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Wei Ji

Researcher at Renmin University of China

Publications -  666
Citations -  26973

Wei Ji is an academic researcher from Renmin University of China. The author has contributed to research in topics: Medicine & Monolayer. The author has an hindex of 64, co-authored 550 publications receiving 20154 citations. Previous affiliations of Wei Ji include East China University of Science and Technology & Huazhong Agricultural University.

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Reversible, erasable, and rewritable nanorecording on an H2 rotaxane thin film.

TL;DR: The phonon dispersions of LiD, LiH and NaH for B1 and B2 phases are computed using density-functional perturbation theory with both local density and generalized gradient approximations and it is found that the B2 phase is unstable at low pressure for all the systems considered.
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A family of high-temperature ferromagnetic monolayers with locked spin-dichroism-mobility anisotropy: MnNX and CrCX (X = Cl, Br, I; C = S, Se, Te)

TL;DR: In this article, the authors theoretically predicted a family of high Tc ferromagnetic monolayers, namely MnNX and CrCX (X = Cl, Br and I; C = S, Se and Te).
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Current use and development of fish vaccines in China

TL;DR: Seven aquatic vaccines are summarized, including the live vaccine against grass carp hemorrhagic disease, the inactivated vaccine against Aeromonas hydrophila sepsis in fish, the live vaccines against Edwardsiella tarda in turbot, and the anti-idiotypic antibody vaccine against Vibrio alginolyticus, V. parahaemolyticUS, and E. tardA in Japanese flounder are summarized.
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Stable, reproducible nanorecording on rotaxane thin films.

TL;DR: Taking advantage of the switching property, reproducible nanometer-scale recording dots are achieved on rotaxane LB films via voltage application using a scanning tunneling microscope probe.
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Self-Assembly of Aromatic Amino Acid Enantiomers into Supramolecular Materials of High Rigidity.

TL;DR: This study investigated the self-assembly mechanism of amyloid-like structure formation by two aromatic amino acids, phenylalanine and tryptophan, both previously found as extremely important for the nucleation and self- assembly of aggregation-prone peptide regions into functional structures.