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Jason J. Chruma

Researcher at Sichuan University

Publications -  43
Citations -  2384

Jason J. Chruma is an academic researcher from Sichuan University. The author has contributed to research in topics: Chirality (chemistry) & Catalysis. The author has an hindex of 21, co-authored 43 publications receiving 1891 citations. Previous affiliations of Jason J. Chruma include University of Virginia & Columbia University.

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Near-infrared phosphorescence: materials and applications

TL;DR: This review describes the overall progress made in the past ten years on NIR phosphorescent transition-metal complexes including Cu(I), Cu(II), Cr(III), Re(I, Re-I), Re-III, Ru(II) and Au(I) complexes, with a primary focus on material design complemented with a selection of optical, electronic, sensory, and biologic applications.
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Small-molecule inhibitors of HIV-1 entry block receptor-induced conformational changes in the viral envelope glycoproteins

TL;DR: A receptor-induced conformational rearrangement of gp120-gp41 is defined that is important for both CD4-dependent andCD4-independent HIV-1 entry and is susceptible to inhibition by low-molecular-weight compounds.
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Enhanced Triplet–Triplet Energy Transfer and Upconversion Fluorescence through Host–Guest Complexation

TL;DR: Through host-guest complexation, the efficiencies of both triplet-triplet energy transfer and TTA were significantly enhanced, which overcompensated for the loss of the fluorescence quantum yield of the emitters (hosts).
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Temperature-Driven Planar Chirality Switching of a Pillar[5]arene-Based Molecular Universal Joint

TL;DR: The study of an enantiopure bicyclic pillar-based molecular universal joint by single-crystal X-ray diffraction allowed for the first time the unequivocal assignment of the absolute configuration of a planar chiral pillar[5]arene by circular dichroism spectroscopy.
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Localized Changes in the gp120 Envelope Glycoprotein Confer Resistance to Human Immunodeficiency Virus Entry Inhibitors BMS-806 and #155

TL;DR: Structural considerations suggest a model in which BMS-806 and #155 bind gp120 prior to receptor binding and, upon CD4 binding, are accommodated in the Phe-43 cavity and adjacent channel, which explains the mode of action of these drugs.