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1.
Plast Reconstr Surg ; 140(5): 1066-1070, 2017 Nov.
Article in English | MEDLINE | ID: mdl-29068946

ABSTRACT

Virtual reality and augmented reality devices have recently been described in the surgical literature. The authors have previously explored various iterations of these devices, and although they show promise, it has become clear that virtual reality and/or augmented reality devices alone do not adequately meet the demands of surgeons. The solution may lie in a hybrid technology known as mixed reality, which merges many virtual reality and augmented realty features. Microsoft's HoloLens, the first commercially available mixed reality device, provides surgeons intraoperative hands-free access to complex data, the real environment, and bidirectional communication. This report describes the use of HoloLens in the operating room to improve decision-making and surgical workflow. The pace of mixed reality-related technological development will undoubtedly be rapid in the coming years, and plastic surgeons are ideally suited to both lead and benefit from this advance.


Subject(s)
Holography/instrumentation , Plastic Surgery Procedures/instrumentation , Surgery, Computer-Assisted/instrumentation , User-Computer Interface , Clinical Decision-Making , Humans , Plastic Surgery Procedures/methods , Surgery, Computer-Assisted/methods , Workflow
2.
Sci Transl Med ; 8(340): 340ra72, 2016 05 25.
Article in English | MEDLINE | ID: mdl-27225182

ABSTRACT

The amyloid-ß peptide (Aß) is a key protein in Alzheimer's disease (AD) pathology. We previously reported in vitro evidence suggesting that Aß is an antimicrobial peptide. We present in vivo data showing that Aß expression protects against fungal and bacterial infections in mouse, nematode, and cell culture models of AD. We show that Aß oligomerization, a behavior traditionally viewed as intrinsically pathological, may be necessary for the antimicrobial activities of the peptide. Collectively, our data are consistent with a model in which soluble Aß oligomers first bind to microbial cell wall carbohydrates via a heparin-binding domain. Developing protofibrils inhibited pathogen adhesion to host cells. Propagating ß-amyloid fibrils mediate agglutination and eventual entrapment of unatttached microbes. Consistent with our model, Salmonella Typhimurium bacterial infection of the brains of transgenic 5XFAD mice resulted in rapid seeding and accelerated ß-amyloid deposition, which closely colocalized with the invading bacteria. Our findings raise the intriguing possibility that ß-amyloid may play a protective role in innate immunity and infectious or sterile inflammatory stimuli may drive amyloidosis. These data suggest a dual protective/damaging role for Aß, as has been described for other antimicrobial peptides.


Subject(s)
Alzheimer Disease/metabolism , Alzheimer Disease/microbiology , Amyloid beta-Peptides/physiology , Caenorhabditis elegans/metabolism , Caenorhabditis elegans/microbiology , Alzheimer Disease/genetics , Amyloid beta-Peptides/genetics , Animals , Animals, Genetically Modified , Caenorhabditis elegans/genetics , Disease Models, Animal , Female , Humans , Immunity, Innate/genetics , Immunity, Innate/physiology , Mice , Mice, Transgenic , Salmonella typhimurium/pathogenicity
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