P21 activated kinase 6: a promising tool for predicting small cell lung cancer diagnosis and treatment response. [PDF]
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Endothelial glycocalyx shedding and oxidative stress in neuronal damage after return of spontaneous circulation in cardiac arrest. [PDF]
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Comparative Proteomic Analysis of Non-Bleached and Bleached Fragments of the Hydrocoral <i>Millepora complanata</i> Reveals Stress Response Signatures Following the 2015-2016 ENSO Event in the Mexican Caribbean. [PDF]
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Targeting Kupffer Cell Enolase 1 Attenuates Liver Inflammation and Injury in Hemorrhagic Shock. [PDF]
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Integrating transcriptomic and proteomic analyses reveals impaired carbohydrate metabolism in tobacco cytoplasmic male sterility. [PDF]
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Abstract Shellfish allergies constitute an important cause of food‐induced anaphylactic reactions, which pose challenges to food safety and human health worldwide. In the present study, the specific IgE (sIgE) binding characteristics of different shrimp proteins of black tiger shrimp (
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In the present study a cDNA encoding a phosphopyruvate hydratase (enolase) was cloned from the muscle of the Chinese shrimp (Fenneropenaeus chinensis) and named as FcEnolase. The cDNA of FcEnolase encoded a protein of 434 amino acid residues with a molecular mass 47.22 kDa. The residues 342-355 constituted the signature motif "LLLKVNQIGSVTES".
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The expression of the adenylate kinase isozymes and of phosphopyruvate hydratase was studied in man-mouse and man-hamster hybrid clones. Concordant segregation of the loci coding for AK-2 and PPH was observed in 54 of 55 primary hybrid clones, and these loci were demonstrated to be synthetic with the loci specifying PGM-1 and PGD.
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Abstract Phosphopyruvate hydratase (enolase) is a housekeeping gene for energy production in many eukaryotes. The 1914-base pair (bp) cDNA sequence of phosphopyruvate hydratase was obtained from the muscles of Marsupenaeus japonicus using RT-PCR and RACE. The results suggested that enolase is highly expressed in the muscle of M. japonicus but not
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Purification and Properties of Bacterial Phosphopyruvate Hydratase
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