The Experts below are selected from a list of 27 Experts worldwide ranked by ideXlab platform

Chen Huang - One of the best experts on this subject based on the ideXlab platform.

  • Retraction Note to: Effects of a Terrified-Sound Stress on Serum Proteomic Profiling in Mice
    Journal of molecular neuroscience : MN, 2016
    Co-Authors: Juan Yang, Xin Zhang, Xiaofan Xiong, Lingyu Zhao, Liying Liu, Yannan Qin, Tusheng Song, Chen Huang
    Abstract:

    The serum proteomic profiles of mice exposed to terrified-sound-induced stress and after stress release were investigated. Serum samples from 32 mice were divided into four groups (n = 8 each) and analyzed using matrix-assisted laser desorption and ionization time-of-flight mass spectrometry techniques (MALDI-TOF MS) combined with magnetic bead-based weak cation-exchange chromatography. ClinProTools software identified several distinct markers that differed between the stressed and control groups and between the stress released and stressed released controls. Of 33 m/z peaks that differed among the four groups, 17 were significantly different (P < 0.05). Five peaks (m/z: 2793.37, 2924.86, 1979.90, 3492.49, 3880.24) showed significant differences in expression after exposure to terrified-sound stress and returned to control levels after stress release. These were sequence identified as peptide regions of Dimethylaniline Monooxygenase, myosin-9, uncharacterized protein in Rattus norvegicus, apolipoprotein C-I, and plasma serine protease inhibitor (Serpina 5). Our study provides the first evidence of significant changes in serum proteomic profiles in mice exposed to terrified-sound stress, which suggests that protein expression profiles are affected by the stress. Normal expression levels were restored after stress release, suggesting the activation of self-adjustment mechanisms for the recovery of protein expression levels altered by this stress.

Juan Yang - One of the best experts on this subject based on the ideXlab platform.

  • Retraction Note to: Effects of a Terrified-Sound Stress on Serum Proteomic Profiling in Mice
    Journal of molecular neuroscience : MN, 2016
    Co-Authors: Juan Yang, Xin Zhang, Xiaofan Xiong, Lingyu Zhao, Liying Liu, Yannan Qin, Tusheng Song, Chen Huang
    Abstract:

    The serum proteomic profiles of mice exposed to terrified-sound-induced stress and after stress release were investigated. Serum samples from 32 mice were divided into four groups (n = 8 each) and analyzed using matrix-assisted laser desorption and ionization time-of-flight mass spectrometry techniques (MALDI-TOF MS) combined with magnetic bead-based weak cation-exchange chromatography. ClinProTools software identified several distinct markers that differed between the stressed and control groups and between the stress released and stressed released controls. Of 33 m/z peaks that differed among the four groups, 17 were significantly different (P < 0.05). Five peaks (m/z: 2793.37, 2924.86, 1979.90, 3492.49, 3880.24) showed significant differences in expression after exposure to terrified-sound stress and returned to control levels after stress release. These were sequence identified as peptide regions of Dimethylaniline Monooxygenase, myosin-9, uncharacterized protein in Rattus norvegicus, apolipoprotein C-I, and plasma serine protease inhibitor (Serpina 5). Our study provides the first evidence of significant changes in serum proteomic profiles in mice exposed to terrified-sound stress, which suggests that protein expression profiles are affected by the stress. Normal expression levels were restored after stress release, suggesting the activation of self-adjustment mechanisms for the recovery of protein expression levels altered by this stress.

Eivind Almaas - One of the best experts on this subject based on the ideXlab platform.

  • Population-specific renal proteomes of marine and freshwater three-spined sticklebacks.
    Journal of proteomics, 2015
    Co-Authors: Dietmar Kültz, Darlene Paguio, Tuan Pham, Marius Eidsaa, Eivind Almaas
    Abstract:

