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Showing 1 to 4 of 4 for “"small heat-shock protein (sHsp)"”.

  1. Degradation of the E. coli small heat-shock proteins by the AAA+ protease lon : significance to protein quality-control

    … and elimination of damaged and aggregated proteins requires the concerted effort of several branches of the protein quality-control network. This network includes refolding chaperones, disaggregases, holdases and proteases. Many years of investigation have led to a partial understanding of …

    mit Repository record for Degradation of the E. coli small heat-shock proteins by the AAA+ protease lon : significance to protein quality-control (opens in a new tab)

  2. Characterization of a Beta-glucosidase Aggregating Factor Responsible for the Null Beta-glucosidase Phenotype in Maize (Zea mays L.)

    … aggregating factor (BGAF). BGAF is a 32 kD protein that binds specifically to β-glucosidase and renders it insoluble during extraction. The data unequivocally demonstrate that BGAF is solely responsible for β-glucosidase aggregation and insolubility, and thus, the apparent null phenotype. …

    vt Repository record for Characterization of a Beta-glucosidase Aggregating Factor Responsible for the Null Beta-glucosidase Phenotype in Maize (Zea mays L.) (opens in a new tab)

  3. The sHsp expression signature in the brain and modulation in models of chronic neurodegeneration

    Intrinsic protein folding pathways are modulated by molecular chaperones, such as the diverse<br/>group of heat shock proteins (Hsps). Among these is the small heat shock protein (sHsp)<br/>family which in the mammalian genome consists of 10 low molecular weight (15-30kDa)<br/>members. The sHsps …

    soton Repository record for The sHsp expression signature in the brain and modulation in models of chronic neurodegeneration (opens in a new tab)

  4. Contributions of aromatic pairs of human Gamma-D-Crystallin to its folding, stability, aggregation, and interaction with human Alpha B-Crystallin

    Two distinct groups of proteins, a-crystallins and [Beta][gamma]-crystallins, constitute 90% of the vertebrate eye lens soluble proteins. Long-term solubility and stability against unfolding and aggregation are essential properties of crystallins and crucial to the function of the lens. Aggregation …

    mit Repository record for Contributions of aromatic pairs of human Gamma-D-Crystallin to its folding, stability, aggregation, and interaction with human Alpha B-Crystallin (opens in a new tab)