Publication2024
An insight into the role of the N-terminal domain of Salmonella CobB in oligomerization and Zn2+ mediated inhibition of the deacetylase activity
The record
- Type
- Publication
- Date
- 1 January 2024
- Level
- National
- Journal
- Frontiers in Molecular Biosciences
- Volume
- 11
- Published
- 1 January 2024
- DOI
- 10.3389/fmolb.2024.1345158
- Scopus ID
- 85188676757
- ISSN
- 2296889X
- Authors
- 8
- Open access
- Yes
- Citations
- 3
- International co-authorship
- No
- Co-author countries
- IN
Classification
Every label below carries the reasoning it was assigned on, the confidence band it was assigned in, and what produced it. The rubric is published.
UN Sustainable Development Goals
9.5 Enhance scientific research, upgrade technological capabilities, and increase researchers and R&D spending
Biochemistry research on CobB deacetylase enzyme oligomerization and zinc-mediated inhibition mechanisms in Salmonella, advancing molecular research.
- High confidence
- The subject matter is a strong and direct inference from the record type, the funding or organising body, or the programme context, even where the title alone is thin. Example: an ICMR-funded project against SDG 3, on the strength of the agency.
- Judged
- Judged against the published classification rubric, under the rubric and prompt versions recorded with the run that produced it.
- Produced by
- claude-haiku-4-5-20251001, under kortex-publication-v1
Viksit Bharat @2047
vb-3.1 Research and development
Research on bacterial enzyme structures and inhibition pathways contributes to molecular biology and biomedical research capacity.
- Produced by
- claude-haiku-4-5-20251001, under kortex-publication-v1
Each label above carries the instrument and the version that produced it. How each classification is reached.
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Provenance
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- Source rows resolved into this record
- 1
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Citing this record
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KIIT Deemed to be University. “An insight into the role of the N-terminal domain of Salmonella CobB in oligomerization and Zn2+ mediated inhibition of the deacetylase activity”. Kortex.