Author

F. Ashish

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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Biophysics· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Approach:deep learning· 1 Research Focus:host-pathogen & immune response· 1 Organism:plant (other)· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

N. Kalidas· 2 shared N. Peddada· 2 shared A. Mukhopadhyay· 1 shared A. Sagar· 1 shared H. OJHA· 1 shared J. S. TYAGI· 1 shared K. Dhiman· 1 shared K. Pandey· 1 shared

Activity by Year

2019-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 13 mutual co-author links

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2 shared papersBiophysics

N. Kalidas

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

VISUALIZING THE NUCLEATING AND CAPPED STATES OF F-ACTIN BY Ca2+-GELSOLIN: SAXS DATA BASED STRUCTURES OF BINARY AND TERNARY COMPLEXES

A. Sagar, N. Peddada, V. CHOUDHARY, Y. Mir, R. Garg, F. Ashish

This study uses SAXS to reveal structural insights into how Ca2+-gelsolin depolymerizes and caps F-actin, identifying GA and GA2 complexes as key intermediates.

bioRxiv · Mar 9, 2024Biophysics

SAXS DATA BASED GLYCOSYLATED MODELS OF HUMAN ALPHA-1-ACID GLYCORPROTEIN, A KEY PLAYER IN HEALTH, DISEASE AND DRUG CIRCULATION

N. Kalidas, N. Peddada, K. Pandey, F. Ashish

The paper uses SAXS data and computational modeling to create glycosylated models of human alpha-1-acid glycoprotein, showing better agreement with experimental data than unglycosylated models.

bioRxiv · Feb 1, 2024Biophysics

Plasmodium falciparum Kelch13 and its artemisinin-resistant mutants assemble as hexamers in solution: a SAXS data driven shape restoration study.

N. Goel, K. Dhiman, N. Kalidas, A. Mukhopadhyay, F. Ashish, S. Bhattacharjee

This study uses SAXS data to show that PfKelch13 forms a stable hexamer with specific domain arrangements, and that resistant mutants have altered spatial configurations.

bioRxiv · Feb 7, 2021 · PreprintBiochemistry

A novel function of M. tuberculosis chaperonin paralog GroEL1 in copper homeostasis

M. Y. ANSARI, S. D. BATRA, H. OJHA, F. ASHISH, J. S. TYAGI, S. C. MANDE

This study identifies GroEL1 in Mycobacterium tuberculosis as a copper-binding chaperone that protects against copper toxicity by maintaining redox balance and preventing DNA damage.

bioRxiv · Sep 14, 2019 · PreprintBiophysics