The Ubiquitin System
Author : Milton J. Schlesinger
Publisher : Cold Spring Harbor Laboratory Press
Page : 218 pages
File Size : 50,87 MB
Release : 1988
Category : Science
ISBN :
Ubiquitin and the Biology of the Cell
Author : Jan-Michael Peters
Publisher : Springer Science & Business Media
Page : 498 pages
File Size : 29,10 MB
Release : 1998-05-31
Category : Science
ISBN : 0306456494
Book Description
The last several years have been a landmark period in the ubiquitin field. 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 first book on ubiquitin was published almost a decade ago [M. Rechsteiner (ed. ), Ubiquitin, Plenum Press, 1988]. In this span, students of the cell cycle, transcription, signal transduction, protein sorting, neuropathology, cancer, virology, and immunology have attempted to chart the role of ubi quit in in their particular experimental systems, and this integration of the field into cell biology as a whole continues at a remarkable pace. We hope that for active researchers in the field as well as for newcomers and those on the fence, this book will prove helpful for its breadth, historical perspective, and practical tips. Structural data are now available on many of the components of the ubiquitin pathway. The structures have provided basic insights into the unusual biochemical mechanisms of ubiquitination and proteasome-mediated proteolysis. Because high-speed computer graphics can convey structures more effectively than print media, we have supplemented the figures of the book with a Worldwide Web site that can display the structures in a flexible, viewer-controlled format.
Ubiquitin Proteasome System
Author : Matthew Summers
Publisher : BoD – Books on Demand
Page : 228 pages
File Size : 15,85 MB
Release : 2019-06-19
Category : Science
ISBN : 1838804900
Book Description
The human ubiquitin proteasome system (UPS) is comprised of nearly 1000 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, ranging from cancer to neurodegenerative diseases such as Parkinson's. The goal of this book is to deliver a collection of synopses of current areas of UPS research that highlights the importance of understanding the biology of the UPS to identify disease-relevant pathways, and the need to elucidate the molecular machinations within the UPS to develop methods for therapeutic modulation of these pathways.
Ubiquitin Proteasome System
Author : Aldrin V. Gomes
Publisher : Nova Medicine & Health
Page : 0 pages
File Size : 41,7 MB
Release : 2018
Category : Central nervous system
ISBN : 9781536135183
Book Description
Over the last decade, major advancements in our understanding of the ubiquitin-proteasome system (UPS) have occurred. This book focuses on recent trends in the UPS. The UPS is possibly the most complex of all intracellular pathways as close to 7% of all genes in the human genome make up part of the UPS. This complex system serves as an essential role in intracellular protein degradation, and because of its critical function, improper functioning of the UPS is associated with nearly all know diseases, including cancer, cardiovascular disease, and neurological diseases. The proteolytic component of the UPS is the proteasome, a multicatalytic complex found in the nucleus and cytoplasm. Another form of the proteasome, the immunoproteasome, is less abundant than the constitutive proteasome, but is important in immune response and degradation of oxidized proteins, and recent research suggests that it may be important in longevity. The articles in this book discuss recent findings which indicate that mutations in proteins involved with the UPS are associated with genetic diseases such as familial dilated cardiomyopathy, Nakajo syndrome, and spinal muscular atrophy (X-linked). Some chapters also discuss recent results which suggest that the UPS is heavily regulated by post-translational modifications such as phosphorylation, acetylation, and methylation. The UPS is also heavily regulated by ubiquitination itself. This book contains a research article using PubMed bibliometric data to present current research trends in the UPS. Articles are written so that no one tissue is emphasized to allow readers from any discipline to benefit from this information.
Total Chemical Synthesis of Proteins
Author : Ashraf Brik
Publisher : John Wiley & Sons
Page : 626 pages
File Size : 44,53 MB
Release : 2021-06-08
Category : Science
ISBN : 3527346600
Book Description
How to synthesize native and modified proteins in the test tube With contributions from a panel of experts representing a range of disciplines, Total Chemical Synthesis of Proteins presents a carefully curated collection of synthetic approaches and strategies for the total synthesis of native and modified proteins. Comprehensive in scope, this important reference explores the three main chemoselective ligation methods for assembling unprotected peptide segments, including native chemical ligation (NCL). It includes information on synthetic strategies for the complex polypeptides that constitute glycoproteins, sulfoproteins, and membrane proteins, as well as their characterization. In addition, important areas of application for total protein synthesis are detailed, such as protein crystallography, protein engineering, and biomedical research. The authors also discuss the synthetic challenges that remain to be addressed. This unmatched resource: Contains valuable insights from the pioneers in the field of chemical protein synthesis Presents proven synthetic approaches for a range of protein families Explores key applications of precisely controlled protein synthesis, including novel diagnostics and therapeutics Written for organic chemists, biochemists, biotechnologists, and molecular biologists, Total Chemical Synthesis of Proteins provides key knowledge for everyone venturing into the burgeoning field of protein design and synthetic biology.
