WordNet

(mechanics) the equal and opposite force that is produced when any force is applied to a body; "every action has an equal and opposite reaction"
a response that reveals a persons feelings or attitude; "he was pleased by the audiences reaction to his performance"; "John feared his mothers reaction when she saw the broken lamp"
a bodily process occurring due to the effect of some antecedent stimulus or agent; "a bad reaction to the medicine"; "his responses have slowed with age" (同)response
doing something in opposition to another way of doing it that you dont like; "his style of painting was a reaction against cubism"
an idea evoked by some experience; "his reaction to the news was to start planning what to do"
extreme conservatism in political or social matters; "the forces of reaction carried the election"

PrepTutorEJDIC

{名}(…に対する)『反応』《+『to』+『名』》 / 〈U〉(…に対する)(政治的・社会的な)『反動』,逆コース《+『against』+『名』》 / 〈U〉〈C〉化学反応,化学変化 / 〈U〉〈C〉(物理学で)反作用

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1. 急性輸血反応が疑われる患者に対するアプローチ approach to the patient with a suspected acute transfusion reaction
2. 薬物アレルギー：分類および臨床的特徴 drug allergy classification and clinical features
3. 分子標的剤およびその他の生物製剤を用いた癌治療による皮膚合併症 cutaneous complications of molecularly targeted therapy and other biologic agents used for cancer therapy
4. 全身化学療法に対する輸注反応 infusion reactions to systemic chemotherapy
5. 造影剤に対する即時型過敏反応：再発反応の予防 immediate hypersensitivity reactions to radiocontrast media prevention of recurrent reactions

English Journal

Identification, expression and bioactivity of hexokinase in amphioxus: Insights into evolution of vertebrate hexokinase genes.

Li M1, Gao Z1, Wang Y1, Wang H2, Zhang S3.Author information 1Laboratory for Evolution & Development, Institute of Evolution & Marine Biodiversity and Department of Marine Biology, Ocean University of China, Qingdao 266003, China.2Key Laboratory of Nutrition and Metabolism, Institute for Nutritional Sciences, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai, China.3Laboratory for Evolution & Development, Institute of Evolution & Marine Biodiversity and Department of Marine Biology, Ocean University of China, Qingdao 266003, China. Electronic address: sczhang@ouc.edu.cn.AbstractHexokinase family includes hexokinases I, II, III and IV, that catalyze the phosphorylation of glucose to produce glucose 6-phosphate. Hexokinase IV, also known as glucokinase, is only half size of the other types of hexokinases that contain two hexokinase domains. Despite the enormous progress in the study of hexokinases, the evolutionary relationship between glucokinase and other hexokinases is still uncertain, and the molecular processes leading to the emergence of hexokinases in vertebrates remain controversial. Here we clearly demonstrated the presence of a single hexokinase-like gene in the amphioxus Branchiostoma japonicum, Bjhk, which shows a tissue-specific expression pattern, with the most abundant expression in the hepatic caecum, testis and ovary. The phylogenetic and synteny analyses both reveal that BjHK is the archetype of vertebrate hexokinases IV, i.e. glucokinases. We also found for the first time that recombinant BjHK showed functional enzyme activity resembling vertebrate hexokinases I, II, III and IV. In addition, a native glucokinase activity was detected in the hepatic caecum. Finally, glucokinase activity in the hepatic caecum was markedly reduced by fasting, whereas it was considerably increased by feeding. Altogether, these suggest that Bjhk represents the archetype of glucokinases, from which vertebrate hexokinase gene family was evolved by gene duplication, and that the hepatic caecum plays a role in the control of glucose homeostasis in amphioxus, in favor of the notion that the hepatic caecum is a tissue homologous to liver.
Gene.Gene.2014 Feb 10;535(2):318-26. doi: 10.1016/j.gene.2013.10.068. Epub 2013 Nov 19.
Hexokinase family includes hexokinases I, II, III and IV, that catalyze the phosphorylation of glucose to produce glucose 6-phosphate. Hexokinase IV, also known as glucokinase, is only half size of the other types of hexokinases that contain two hexokinase domains. Despite the enormous progress in t
PMID 24262936

WbgL: a novel bacterial α1,2-fucosyltransferase for the synthesis of 2'-fucosyllactose.

