A TMT-based proteomic approach for investigating the effect of electron beam irradiation on the textural profiles of Litopenaeus vannamei during chilled storage.
暂无分享,去创建一个
Yaqiong Liu | Jie Wang | Jianfeng Sun | Wenxiu Wang | R. Suo | Haoran Wang | Xingbo Liu | Yangyang Wang
[1] Yaqiong Liu,et al. Changes in quality characteristics of shrimp (Penaeus chinensis) during refrigerated storage and their correlation with protein degradation , 2022, Journal of Food Composition and Analysis.
[2] Haitao Shao,et al. Determination of the optimal electron beam irradiation dose for treating shrimp (Solenocera melantho) by means of physical and chemical properties and bacterial communities , 2022, LWT.
[3] Haile Ma,et al. Effects of ultrasound on the thawing of quick-frozen small yellow croaker (Larimichthys polyactis) based on TMT-labeled quantitative proteomic. , 2021, Food chemistry.
[4] Haitao Shao,et al. Effects of different doses of electron beam irradiation on bacterial community of Portunus trituberculatus , 2021 .
[5] S. Benjakul,et al. Label-free proteomic analysis revealed the mechanisms of protein oxidation induced by hydroxyl radicals in whiteleg shrimp (Litopenaeus vannamei) muscle. , 2021, Food & function.
[6] Yili Yang,et al. Food irradiation: a promising technology to produce hypoallergenic food with high quality , 2021, Critical reviews in food science and nutrition.
[7] Jie Pang,et al. Differential Proteomics Analysis of Penaeus vannamei Muscles with Quality Characteristics by TMT Quantitative Proteomics during Low-Temperature Storage. , 2021, Journal of agricultural and food chemistry.
[8] Keyu Wang,et al. Protein changes in shrimp ( Metapenaeus ensis ) frozen stored at different temperatures and the relation to water‐holding capacity , 2021 .
[9] S. Benjakul,et al. Insights into the similarities and differences of whiteleg shrimp pre-soaked with sodium tripolyphosphate and sodium trimetaphosphate during frozen storage. , 2021, Food chemistry.
[10] M. Magiera,et al. Tubulin polyglutamylation, a regulator of microtubule functions, can cause neurodegeneration , 2021, Neuroscience Letters.
[11] V. Venugopal,et al. Electron beam irradiation to control biohazards in seafood , 2021 .
[12] A. P. Diz,et al. Proteomic analysis and biochemical alterations in marine mussel gills after exposure to the organophosphate flame retardant TDCPP. , 2020, Aquatic toxicology.
[13] Yongkang Luo,et al. Search for proteomic markers for stunning stress and stress-induced textural tenderization in silver carp (Hypophthalmichthys molitrix) fillets using label-free strategy. , 2020, Food research international.
[14] M. Federighi,et al. Control of Foodborne Biological Hazards by Ionizing Radiations , 2020, Foods.
[15] Xiao-yan Zu,et al. Cobalt-60 and electron beam irradiation induced lipid oxidation on largemouth bass (Micropterus salmoides). , 2020, Journal of the science of food and agriculture.
[16] Meng Gou,et al. Protein biomarkers associated with frozen Japanese puffer fish (Takifugu rubripes) quality traits. , 2020, Food chemistry.
[17] Ravishankar Chandragiri Nagarajarao,et al. Effect of electron beam irradiation on the biochemical, microbiological and sensory quality of Litopenaeus vannamei during chilled storage , 2020, Journal of Food Science and Technology.
[18] Min Zhang,et al. Effects of gamma ray irradiation-induced protein hydrolysis and oxidation on tenderness change of fresh pork during storage. , 2020, Meat science.
[19] J. M. Gallardo,et al. Proteome profiling of L3 and L4 Anisakis simplex development stages by TMT-based quantitative proteomics. , 2019, Journal of proteomics.
[20] Lijun Sun,et al. Evaluation the effect of mycotoxins on shrimp ( Litopenaeus vannamei ) muscle and their limited exposure dose for preserving the shrimp quality , 2019, Journal of Food Processing and Preservation.
[21] J. Adamec,et al. Influence of oxidative damage to proteins on meat tenderness using a proteomics approach. , 2019, Meat science.
[22] Wenge Yang,et al. The effect of electron beam irradiation on IgG binding capacity and conformation of tropomyosin in shrimp. , 2018, Food chemistry.
[23] Wenge Yang,et al. Effects of electron beam irradiation on the biochemical properties and structure of myofibrillar protein from Tegillarca granosa meat. , 2018, Food chemistry.
[24] Yongkang Luo,et al. Differential proteomic analysis to identify proteins associated with quality traits of frozen mud shrimp (Solenocera melantho) using an iTRAQ-based strategy. , 2018, Food chemistry.
[25] M. Ciaramella,et al. Proteomic approach to characterize biochemistry of meat quality defects. , 2017, Meat science.
[26] Chung-Yi Wang,et al. Microbial decontamination of food by electron beam irradiation , 2015 .
[27] L. Tomanek. Proteomic responses to environmentally induced oxidative stress , 2015, The Journal of Experimental Biology.
[28] Sayanti Ghosh,et al. Effect of gamma irradiation and frozen storage on the quality of fresh water prawn (Macrobrachium rosenbergii) and tiger prawn (Penaeus monodon) , 2015 .
[29] W. Frontera,et al. Skeletal Muscle: A Brief Review of Structure and Function , 2014, Calcified Tissue International.
[30] D. Shi,et al. The PDZ-containing unconventional myosin XVIIIA regulates embryonic muscle integrity in zebrafish. , 2014, Journal of genetics and genomics = Yi chuan xue bao.
[31] Stefania Balzan,et al. Proteomic changes involved in tenderization of bovine Longissimus dorsi muscle during prolonged ageing. , 2012, Food chemistry.
[32] P. Pinton,et al. Mitochondria-Ros Crosstalk in the Control of Cell Death and Aging , 2011, Journal of signal transduction.
[33] Lingling Wang,et al. Two thymosin-repeated molecules with structural and functional diversity coexist in Chinese mitten crab Eriocheir sinensis. , 2009, Developmental and comparative immunology.
[34] P. Carmona,et al. Raman spectroscopic study of electron-beam irradiated cold-smoked salmon , 2009 .
[35] M. Ohnishi-Kameyama,et al. Postmortem changes in bovine troponin T isoforms on two-dimensional electrophoretic gel analyzed using mass spectrometry and western blotting: The limited fragmentation into basic polypeptides. , 2007, Meat science.
[36] Y. Xiong,et al. Biochemical changes in myofibrillar protein isolates exposed to three oxidizing systems. , 2006, Journal of agricultural and food chemistry.
[37] E. Huff-Lonergan,et al. Oxidative environments decrease tenderization of beef steaks through inactivation of mu-calpain. , 2004, Journal of animal science.
[38] A. Fukuzawa,et al. The entire cDNA sequences of projectin isoforms of crayfish claw closer and flexor muscles and their localization , 2004, Journal of Muscle Research & Cell Motility.
[39] M. Obinata,et al. Genome structure and differential expression of two isoforms of a novel PDZ-containing myosin (MysPDZ) (Myo18A). , 2003, Journal of biochemistry.
[40] M. Feder,et al. Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. , 1999, Annual review of physiology.