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by A.J. Rivett
Download Intracellular Protein Degradation, Volume 27 (Advances in Molecular and Cell Biology) fb2
Biological Sciences
  • Author:
    A.J. Rivett
  • ISBN:
    0762303875
  • ISBN13:
    978-0762303878
  • Genre:
  • Publisher:
    Elsevier Science; 1 edition (August 21, 1998)
  • Pages:
    310 pages
  • Subcategory:
    Biological Sciences
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    1878 kb
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Print Book & E-Book. View all volumes in this series: Advances in Molecular and Cell Biology. Pathways for the Degradation of Intracellular Proteins within Lysosomes in Higher Eukaryotes (E. Knecht, .

Print Book & E-Book. ISBN 9780762303878, 9780080877129. Biochemical Properties and Biological Functions of ATP-Dependent Proteases in Bacterial Cells (. The Critical Role of the Pathway in Muscle Wasting in Comparison to Lysosomal and Ca2+-dependent Systems (D. Attaix and D. Taillandier).

Protein degradation has been identified as a centerpiece of regulation of cell functions. Not surprisingly, its deregulation is implied in almost any pathological condition. This book describes how aged proteins are eliminated during cell metabolism, how cell proliferation is regulated by protein degradation and how its deregulation can contribute to the development of cancer, how protein degradation is modified during normal and abnormal aging, in particular with regard to Alzheimer's disease and other degenerative diseases of the brain and central nervous system.

Somat Cell Mol Genet 20: 27–38. Google Scholar van Broekhoven C (1995) Molecular genetics of Alzheimer disease: identification of genes and mutations. Andrew SE, Goldberg YP, Kremer B, et al (1993) The relationship between trinucleotide (CAG) repeat length and clinical features of Huntington's disease. Nature Genet 4: 398–403. Johnson JW, Ascher P (1990) Voltage-dependent block by intracellular Mg2+ of -activated channels. Biophys J 57: 1085–1090. van Broekhoven C (1995) Molecular genetics of Alzheimer disease: identification of genes and mutations.

Intracellular Protein Degradation book. Intracellular protein degradation is much more than just a mechanism for the removal of incorrectly folded or damaged proteins.

Intracellular Protein Degradation,27 . Описание: The book summarizes our progress in understanding the receptor and intracellular signaling mechanisms utilized by a family of proteins called the semaphorins. Originally these protein were identified as "axon guidance cues" important for the formation of nerve tracts but now it is realized that semaphorins subserve several distinct functions in a multitude of organ systems.

Advances in optical methods, in vitro culture systems and molecular biology led to the advent of live cell imaging techniques

Advances in optical methods, in vitro culture systems and molecular biology led to the advent of live cell imaging techniques.

Molecular and cell biology, Cell biology. Advances in cellular, molecular, and biomechanical sciences have enabled the appreciation and understanding of the construction and function of the endothelial barrier, as well as the many important regulatory functions of the endothelium. Thus, as keepers of the dam, an intimate acquaintance with its composition, maintenance, and regulation is needed. A system of intracellular activatory and inhibitory signaling molecules interacts directly or indirectly with these cytoskeletal structures and tightly controls the cytoskeletal function.

1 - A hierarchy of molecular recognition signals for protein degradation - 5. Regulation of intracellular.

Open Reading Frame (ORF). PCR & Amplification.

This volume brings together a set of reviews that provide a summary of our current knowledge of the proteolytic machinery and of the pathways of protein breakdown of prokaryotic and eukaryotic cells. Intracellular protein degradation is much more than just a mechanism for the removal of incorrectly folded or damaged proteins. Since many short-lived proteins have important regulatory functions, proteolysis makes a significant contribution to many cellular processes including cell cycle regulation and transciptional control. In addition, limited proteolytic cleavage can provide a rapid and efficient mechanism of enzyme activation or inactivation in eukaryotic cells. In the first chapter, Maurizi provides an introduction to intracellular protein degradation, describes the structure and functions of bacterial ATP-dependent proteases, and explores the relationship between chaperone functions and protein degradation. Many of the principles also apply to eukaryotic cells, although the proteases involved are often not the same. Interestingly, homologues of one of the bacterial proteases, Ion protease, have been found in mitochondria in yeast and mammals, and homologues of proteasomes, which are found in all eukaryotic cells (see below), have been discovered in some eubacteria. Studies of proteolysis in yeast have contributed greatly to the elucidation of both lysosomal (vacuolar) and nonlysosomal proteolytic pathways in eukaryotic cells. Thumm and Wolf (chapter 2) describe studies that have elucidated the functions of proteasomes in nonlysosomal proteolysis and the contributions of lysosomal proteases to intracellular protein breakdown. Proteins can be selected for degradation by a variety of differen mechanisms. The ubiquitin system is one complex and highly regulated mechanism by which eukaryotic proteins are targetted for degradation by proteosomes. In chapter 3, Wilkinson reviews the components and functions of the ubiquitin system and considers some of the known substrates for this pathway which include cell cycle and transcriptional regulators. The structure and functions of proteosomes and their regulatory components are described in the two subsequent chapters by Tanaka and Tanahashi and by Dubiel and Rechsteiner. Proteasomes were the first known example of threonine proteases. They are multisubunit complexes that, in addition to being responsible for the turnover of most short-lived nuclear and cytoplasmic protein, are also involved in antigen processing for presentation by the MHC class I pathway. Recent studies reviewed by McCracken and colleagues (chapter 6) lead to the exciting conclusion that some ER-associated proteins are degraded by cytosolic proteasomes. Lysosomes are responsible for the degradation of long-lived proteins and for the enhanced protein degradation observed under starvation conditions. In chapter 7 Knecht and colleagues review the lysosomal proteases and describe studies of the roles of lysosomes and the mechanisms for protein uptake into lysosomes. Methods of measuring the relative contribution of different proteolytic systems (e.g., ubiquitin-proteasome pathway, calcium-dependent proteases, lysosomes) to muscle protein degradation, and the conclusions from such studies, are reviewed by Attai and Taillinder in the following chapter. Finally, proteases play an important role in signaling apoptosis by catalyzing the limited cleavage of enzymes. Mason and Beyette review the role of the major players, caspases, which are both activated by and catalyze limite proteolysis, and also consider the involvement of other protoelytic enzymes in this pathway leading cell death.