Jinxia Deng

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We present here a dynamic receptor-based pharmacophore model representing the complementary features of the active site region of HIV-1 integrase (IN), which was developed from a series of representative conformations of IN. Conformations of IN were sampled through a molecular dynamics study of the catalytic domain of an IN monomer, and an ensemble of(More)
BACKGROUND Recently, there has been a surge of interest in developing compounds selectively targeting mitochondria for the treatment of neoplasms. The critical role of mitochondria in cellular metabolism and respiration supports this therapeutic rationale. Dysfunction in the processes of energy production and metabolism contributes to attenuation of(More)
HIV-1 integrase is one of the three essential enzymes required for viral replication and has great potential as a novel target for anti-HIV drugs. Although tremendous efforts have been devoted to understanding this protein, the conformation of the catalytic core domain around the active site, particularly the catalytic loop overhanging the active site, is(More)
  • Qiang Li, He Zhu, Lirong Zheng, Longlong Fan, Yang Ren, Jun Chen +2 others
  • 2016
the corrugated layer structure of rhombohedral A7 connected by so-called metallic-covalent bonds, [17,18] which is stabilized by Jones–Peielrs mechanism. [19] Thermal expansion matching has always been the key issue to decide the effectiveness and cycling life in nanodevices, especially for the nanomaterials working under variable temperature like(More)
Control of negative thermal expansion is a fundamentally interesting topic in the negative thermal expansion materials in order for the future applications. However, it is a challenge to control the negative thermal expansion in individual pure materials over a large scale. Here, we report an effective way to control the coefficient of thermal expansion(More)
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