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Showing 1 to 7 of 7 for “"alpha B Crystallin"”.

  1. Charakterisierung der Bindung des Stressproteins Alpha-B-Crystallin an kardiale Myofibrillen unter Ischämie

    … vorkommenden kardialen Stressproteins aB-Crystallin vom Zytosol an die Myofibrillen kommt. Dabei führen bereits kurzdauernde Ischämieperioden zu einer kompletten Umverteilung von aB-Crystallin in die Z/I-Region des Sarkomers. Es war das Ziel dieser Arbeit, diese Bindung von …

    wurz-thes Repository record for Charakterisierung der Bindung des Stressproteins Alpha-B-Crystallin an kardiale Myofibrillen unter Ischämie (opens in a new tab)

  2. Charakterisierung der kardialen Funktion des Stressproteins alpha-B-Crystallin am isolierten Papillarmuskel der Maus

    … Kardiomyopathie, der eine Missense-Mutation des alpha-B-Crystallin-Gens zugrunde liegt, weist auf eine wichtige Bedeutung des Stressproteins alpha-B-Crystallin im Herzen hin. Die chaperone-ähnlichen Eigenschaften von alpha-B-Crystallin und die unter kardialer Ischämie zu beobachtende schnelle …

    wurz-thes Repository record for Charakterisierung der kardialen Funktion des Stressproteins alpha-B-Crystallin am isolierten Papillarmuskel der Maus (opens in a new tab)

  3. The characterization of human [gamma]D-crystallin mutants and their differential interactions with the lens chaperone [alpha]B-crystallin

    … cataract cases, aggregation or precipitation of crystallin proteins results in the formation of large structures that scatter light, preventing the pinpoint focusing on the retina normally accomplished by the lens. The human eye lens is composed of fiber cells packed with crystallins up to 450 …

    mit Repository record for The characterization of human [gamma]D-crystallin mutants and their differential interactions with the lens chaperone [alpha]B-crystallin (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)

  5. In vitro interactions of the small heat shock protein chaperone human [alpha]B-crystallin with its physiological substrates in the lens [gamma]-crystallins

    The passive chaperone a-crystallin, a small heat shock protein, is one of the ubiquitous crystallins in vertebrate lenses, along with the [beta][gamma]-crystallins. It is composed of two subunits (~ 20 kDa) aA- and [alpha]B-crystallin (aA- and [alpha]B-Crys), which form a hetero-oligomeric, …

    mit Repository record for In vitro interactions of the small heat shock protein chaperone human [alpha]B-crystallin with its physiological substrates in the lens [gamma]-crystallins (opens in a new tab)

  6. Oral and Oropharyngeal Cancer - Aspects on Epidemiology and Prognostic Markers

    … used, making it difficult to compare results. Alpha B-crystallin, a small heat-shock protein, has in a previous study been found to be an independent prognostic marker for poor outcome in head and neck SCC. This thesis aimed to investigate the epidemiological changes for tongue cancer in the …

    lund Repository record for Oral and Oropharyngeal Cancer - Aspects on Epidemiology and Prognostic Markers (opens in a new tab)

  7. Microfluidic Approaches for Investigating Aggregated Forms of Disease-Related Proteins

    … as intrinsically disordered proteins, e.g. $\alpha$-Synuclein (aSyn) and A$\beta$40, and their respective oligomers. Another advantage of this method is its applicability for studies of brain aSyn from transgenic overexpressing mice (OVX). Furthermore, I explore the potential of IDS for the …

    cambridge Repository record for Microfluidic Approaches for Investigating Aggregated Forms of Disease-Related Proteins (opens in a new tab)