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Georgi Z. Genchev

Researcher at Shanghai Jiao Tong University

Publications -  26
Citations -  349

Georgi Z. Genchev is an academic researcher from Shanghai Jiao Tong University. The author has contributed to research in topics: Protein folding & Gene. The author has an hindex of 8, co-authored 23 publications receiving 261 citations. Previous affiliations of Georgi Z. Genchev include University of Illinois at Chicago & Boston Children's Hospital.

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Mechanically untying a protein slipknot: multiple pathways revealed by force spectroscopy and steered molecular dynamics simulations.

TL;DR: The results demonstrate the bifurcation of the mechanical unfolding pathway of AFV3-109 and point to the generality of a kinetic partitioning mechanism for protein folding/unfolding.
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A Single-Molecule Perspective on the Role of Solvent Hydrogen Bonds in Protein Folding and Chemical Reactions

TL;DR: These experiments provide new information on the nature of the underlying interactions in protein folding and chemical reactions and demonstrate the power of single-molecule techniques to identify the changes induced by a small change in hydrogen bond strength.
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Stabilization Provided by Neighboring Strands Is Critical for the Mechanical Stability of Proteins

TL;DR: It is shown that Top7 and barstar, which have similar topology in their force-bearing region, exhibit vastly different mechanical-stability characteristics, and this previously overlooked stabilization effect from neighboring beta-strands is likely to be a general mechanism in protein mechanics.
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Multi-omics facilitated variable selection in Cox-regression model for cancer prognosis prediction.

TL;DR: Two methods to incorporate the association among different types of omics data fit the Cox proportional hazards model and predict a risk score based on mRNA expression profiles and achieve better performance in predicting patients' survival in glioblastoma and lung adenocarcinoma.
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Mechanical Signaling on the Single Protein Level Studied Using Steered Molecular Dynamics

TL;DR: The role of steered molecular dynamics simulations in providing details at the atomic level on a group of protein domains, which play a fundamental role in signal exchange by responding properly to mechanical strain, is focused on.