Engels L, Elling L.Author information Laboratory for Biomaterials, Institute of Biotechnology and Helmholtz-Institute for Biomedical Engineering, RWTH Aachen University, Worringer Weg 1, 52074 Aachen, Germany.AbstractFucosyltransferases (FucTs) are essential tools for the synthesis of fucosylated glycoconjugates. Multistep enzyme catalysis of fucosylated glycans is not limited as long as isolated and well-characterized FucTs are available. The present paper introduces a novel bacterial α1,2-FucT of the glycosyltransferase family 11 encoded by the gene wbgL in the E. coli O126 genome, which only displays 25-30% homology to previously published α1,2-FucTs. A tailor made cloning and expression strategy allowed the successful production of active soluble enzyme in the cytoplasm of E. coli BL21(DE3) and E. coli JM109(DE3), respectively. The lack of a DxD motif and its high activity without divalent metal ions suggests that WbgL belongs to the GT-B fold superfamily. Substrate screening revealed the highest activity for β4-linked galactoside acceptor substrates, such as lactose and lactulose, making WbgL unique among other characterized α1,2-FucTs. Based on its excellent kinetic efficiency for lactose, we present here a sequential reaction strategy for the synthesis of α1,2-fucosyllactose in one pot including the synthesis of the donor substrate 3,3'-Diaminobenzidine (GDP)-β-l-fucose by the bifunctional l-fucokinase/GDP-β-l-Fuc pyrophosphorylase of Bacteroides fragilis 9343.
Glycobiology.Glycobiology.2014 Feb;24(2):170-8. doi: 10.1093/glycob/cwt096. Epub 2013 Nov 17.
Fucosyltransferases (FucTs) are essential tools for the synthesis of fucosylated glycoconjugates. Multistep enzyme catalysis of fucosylated glycans is not limited as long as isolated and well-characterized FucTs are available. The present paper introduces a novel bacterial α1,2-FucT of the glycosyl
PMID 24249735

Glycidol induces axonopathy and aberrations of hippocampal neurogenesis affecting late-stage differentiation by exposure to rats in a framework of 28-day toxicity study.

Akane H1, Shiraki A2, Imatanaka N3, Akahori Y3, Itahashi M2, Abe H2, Shibutani M4.Author information 1Laboratory of Veterinary Pathology, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu-shi, Tokyo 183-8509, Japan.2Laboratory of Veterinary Pathology, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu-shi, Tokyo 183-8509, Japan; Pathogenetic Veterinary Science, United Graduate School of Veterinary Sciences, Gifu University, 1-1 Yanagido, Gifu-shi, Gifu 501-1193, Japan.3Chemicals Evaluation and Research Institute, 1-4-25 Koraku, Bunkyo-ku, Tokyo 112-0004, Japan.4Laboratory of Veterinary Pathology, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu-shi, Tokyo 183-8509, Japan. Electronic address: mshibuta@cc.tuat.ac.jp.AbstractDevelopmental exposure to glycidol induces aberrations of late-stage neurogenesis in the hippocampal dentate gyrus of rat offspring, whereas maternal animals develop axonopathy. To investigate the possibility whether similar effects on adult neurogenesis could be induced by exposure in a framework of 28-day toxicity study, glycidol was orally administered to 5-week-old male Sprague-Dawley rats by gavage at 0, 30 or 200mg/kg for 28 days. At 200mg/kg, animals revealed progressively worsening gait abnormalities as well as histopathological and immunohistochemical changes suggestive of axonal injury as evidenced by generation of neurofilament-L(+) spheroids in the cerebellar granule layer and dorsal funiculus of the medulla oblongata, central chromatolysis in the trigeminal nerve ganglion cells and axonal degeneration in the sciatic nerves. At the same dose, animals revealed aberrations in neurogenesis at late-stage differentiation as evidenced by decreases of both doublecortin(+) and dihydropyrimidinase-like 3(+) cells in the subgranular zone (SGZ) and increased reelin(+) or calbindin-2(+) γ-aminobutyric acid-ergic interneurons and neuron-specific nuclear protein(+) mature neurons in the dentate hilus. These effects were essentially similar to that observed in offspring after maternal exposure to glycidol. These results suggest that glycidol causes aberrations in adult neurogenesis in the SGZ at the late stage involving the process of neurite extension similar to the developmental exposure study in a standard 28-day toxicity study.
Toxicology letters.Toxicol Lett.2014 Jan 30;224(3):424-32. doi: 10.1016/j.toxlet.2013.10.026. Epub 2013 Nov 1.
Developmental exposure to glycidol induces aberrations of late-stage neurogenesis in the hippocampal dentate gyrus of rat offspring, whereas maternal animals develop axonopathy. To investigate the possibility whether similar effects on adult neurogenesis could be induced by exposure in a framework o
PMID 24185127