5 edition of Intracellular Protein Degradation (Advances in Molecular and Cell Biology) found in the catalog.
Published
December 1, 1998
by Elsevier Science
.
Written in
| The Physical Object | |
|---|---|
| Format | Hardcover |
| Number of Pages | 312 |
| ID Numbers | |
| Open Library | OL8031880M |
| ISBN 10 | 0762303875 |
| ISBN 10 | 9780762303878 |
The first volume in a new series dedicated to protein degradation, this book lays the foundations of targeted protein breakdown via the ubiquitin pathway. The outstanding importance of the ubiquitin pathway has been recognized with the Nobel Prize in Chemistry for Aaaron Chiechanover, Avram Hershko, and Irwin Rose. This book contains most of the papers presented. at the Second International Symposium on Intracellular Protein OItaboiism, which was held on May , in Ljubljana, Yugoslavia. The papers presented in this book cover a wide variety of areas related to protein turnover and responsible.
The roles of intracellular protein-degradation pathways in neurodegeneration David C. Rubinsztein 1 Nature volume , pages – () Cite this articleCited by: THE LYSOSOME AND INTRACELLULAR PROTEIN DEGRADATION. In the mids, Christian de Duve discovered the lysosome (see, for example, de Duve et al.8 and Gianetto et al.9) (Figure 1).The lysosome was first recognized biochemically in rat liver as a vacuolar structure that contains various hydrolytic enzymes which function optimally at an acidic pH. Here we used five sets of ‘bait-genes’ known to be involved in protein degradation (29 genes), amino acid metabolism (36), chlorophyll breakdown (4), ubiquitinylation (31) and autophagy (5 genes) in an attempt to identify further candidate genes involved in the mechanism of protein degradation as an alternative respiratory by:
The contribution of proteases in the central vacuole of Chara corallina internodal cells to overall cellular protein degradation was examined. I measured the decrease in the trichloroacetic acid (TCA)-precipitable radioactivity in the cell for a 6-d chase period after labeling cellular proteins with [3H]leucine. The kinetics of [3H]leucine-labeled protein disappearance showed that the half. Protein degradation in the lysosomes Lysosomes degrade extracellular proteins that the cell incorporates by endocytosis. Lysosomes can also degrade intracellular proteins that are enclosed in other membrane-limited organellas. In well-nourished cells, lysosomal protein degradation is non-selective (non- regulated). In starved cells, lysosomes. The lysosome and intracellular protein degradation: In the mids, Christian de Duve discovered the lysosome (see, for example, Refs. 8 and 9 and Figure 1). The lysosome was first recognized biochemically in rat liver as a vacuolar structure that contains various hydrolytic enzymes which function optimally at an acidic pH. It is.
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SyntaxTextGen not activated Therefore, our pdf is to provide an updated summary of the current knowledge on the proteolytic machinery involved in intracellular protein degradation and its physiological and pathological relevance, especially addressed to newcomers in the field who may find further details in more specialized by: All eukaryotic cells contain download pdf compartments that interact with the cell's environment.
Vesicles transport proteins and lipids between these compartments via two major pathways: the outwards, exocytic pathway, carries material synthesized in the cytoplasm to the cell milieu, and the inwards, endocytic pathway, internalizes material from the environment to the inside of the by: 1.
Intracellular protein degradation: constant destruction ebook continuous rejuvenation All intracellular proteins undergo continuous synthesis and degradation (Mortimore et al., ; Schimke, ). This constant protein turnover, among other functions, helps reduce, to a .
