S. Haldar

Next-Gen Profiling of Tumor-resident Stem Cells using Machine learning

This paper introduces OSCORP, a machine learning method that identifies cancer stem cells with 99% accuracy using bulk RNAseq data, revealing CSC states and their clinical and transcriptomic signatures across 22 cancer types.

Methotrexate-modulated talin-dynamics drives cellular mechanical phenotypes via YAP signalling

This study shows methotrexate modulates talin dynamics, affecting YAP signaling and cancer cell mechanical properties through focal adhesion changes.

Force-regulated chaperone activity of BiP/ERdj3 is opposite to their homologs DnaK/DnaJ: explained by strain energy

This study compares the force-regulated chaperone activity of tunnel-associated BiP/ERdj3 and their cytoplasmic homologs DnaK/DnaJ, revealing that BiP/ERdj3 act as foldases under force while DnaK/DnaJ act as holdases.

Pan-cancer Analysis Predicts Kindlin-associated Global Mechanochemical Perturbation

This study analyzes pan-cancer data to show kindlin alterations are associated with poor survival, advanced tumor stages, and synergistic effects with cancer hallmark genes.

Trimethylamine N-oxide (TMAO) enhances substrate mechanical stability probed by single molecule magnetic tweezers

This study investigates how TMAO affects the mechanical stability of proteins using single-molecule magnetic tweezers, finding it increases unfolding force and alters folding kinetics.

Talin-drug interaction reveals a key molecular determinant for biphasic mechanical effect: studied under single-molecule resolution

This study investigates talin-drug interactions using single-molecule techniques, revealing biphasic mechanical effects and mechanistic insights into drug-induced stability changes.

Ligand-induced unfolding mechanism of an RNA G-quadruplex

This study investigates the mechanism by which TMPyP4 induces unfolding of RNA G-quadruplexes using simulations and experiments, revealing a two-state interaction mechanism.

Planar aggregation of the influenza viral fusion peptide alters membrane structure and hydration, promoting poration.

This study shows that influenza viral fusion peptides aggregate on membranes, altering structure and hydration to promote poration.

DsbA is a redox-switchable mechanical chaperone

This study shows DsbA acts as a redox-switchable mechanical chaperone, reducing ATP consumption for periplasmic translocation by up to 33%.

Real time observation of chaperone-modulated talin mechanics under single molecule resolution

This study investigates how chaperones modulate talin mechanics under single-molecule resolution, showing they alter unfolding forces and energy landscapes.

Direct observation of the mechanical role of bacterial chaperones in protein folding

The paper uses magnetic-tweezers to study how chaperones respond to mechanical force, revealing their roles in generating or consuming energy during protein folding.

Connecting conformational stiffness of the protein with energy landscape by a single experiment

This paper introduces a method to simultaneously measure multiple physical properties of a single protein molecule in real-time, revealing how salt concentration affects its conformational flexibility and energy landscape.

Precise triggering and chemical control of single-virus fusion within endosomes

This paper develops a method to precisely control single-virus fusion within endosomes using chemical triggers, enabling study of fusion dynamics under physiological conditions.

Ultra-fast electroporation of giant unilamellar vesicles -- Experimental validation of a molecular model

The paper experimentally validates a molecular model of electroporation by comparing vesicle permeabilization kinetics with molecular simulations.

Protein folding modulates the adhesion strategy of Gram positive pathogens

This study shows how protein folding modulates the adhesion strategy of Gram positive pathogens by switching between reversible and irreversible bonding under different mechanical forces.

The Mechanical Power of Protein Folding

This study shows disulfide bonds in titin Ig domains amplify mechanical power during muscle contraction by enabling high-force folding, boosting power output from 0 to 6,000 zeptowatts at 6.0 pN.