Proteostasis and Disease
Author : Rosa Barrio
Publisher : Springer Nature
Page : 350 pages
File Size : 42,36 MB
Release : 2020-04-09
Category : Science
ISBN : 3030382664
Book Description
This book, written by members of the European network PROTEOSTASIS, provides an up-to-date review of the research regarding protein homeostasis in health and disease. With new discoveries contributing to the increasing complexity of this topic, the book offers a detailed overview of the pathways regulating protein homeostasis, including autophagy and the ubiquitin protein family. Following a basic introduction, it explains how defects in protein homeostasis contribute to numerous pathologies, including cancer, neurodegeneration, inflammation and a number of rare diseases. In addition, it discusses, the role of protein homeostasis in cellular development and physiology. Highlighting the latest research in the field of protein homeostasis and its implications for various clinically relevant diseases, the book appeals to researchers and clinicians, while also offering a reference guide for scholars who are new to the field.
Proteasome Inhibitors in Cancer Therapy
Author : Julian Adams
Publisher : Springer Science & Business Media
Page : 319 pages
File Size : 22,67 MB
Release : 2004-05-25
Category : Medical
ISBN : 1592597947
Book Description
A panel of leading academic and pharmaceutical investigators takes stock of the remarkable work that has been accomplished to date with proteasome inhibitors in cancer, and examines emerging therapeutic possibilities. The topics range from a discussion of the chemistry and cell biology of the proteasome and the rationale for proteasome inhibitors in cancer to a review of current clinical trials underway. The discussion of rationales for testing proteasome inhibitors in cancer models covers the role of the proteasome in NF-kB activation, the combining of conventional chemotherapy and radiation with proteasome inhibition, notably PS-341, new proteasome methods of inhibiting viral maturation, and the role of protesome inhibition in the treatment of AIDS. The authors also document the development of bortezomib (VelcadeTM) in Phase I clinical trials and in a multicentered Phase II clinical trials in patients with relapsed and refractory myeloma.
The dynamic state of body constituents
Author : Rudolf Schoenheimer
Publisher :
Page : 78 pages
File Size : 50,47 MB
Release : 1949
Category :
ISBN :
Book Description
Protein Turnover and Lysosome Function
Author : Harold L. Segal
Publisher :
Page : 826 pages
File Size : 47,9 MB
Release : 1978
Category : Science
ISBN :
Book Description
Protein Turnover and Lysosome Function comprises the proceedings of a symposium under the same title held at the State University of New York at Buffalo on August 21-26, 1977. The book discusses mechanisms of protein turnover, as well as the identification and characterization of intracellular proteases. The text also describes the internalization of macromolecules into the intracellular digestive system; the types of specificity entailed; and the fate of the membrane material involved in the vacuolization process. Biochemists, pathologists, cell biologists, molecular biologists, and physiologists will find the book invaluable.
The Septin CDCrel-1 [microform] : Protein Associations, Modifications and Effects on Exocytosis
Author : Crestina L. Beites
Publisher : National Library of Canada = Bibliothèque nationale du Canada
Page : 452 pages
File Size : 40,15 MB
Release : 2004
Category :
ISBN : 9780612915961
Book Description
SNARE proteins mediate the docking and/or fusion of the vesicle with the plasma membrane. However, it is not clearly understood how this process is regulated. In a search for potential SNARE regulators, we have identified a novel snare interacting protein, the septin CDCrel-1. Septins were first identified as filamentous proteins required for cytokinesis in yeast. However, in mammals little is known about their functions. I show here that cdcrel-1 is predominantly expressed in the brain where it associates with membranes via binding to syntaxin 1A. Wildtype CDCrel-1 transfected into HIT-T15 cells inhibits secretion while mutated forms of CDCrel-1 potentiate secretion, suggesting that cdcrel-1 may be regulating vesicle targeting and/or fusion events. I further map the CDCrel-1 domains important for syntaxin binding and investigate the ability of CDCrel-1 to bind to syntaxin when in various SNARE complexes. CDCrel-1 can bind syntaxin in a SNARE complex, but its binding is occluded by alpha-SNAP. This suggests that CDCrel-1 may act as a novel filamentous element, regulating the delivery and/or fusion of vesicles to the presynaptic membrane through its interaction with syntaxin and the 7S complex. The regulation of filaments may be via post-translational modifications. Indeed we have discovered a novel interaction between SUMO E3 PIAS proteins and CDCrel-1. The conjugation of SUMO to substrates is dependent upon an E1 and E2, whereas specificity is mediated by an E3. Although several SUMO-1 substrates have been characterized, conjugation solely by SUMO-2/3 has not been described. Here I describe the colocalization of CDCrel-1 with SUMO-2 and 3 but not SUMO-1. Transfection of SUMO-2/3 but not SUMO-1 causes a reorganization of CDCrel-1 distribution in CHO cells. Furthermore, CDCrel-1 sequesters the nuclear pool of SUMO-2/3 and of the E2 Ubc9 but not SUMO1 into the cytoplasm. Sumoylation of CDCrel-l is shown in vivo and putative SUMO modification sites on CDCrel-1 are investigated by deletion of lysine residues. These experiments strongly suggest that CDCrel-1 is sumoylated specifically by SUMO-2/3. Sumoylation of CDCrel-1 may therefore play a regulatory role in secretion and septin filament formation. Future work will be aimed at determining the functional significance of SUMO modified CDCrel-1.
