Author

K. Gadhave

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 3 Biophysics· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:protein folding & dynamics· 3 Organism:virus· 3 Assay:protein structure· 2 Approach:statistical model· 2 Research Focus:cell type annotation· 1 Research Focus:clustering· 1 Approach:deep learning· 1

Frequent Co-Authors

R. Giri· 6 shared A. Kumar· 4 shared N. Garg· 4 shared S. K. Kapuganti· 4 shared K. U. Saumya· 3 shared P. Kumar· 3 shared T. Bhardwaj· 3 shared M. Vendruscolo· 2 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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6 shared papersBiophysics

R. Giri

Mutual co-authors in cluster

Author profile →

7 papers

Recent·Most cited

The aggregation potential of Zika virus proteome

R. Giri, T. Bhardwaj, K. U. Saumya, K. Gadhave, S. K. Kapuganti, N. Sharma

This study identifies aggregation-prone regions in the Zika virus proteome using computational tools and experimental validation, showing several viral proteins can form amyloid-like fibrils.

bioRxiv · Mar 26, 2022 · PreprintBiophysics

Bioinspired Dual-Functional Solid Lipid Nanoformulations for Targeted Drug Delivery and Sustained Release for Enhancement of Potency of Albendazole, an Antihelminthic Drug

S. Sharma, V. Goel, P. Kaur, K. Gadhave, N. Garg, L. D. Singla, D. Choudhury

This paper develops bioinspired solid lipid nanoparticles for targeted drug delivery of albendazole, showing enhanced potency and sustained release against gastrointestinal helminths.

bioRxiv · Jul 24, 2021 · PreprintMicrobiology

Amyloidogenic proteins in the SARS-CoV and SARS-CoV-2 proteomes

T. Bhardwaj, K. Gadhave, S. K. Kapuganti, P. Kumar, Z. F. Brotzakis, K. U. Saumya, N. Nayak, A. Kumar, N. Garg, M. Vendruscolo, R. Giri

This study investigates protein aggregation in SARS-CoV and SARS-CoV-2 proteomes, finding that several SARS-CoV-2 proteins form cytotoxic aggregates via a nucleation-dependent mechanism.

bioRxiv · May 29, 2021Biophysics

P53 TAD2 Domain (38-61) Forms Amyloid-like Aggregates in Isolation

K. Gadhave, S. K. Kapuganti, P. M. Mishra, R. Giri

This study investigates the aggregation behavior of the P53 TAD2 domain (38-61) in isolation, showing it forms amyloid-like aggregates under acidic pH conditions.

bioRxiv · Apr 9, 2021Biochemistry

Environmental Dependence of the Structure of the C-terminal Domain of the SARS-CoV-2 Envelope Protein

K. Gadhave, A. Kumar, P. Kumar, S. K. Kapuganti, N. Garg, M. Vendruscolo, R. Giri

This paper investigates how environmental factors affect the conformation of the C-terminal domain of the SARS-CoV-2 envelope protein, showing it transitions between disordered, membrane-bound, and amyloid states.

bioRxiv · Dec 29, 2020 · PreprintBiophysics

Zika Virus Capsid Anchor Forms Cytotoxic Amyloid-like Fibrils

K. U. Saumya, K. Gadhave, A. Kumar, R. Giri

This study investigates the amyloid-forming propensity of the Zika virus Capsid-anchor (CA) peptide and shows it forms cytotoxic amyloid-like fibrils.

bioRxiv · Nov 13, 2020Biochemistry

Conformational Dynamics of NSP11 Peptide of SARS-CoV-2 Under Membrane Mimetics and Different Solvent Conditions

K. Gadhave, P. Kumar, A. Kumar, T. Bhardwaj, N. Garg, R. Giri

This study investigates the conformational dynamics of SARS-CoV-2 nsp11 peptide under different membrane mimetics and solvent conditions, revealing its disordered nature and helical propensity in specific environments.

bioRxiv · Oct 7, 2020Biochemistry