroviral integration pathway (2025)
-
A Positive Charge Preservation at Position 116 of αA-Crystallin Is Critical for Its Structural and Functional Integrity (2002)
-
Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of αB-crystallin (2001)
-
The αA-Crystallin R116C Mutant Has a Higher Affinity for Forming Heteroaggregates with αB-Crystallin (2001)
Collaboration Network
Top Collaborators
- A Positive Charge Preservation at Position 116 of αA-Crystallin Is Critical for Its Structural and Functional Integrity
- The αA-Crystallin R116C Mutant Has a Higher Affinity for Forming Heteroaggregates with αB-Crystallin
- Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of αB-crystallin
- A Positive Charge Preservation at Position 116 of αA-Crystallin Is Critical for Its Structural and Functional Integrity
- A Positive Charge Preservation at Position 116 of αA-Crystallin Is Critical for Its Structural and Functional Integrity
- Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of αB-crystallin
- Substituted hydrophobic and hydrophilic residues at methionine-68 influence the chaperone-like function of αB-crystallin
- Delineation of a novel assembly intermediate in retroviral integration pathway
- Delineation of a novel assembly intermediate in retroviral integration pathway
- Delineation of a novel assembly intermediate in retroviral integration pathway
- Delineation of a novel assembly intermediate in retroviral integration pathway
- Delineation of a novel assembly intermediate in retroviral integration pathway
Similar Researchers
Based on overlapping research topics