5 edition of Ubiquitin and the biology of the cell found in the catalog.
Includes bibliographical references and index.
|Statement||edited by Jan-Michael Peters, J. Robin Harris, and Daniel Finley.|
|Contributions||Peters, Jan-Michael., Harris, James R., Finley, Daniel.|
|LC Classifications||QP552.U24 U253 1998|
|The Physical Object|
|Pagination||xx, 472 p. :|
|Number of Pages||472|
|LC Control Number||98018550|
Ubiquitin is a small protein that exists in all eukaryotic performs its myriad functions through conjugation to a large range of target proteins. A variety of different modifications can occur. The ubiquitin protein itself consists of 76 amino acids and has a molecular mass of about kDa. Key features include its C-terminal tail and the 7 lysine residues. Ubiquitin is a small protein of 76 amino acids (Figure 1).Ubiquitin had been isolated from thymus prior to its identification as APF 10 The evidence available at the time indicated that it was a universal constituent of living cells. Indeed, ubiquitin is present in all eukaryotic cells and is one of the highly evolutionarily conserved proteins.
() The ubiquitinS proteasome system at the nexus of plant biology. Nat Rev Mol Cell Biol – [ PubMed ] Vijay-Kumar S, Bugg CE, Wilkinson KD, Vierstra RD, Hatfield PM, Cook WJ. Protein ubiquitination regulates almost every process in eukaryotic cells. The study of the many enzymes involved in the ubiquitination system and the development of ubiquitination-associated therapeutics are important areas of current research. Synthetic tools such as ubiquitin-based chemical probes have been maki Celebrating 10 years of Chemical Science.
Molecular Biology of the Cell is the classic in-dept text reference in cell biology. By extracting the fundamental concepts from this enormous and ever-growing field, the authors tell the story of cell biology, and create a coherent framework through which non-expert readers may approach the subject/5(). Cell census. What is the pH of a cell? What are the concentrations of different ions in cells? What are the concentrations of free metabolites in cells? What lipids are most abundant in membranes? How many proteins are in a cell? What are the most abundant proteins in a cell? How much cell-to-cell variability exists in protein expression?
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Ubiquitin and the Biology of the Cell, as the editors note, is published 10 years after the first book on ubiquitin appeared and 23 years after the first biochemical description of this ubiquitous Author: Mark Rolfe. The breadth of ubiquitin's roles in cell biology was first sketched, and the importance of ubiquitin-dependent proteolysis as a regulatory mechanism gained general acceptance.
The many strands of work that led to this new perception are re counted in this book. A consequence of this progress is that the field has grown dramatically since the.
The breadth of ubiquitin's roles in cell biology was first sketched, and the importance of ubiquitin-dependent proteolysis as a regulatory mechanism gained general acceptance.
The many strands of work that led to this new perception are re counted in this book. The many strands of work that led to this new perception are re-counted in Ubiquitin and the Biology of the Cell. A consequence of this progress is that the field has grown dramatically since the first book on ubiquitin was published almost a decade ago [M.
Ubiquitin and the biology of the cell book (ed.), Ubiquitin, Plenum Press, ].Price Range: £ - £ The human ubiquitin proteasome system (UPS) is comprised of nearly proteins.
Although originally identified as a mechanism of protein destruction, the UPS has numerous additional functions and mediates central signaling events in myriad processes involved in both cellular and organismal health and homeostasis.
Numerous pathways within the UPS are implicated in disease, Author: Matthew Summers. Protein Degradation: Cell Biology of the Ubiquitin-Proteasome System R. John Mayer, Aaron J. Ciechanover, Martin Rechsteiner The third of four volumes discusses the role of ubiquitin-mediated protein breakdown in cellular regulation and physiology.
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.
Aaron Ciechanover is one of the editors of this series, and Avram Hershko. The ubiquitin-proteasome pathway: on protein death and cell life.
EMBO J. 17, – (). CAS Article Google Scholar. As our understanding of ubiquitin-dependent control of stem cell biology increases, so too are calls to modulate the activity of ubiquitylation enzymes for therapeutic benefit. Proof of concept has been provided by thalidomide and related compounds that bind to a CUL4-dependent E3 ligase built around the substrate adaptor cereblon.
