We propose a novel network that learns a part-aligned representation for person re-identification. It handles the body part misalignment problem, that is, body parts are misaligned across human detections due to pose/viewpoint change and unreliable detection. Our model consists of a two-stream network (one stream for appearance map extraction and the other one for body part map extraction) and a bilinear-pooling layer that generates and spatially pools a partaligned map. Each local feature of the part-aligned map is obtained by a bilinear mapping of the corresponding local appearance and body part descriptors. Our new representation leads to a robust image matching similarity, which is equivalent to an aggregation of the local similarities of the corresponding body parts combined with the weighted appearance similarity. This part-aligned representation reduces the part misalignment problem significantly. Our approach is also advantageous over other pose-guided representations (e.g., extracting representations over the bounding box of each body part) by learning part descriptors optimal for person re-identification. For training the network, our approach does not require any part annotation on the person re-identification dataset. Instead, we simply initialize the part sub-stream using a pre-trained sub-network of an existing pose estimation network, and train the whole network to minimize the re-identification loss. We validate the effectiveness of our approach by demonstrating its superiority over the state-of-the-art methods on the standard benchmark datasets, including Market-1501, CUHK03, CUHK01 and DukeMTMC, and standard video dataset MARS.

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TRPV1 is a channel expressed highly in small sensory neurons. TRPV1 is a ligand-gated, cation channel that is activated by heat, acid and capsaicin, a principal ingredient in hot peppers. Because of its possible role as a polymodal molecular detector, TRPV1 is studied most extensively. In mice lacking TRPV1, thermal hyperalgesia induced by inflammation is reduced, suggesting a role for mediating inflammatory pain. Activity of TRPV1 is modulated by actions of various kinases such as protein kinase A and C. Furthermore, phosphorylation by Ca(2+)-calmodulin-dependent kinase II is required for its ligand binding. TRPV1 is activated by various endogenous lipids, such as anandamide, N-arachidonoyl-dopamine, and various metabolic products of lipoxygenases. 12-hydroperoxyeicosatetraenoic acid, an immediate metabolic product of 12-lipoxygenase, activates TRPV1 and shares 3-dimensional structural similarity with capsaicin. Because lipoxygenase products can activate TRPV1 in sensory neurons, upstream signals to lipoxygenase/TRPV1 pathway have been questioned. Indeed, bradykinin, a potent pain-causing substance, is now known to activate TRPV1 via lipoxygenase pathway. However, we cannot overlook the sensitizing effect of bradykinin via the phospholipase C or protein kinase C pathway. Interestingly, histamine, a pruritogenic substance, also appears to use the lipoxygenase/TRPV1 pathway in order to excite sensory neurons. Because of its role in the mediation of nociception, antagonists of TRPV1 are targeted for development of potential analgesics. In the present review, theoretical background of organic synthesis of SC0030, a potent antagonist of TRPV1 is presented.

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The Hsp90 facilitates proper folding of signaling proteins associated with cancer progression, gaining attention as a target for therapeutic intervention.