Pengyun Li

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FKBP52 is a member of the FK506-binding protein family (FKBPs). The N-terminal domain of FKBP52 (FKBP52-N; residues 1-140) is responsible for peptidyl-prolyl isomerase activity and binding of FK506. Here, the crystal structure of FKBP52-N has been determined by molecular replacement to 2.4 A. FKBP52-N is defined by a six-stranded antiparallel beta-sheet(More)
  • Miguel Angel Sánchez-Garrido, Kirk M. Habegger, Christoffer Clemmensen, Cassie Holleman, Timo D. Müller, Diego Perez-Tilve +7 others
  • 2016
OBJECTIVE Fibroblast activation protein (FAP) is a serine protease belonging to a S9B prolyl oligopeptidase subfamily. This enzyme has been implicated in cancer development and recently reported to regulate degradation of FGF21, a potent metabolic hormone. Using a known FAP inhibitor, talabostat (TB), we explored the impact of FAP inhibition on metabolic(More)
Vascular hyporeactivity is one of the major causes responsible for refractory hypotension and associated mortality in severe hemorrhagic shock. Mitochondrial permeability transition (mPT) pore opening in arteriolar smooth muscle cells (ASMCs) is involved in the pathogenesis of vascular hyporeactivity. However, the molecular mechanism underlying(More)
We report the first experimental realization of classical hypercorrelation, correlated simultaneously in every degree of freedom (DOF), from observing a Bell-type inequality violation in each DOF: polarization and orbital angular momentum (OAM). Based on such a classical hypercorrelation, we have realized the analogy of quantum superdense coding in(More)
The mol-ecule of the title compound, C(22)H(27)NO(9), an azasugar derivative, consists of one benzene ring and two fused rings, which have the cis arrangement at the ring junctions, and gives a V-shaped geometry. The inter-planar angle between the five- and six-membered rings is 65.69 (11)°. The crystal structure is stablized by weak inter-molecular C-H⋯O(More)
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