    Quantitative proteomics was used to reveal biochemical differences in kidneys of marine and freshwater three-spined sticklebacks. More than 1500 unambiguous proteins were identified, 106 of which are robustly co-translationally modified. Amino-terminal acetylation sites for 94 and proline hydroxylation sites for 12 proteins, including 4 protein disulfide isomerases having the consensus motif APWCGHCK, were determined. More than 1500 proteins were quantified by LC-MS/MS yielding 120 proteins with consistent population-specific abundance differences. Twenty-five of these were selected for validation by data-independent acquisition (DIA) and spectral library based MS2 quantitation. A dense biochemical network was revealed, which promotes the synthesis of the organic osmolytes betaine, sorbitol, trimethylamine oxid (TMAO), and urea. It contains 33 of 49 proteins that are elevated in marine compared to freshwater sticklebacks, including the most highly elevated proteins (Dimethylaniline Monooxygenase, alanine-glyoxylate aminotransferase, glycine N-methyltransferase). Freshwater stickleback kidneys contain elevated levels of proteolytic, cytoskeletal, extracellular matrix, and calcium signaling proteins. Proteins that are most elevated in freshwater sticklebacks are ES1 protein homolog, apoptosis-associated speck-like protein containing a CARD and caspase 1. Protein-abundance network analysis demonstrates significantly higher levels of synchronized abundance control in marine sticklebacks. The significance of these findings for biochemical diversification of renal function in marine and FW sticklebacks is discussed.

Xin Zhang - One of the best experts on this subject based on the ideXlab platform.

  • Retraction Note to: Effects of a Terrified-Sound Stress on Serum Proteomic Profiling in Mice
    Journal of molecular neuroscience : MN, 2016
    Co-Authors: Juan Yang, Xin Zhang, Xiaofan Xiong, Lingyu Zhao, Liying Liu, Yannan Qin, Tusheng Song, Chen Huang
    Abstract:

    The serum proteomic profiles of mice exposed to terrified-sound-induced stress and after stress release were investigated. Serum samples from 32 mice were divided into four groups (n = 8 each) and analyzed using matrix-assisted laser desorption and ionization time-of-flight mass spectrometry techniques (MALDI-TOF MS) combined with magnetic bead-based weak cation-exchange chromatography. ClinProTools software identified several distinct markers that differed between the stressed and control groups and between the stress released and stressed released controls. Of 33 m/z peaks that differed among the four groups, 17 were significantly different (P < 0.05). Five peaks (m/z: 2793.37, 2924.86, 1979.90, 3492.49, 3880.24) showed significant differences in expression after exposure to terrified-sound stress and returned to control levels after stress release. These were sequence identified as peptide regions of Dimethylaniline Monooxygenase, myosin-9, uncharacterized protein in Rattus norvegicus, apolipoprotein C-I, and plasma serine protease inhibitor (Serpina 5). Our study provides the first evidence of significant changes in serum proteomic profiles in mice exposed to terrified-sound stress, which suggests that protein expression profiles are affected by the stress. Normal expression levels were restored after stress release, suggesting the activation of self-adjustment mechanisms for the recovery of protein expression levels altered by this stress.

Tusheng Song - One of the best experts on this subject based on the ideXlab platform.

  • Retraction Note to: Effects of a Terrified-Sound Stress on Serum Proteomic Profiling in Mice
    Journal of molecular neuroscience : MN, 2016
    Co-Authors: Juan Yang, Xin Zhang, Xiaofan Xiong, Lingyu Zhao, Liying Liu, Yannan Qin, Tusheng Song, Chen Huang
    Abstract:

    The serum proteomic profiles of mice exposed to terrified-sound-induced stress and after stress release were investigated. Serum samples from 32 mice were divided into four groups (n = 8 each) and analyzed using matrix-assisted laser desorption and ionization time-of-flight mass spectrometry techniques (MALDI-TOF MS) combined with magnetic bead-based weak cation-exchange chromatography. ClinProTools software identified several distinct markers that differed between the stressed and control groups and between the stress released and stressed released controls. Of 33 m/z peaks that differed among the four groups, 17 were significantly different (P < 0.05). Five peaks (m/z: 2793.37, 2924.86, 1979.90, 3492.49, 3880.24) showed significant differences in expression after exposure to terrified-sound stress and returned to control levels after stress release. These were sequence identified as peptide regions of Dimethylaniline Monooxygenase, myosin-9, uncharacterized protein in Rattus norvegicus, apolipoprotein C-I, and plasma serine protease inhibitor (Serpina 5). Our study provides the first evidence of significant changes in serum proteomic profiles in mice exposed to terrified-sound stress, which suggests that protein expression profiles are affected by the stress. Normal expression levels were restored after stress release, suggesting the activation of self-adjustment mechanisms for the recovery of protein expression levels altered by this stress.