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H. Eugene Stanley

Researcher at Boston University

Publications -  1208
Citations -  134813

H. Eugene Stanley is an academic researcher from Boston University. The author has contributed to research in topics: Complex network & Phase transition. The author has an hindex of 154, co-authored 1190 publications receiving 122321 citations. Previous affiliations of H. Eugene Stanley include University of North Carolina at Chapel Hill & Wesleyan University.

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Kinetics of Formation of Randomly Branched Aggregates: A Renormalization-Group Approach

TL;DR: In this article, the first renormalization-group approach for irreversible growth models of randomly branched aggregates is presented, and the main result is that the Witten-Sander diffusion-limited aggregation model, a discrete version of a dendritic growth model, is in a different universality class than "equilibrium" lattice animals.
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Nanoscale Dynamics of Phase Flipping in Water near its Hypothesized Liquid-Liquid Critical Point

TL;DR: This work simulates the classic ST2 model of water for times up to 1000 ns and system size and finds that for state points near the LL transition line, the entire system flips rapidly between liquid states of high and low density.
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Predictions of dynamic behavior under pressure for two scenarios to explain water anomalies.

TL;DR: This work relates tau to fluctuations of hydrogen bond network and shows that the crossover found for tau for both scenarios is a consequence of the sharp change in the average number of hydrogen bonds at the temperature of the specific heat maximum.
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Stock market contagion during the global financial crisis: A multiscale approach

TL;DR: In this article, a multiscale correlation contagion statistic was proposed to test for stock market contagion during the global financial crisis (GFC) from the US to the other six G7 and BRIC countries.
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Energy landscape in protein folding and unfolding

TL;DR: These findings confirm the validity of the theoretical scenario of a process dominated by different energetic routes, also explaining the water role in the protein configuration stability and highlighting that the protein native state limit is represented by the water singular temperature that characterizes its compressibility and expansivity.