77 research outputs found
Entanglement-enhanced probing of a delicate material system
Quantum metrology uses entanglement and other quantum effects to improve the
sensitivity of demanding measurements. Probing of delicate systems demands high
sensitivity from limited probe energy and has motivated the field's key
benchmark-the standard quantum limit. Here we report the first
entanglement-enhanced measurement of a delicate material system. We
non-destructively probe an atomic spin ensemble by means of near-resonant
Faraday rotation, a measurement that is limited by probe-induced scattering in
quantum-memory and spin-squeezing applications. We use narrowband,
atom-resonant NOON states to beat the standard quantum limit of sensitivity by
more than five standard deviations, both on a per-photon and per-damage basis.
This demonstrates quantum enhancement with fully realistic loss and noise,
including variable-loss effects. The experiment opens the way to ultra-gentle
probing of single atoms, single molecules, quantum gases and living cells.Comment: 7 pages, 8 figures; Nature Photonics, advance online publication, 16
December 201
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Targeting Extracellular Domains D4 and D7 of Vascular Endothelial Growth Factor Receptor 2 Reveals Allosteric Receptor Regulatory Sites
Vascular endothelial growth factors (VEGFs) activate three receptor tyrosine kinases, VEGFR-1, -2, and -3, which regulate angiogenic and lymphangiogenic signaling. VEGFR-2 is the most prominent receptor in angiogenic signaling by VEGF ligands. The extracellular part of VEGF receptors consists of seven immunoglobulin homology domains (Ig domains). Earlier studies showed that domains 2 and 3 (D23) mediate ligand binding, while structural analysis of dimeric ligand/receptor complexes by electron microscopy and small-angle solution scattering revealed additional homotypic contacts in membrane-proximal Ig domains D4 and D7. Here we show that D4 and D7 are indispensable for receptor signaling. To confirm the essential role of these domains in signaling, we isolated VEGFR-2-inhibitory “designed ankyrin repeat proteins” (DARPins) that interact with D23, D4, or D7. DARPins that interact with D23 inhibited ligand binding, receptor dimerization, and receptor kinase activation, while DARPins specific for D4 or D7 did not prevent ligand binding or receptor dimerization but effectively blocked receptor signaling and functional output. These data show that D4 and D7 allosterically regulate VEGFR-2 activity. We propose that these extracellular-domain-specific DARPins represent a novel generation of receptor-inhibitory drugs for in vivo applications such as targeting of VEGFRs in medical diagnostics and for treating vascular pathologies
Clinical overview and treatment options for non-skeletal manifestations of mucopolysaccharidosis type IVA
Phenotypic effects of concomitant insensitive acetylcholinesterase (ace-1 R ) and knockdown resistance (kdr R ) in Anopheles gambiae: a hindrance for insecticide resistance management for malaria vector control
Onset of analgesia with sodium ibuprofen, ibuprofen acid incorporating poloxamer and acetaminophen—a single-dose, double-blind, placebo-controlled study in patients with post-operative dental pain
Craniofacial vertical bone augmentation: A comparison between 3D printed monolithic monetite blocks and autologous onlay grafts in the rabbit
Seleção de traçadores para estudos de eficiência das aplicações de produtos fitossanitários
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