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S. N. Prasanna Murthy

Researcher at Northwestern University

Publications -  22
Citations -  1254

S. N. Prasanna Murthy is an academic researcher from Northwestern University. The author has contributed to research in topics: GTP' & Tissue transglutaminase. The author has an hindex of 17, co-authored 22 publications receiving 1173 citations.

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Vimentin organization modulates the formation of lamellipodia

TL;DR: The disassembly and withdrawal of vimentin intermediate filaments from the plasma membrane induces membrane ruffling and the formation of a lamellipodium and this formation is inhibited when VIF are present.
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Giant axonal neuropathy-associated gigaxonin mutations impair intermediate filament protein degradation.

TL;DR: It is demonstrated that gigaxonin was responsible for the degradation of vimentin IFs and proteasome inhibition by MG-132 reversed the clearance of IF proteins in cells overexpressing gigax onin, demonstrating the involvement of the proteasomal degradation pathway.
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Autonomic Remodeling in the Left Atrium and Pulmonary Veins in Heart Failure - Creation of a Dynamic Substrate for Atrial Fibrillation

TL;DR: In this paper, the role of autonomic remodeling in contributing to atrial fibrillation (AF) substrate in congestive heart failure (CHF) was examined in 38 rapid-ventricular paced dogs and 39 controls under the following conditions: vagal stimulation, isoproterenol infusion, β-adrenergic blockade, acetylcholinesterase (AChE) inhibition (physostigmine), parasympathetic blockade, and double autonomic blockade.
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Capturing the stem cell paracrine effect using heparin-presenting nanofibres to treat cardiovascular diseases.

TL;DR: The potency of the paracrine effect associated with stem cell therapies and the potential of a biomaterial to bind and deliver these factors are demonstrated, pointing to a potential therapy based on synthetic materials and recombinant factors as an acellular therapy.
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The Fibronectin-binding Domain of Transglutaminase (∗)

TL;DR: The fibronectin-combining site of the liver transglutaminase was investigated by testing fragments obtained from the parent protein by controlled digestion with endoproteinase Lys-C and residues 1-7 in the liver enzyme seem to be of particular importance for influencing its ability to bind to fibronECTin.