Author

A. Kulshrestha

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

Biology Disciplines

Click to filter author papers

Biophysics· 3 Physiology· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Research Focus:protein folding & dynamics· 3 Organism:human· 2 Approach:statistical model· 2 Assay:structural biology· 2 Research Focus:cell signaling & trafficking· 1 Approach:deep learning· 1 Research Focus:differential expression· 1 Organism:E. coli· 1

Frequent Co-Authors

K. G. Ayappa· 3 shared R. Roy· 2 shared S. N. Punnathanam· 2 shared A. Bazaz· 1 shared H. N. Davenport· 1 shared H. Q. Ta· 1 shared M. Kuppusamy· 1 shared P. W. Carrott· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersBiophysics

K. G. Ayappa

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Purinergic P2Y2 Receptor-Induced Activation of Endothelial TRPV4 Channels Mediates Lung Ischemia-Reperfusion Injury

M. Kuppusamy, H. Q. Ta, H. N. Davenport, A. Bazaz, A. Kulshrestha, Z. Daneva, Y.-L. Chen, P. W. Carrott, V. E. Laubach, S. K. Sonkusare

This study identifies the purinergic P2Y2 receptor as a mediator of lung ischemia-reperfusion injury by activating endothelial TRPV4 channels through extracellular ATP release via Panx1.

bioRxiv · May 29, 2023Physiology

Cholesterol catalyzes unfolding in membrane inserted motifs of the pore forming protein cytolysin A

A. Kulshrestha, S. N. Punnathanam, R. Roy, K. G. Ayappa

This study shows cholesterol stabilizes an unfolded intermediate in the pore-forming toxin ClyA, lowering free energy barriers and enhancing pore formation kinetics.

bioRxiv · May 7, 2023Biophysics

Computing the mechanism of α-helix to β-sheet transition in proteins using the finitetemperature string method

A. Kulshrestha, S. N. Punnathanam, K. G. Ayappa

This paper uses the finite temperature string method with path collective variables to study the α-helix to β-sheet transition in a mini G-protein, revealing the intermediate steps and energy landscape of the structural change.

bioRxiv · Jul 21, 2022 · PreprintBiophysics

Conformational flexibility is a key determinant of the lytic activity of the pore forming protein, Cytolysin A

A. Kulshrestha, S. Maurya, T. Gupta, R. Roy, S. Punnathanam, K. G. Ayappa

This study shows that conformational flexibility in the β-tongue and N-terminus regions of ClyA is essential for its lytic activity and membrane-mediated conformational transition.

bioRxiv · Oct 23, 2021 · PreprintBiophysics