Ubiquitin C-terminal hydrolase is an example of the DUB that hydrolyses these bonds with broad specificity. Free polyubiquitin chains are cleaved by DUBs to produce monoubiquitin. The chains may be produced by the E1-E2-E3 machinery in the cell free from any substrate protein.
Ubiquitin (see Glossary) is a amino acid polypeptide used to post-translationally modify substrate proteins through covalent attachment at lysine residues via an isopeptide bond.
The cellular ubiquitin system impacts upon nearly all complex cellular events. Historically, it was first associated with the proteasomal degradation pathway and the term ‘ubiquitin proteasome system’ (UPS. ISBN: OCLC Number: Description: xx, pages: illustrations ; 24 cm: Contents: The ubiquitin system: past, present, and future perspectives / Avram Hershko --Polyubiquitin chains / Cecile M.
Pickart --The ubiquitin-conjugation system / Martin Scheffner, Susan Smith, and Stefan Jentsch --The deubiquitinating enzymes / Keith D. Wilkinson and Mark. Ubiquitylation is an essential posttranslational modification that controls cell division, differentiation, and survival in all eukaryotes.
By combining multiple E3 ligases (writers), ubiquitin-binding effectors (readers), and de-ubiquitylases (erasers) with functionally distinct ubiquitylation tags, the ubiquitin system constitutes a powerful signaling network that is employed in similar ways. The small protein ubiquitin plays a vital role in virtually all aspects of cellular life.
Among the diverse signaling outcomes associated with ubiquitination, the most well-established is the targeted degradation of substrates via the proteasome. During cell growth and proliferation, ubiquitin plays an outsized role in promoting progression through the cell cycle.
Abstract. The purpose of this chapter is threefold: (1) to provide the uninitiated reader a brief overview on the functions and mechanisms of the ubiquitin system, as an introduction to topics described in detail in the different chapters of this book; (2) to give to both the uninitiated and to the expert, but relatively newcomer ubiquitinologist a historical perspective on the discovery of.
Vikki M. Weake, Jerry L. Workman, in Handbook of Cell Signaling (Second Edition), Ubiquitination of target proteins involves a three-step enzymatic process. Ubiquitination functions as a versatile signaling mark because substrates can be modified either by the addition of a single ubiquitin molecule (mono-ubiquitination), or by the conjugation of ubiquitin to preceding ubiquitin moieties.
The tumor suppressor p53 prevents tumorigenesis and cancer progression by maintaining genomic stability and inducing cell growth arrest and apoptosis.
Because of the extremely detrimental nature of wild-type p53, cancer cells usually mutate the TP53 gene in favor of their survival and propagation. Some of the mutant p53 proteins not only lose the wild-type activity, but also acquire oncogenic.
* ubiquitin in transcription, DNA monitoring and repair, and peroxisomes, * endocytosis and membrane trafficking * the ubiquitin-proteasome system in plants and muscle development.
Required reading for molecular biologists, cell biologists and physiologists with an interest in the : $ In the past 2 years, two ubiquitin-dependent proteolytic pathways have been established as important players in the regulation of the cell division cycle.
In S. cerevisiae, the entry into S phase requires ubiquitin-mediated degradation of a cdk inhibitor, p40Sic1, in a.
ubiquitin ligase; This protein binds the Ubiquitin-conjugating enzyme with one domain and the target by the other domain. These proteins thus specify the target of ubiquitination by the Ubiquitin-conjugating enzyme protein. The original ubiquitin modification is further modified by the addition, repetitively, of other ubiquitins, making a chain.
The results with ts85 cells also indicated that ubiquitin conjugation was essential for cell viability, the first hint of the enormous, many-sided biological importance of the ubiquitin system. In addition, ts85 cells were preferentially arrested in the G2 phase of the cell cycle, and the synthesis of heat-stress proteins was strongly induced.Protein Ubiquitination in Eukaryotic Biology Ubiquitin is a small, conserved protein present in all eukaryotes.
The cell uses ubiquitin to modify proteins and modulate their functions. When a protein substrate is modified by a chain of multiple ubiquitin molecules. The posttranslational modification with ubiquitin, a process referred to as ubiquitylation, controls almost every process in cells.
Ubiquitin can be attached to substrate proteins as a single moiety or in the form of polymeric chains in which successive ubiquitin molecules are connected through specific isopeptide bonds. Reminiscent of a code, the various ubiquitin modifications adopt distinct.