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Prateeka Borar
Observed name:
Borar, Prateeka
Institutions:
Bose Institute,
European Molecular Biology Laboratory,
European Molecular Biology Laboratory
Observed institutions:
Bose Institute,
European Molecular Biology Laboratory,
European Molecular Biology Laboratory
ORCID:
0009-0001-3583-2179
Observed ORCID:
0009-0001-3583-2179
OpenAlex ID:
A5044700196
Identification of Biomarker Hyaluronan on Colon Cancer Extracellular Vesicles Using Correlative AFM and Spectroscopy
2020
·
Debashish Paul
, Anuradha Roy
, et al.
·
The Journal of Physical Chemistry Letters
·
45
Designing active RNF4 monomers by introducing a tryptophan: avidity towards E2∼Ub conjugates dictates the activity of ubiquitin RING E3 ligases
2019
·
Sayani Sarkar
, Adaitya Prasad Behera
, et al.
·
Biochemical Journal
·
10
Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2025
·
Prateeka Borar
, Tapan Biswas
, et al.
·
eLife
·
4
Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2025
·
Prateeka Borar
, Tapan Biswas
, et al.
·
eLife
·
1
Isolation and characterization of Aeromonas aquariorum from a dye effluent and its effect in bioaugmentation
2015
·
Iosr Journals
, Prateeka Borar
, et al.
·
Figshare
·
1
IKK2/beta mediated phosphorylation of transcription factor Ets2 at site(s) distal to DNA binding domain negatively modulates its DNA binding activity
2026
·
Polley, Smarajit
, SUTRADHAR, DEEPARNA
, et al.
·
Zenodo (CERN European Organization for Nuclear Research)
IKK2/β mediated phosphorylation of transcription factor Ets2 at site(s) distal to DNA binding domain negatively modulates its DNA binding activity
2026
·
Deeparna Sutradhar
, Anna Rose Antony
, et al.
·
bioRxiv (Cold Spring Harbor Laboratory)
PDF
Role of artificial intelligence in advancing cryo electron microscopy
2026
·
Prateeka Borar
, Smarajit Polley
·
Progress in molecular biology and translational science
Author response: Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2025
·
Prateeka Borar
, Tapan Biswas
, et al.
Author response: Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2025
·
Prateeka Borar
, Tapan Biswas
, et al.
Author response: Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2025
·
Prateeka Borar
, Tapan Biswas
, et al.
Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2025
·
Prateeka Borar
, Tapan Biswas
, et al.
·
eLife
Structural Biology of Protein Kinases and Their Regulation
2024
·
Samrat Mitra
, Pranita Ray
, et al.
·
CRC Press eBooks
Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2024
·
Prateeka Borar
, Tapan Biswas
, et al.
·
eLife
PDF
Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2024
·
Prateeka Borar
, Tapan Biswas
, et al.
·
eLife
PDF
Reviewer #2 (Public Review): Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2024
·
Prateeka Borar
, Tapan Biswas
, et al.
Reviewer #3 (Public Review): Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2024
·
Prateeka Borar
, Tapan Biswas
, et al.
Reviewer #1 (Public Review): Dual-specific autophosphorylation of kinase IKK2 enables phosphorylation of substrate IκBα through a phosphoenzyme intermediate
2024
·
Prateeka Borar
, Tapan Biswas
, et al.
Correction: Designing active RNF4 monomers by introducing a tryptophan: avidity towards E2∼Ub conjugates dictates the activity of ubiquitin RING E3 ligases
2019
·
Sayani Sarkar
, Adaitya Prasad Behera
, et al.
·
Biochemical Journal
PDF
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Works count:
20
Citation count:
61
H-index:
3
I10-index:
2
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