Pages that link to "Q34352256"
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The following pages link to Naturally Occurring Osmolytes Modulate the Nanomechanical Properties of Polycystic Kidney Disease Domains (Q34352256):
Displaying 10 items.
- RETRACTED: Probing osmolyte participation in the unfolding transition state of a protein (Q33912398) (← links)
- Low folding cooperativity of HP35 revealed by single-molecule force spectroscopy and molecular dynamics simulation (Q35895128) (← links)
- Polycystins, focal adhesions and extracellular matrix interactions (Q37852177) (← links)
- Protein–excipient interactions: Mechanisms and biophysical characterization applied to protein formulation development (Q37920191) (← links)
- Polycystins and partners: proposed role in mechanosensitivity. (Q38200953) (← links)
- Dynamics of Protein Folding and Cofactor Binding Monitored by Single-Molecule Force Spectroscopy (Q38699291) (← links)
- Single-molecule chemo-mechanical unfolding reveals multiple transition state barriers in a small single-domain protein (Q39977051) (← links)
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods (Q42050087) (← links)
- Polycystins and mechanotransduction: From physiology to disease (Q43161157) (← links)
- Probing Small Molecule Binding to Unfolded Polyprotein Based on its Elasticity and Refolding (Q47142856) (← links)