A TMT-based proteomic approach for investigating the effect of electron beam irradiation on the textural profiles of Litopenaeus vannamei during chilled storage.

[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.