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Sunday, August 2, 2020 | History

3 edition of GTPases (Frontiers in Molecular Biology) found in the catalog.

GTPases (Frontiers in Molecular Biology)

by Alan Hall

  • 138 Want to read
  • 30 Currently reading

Published by Oxford University Press, USA .
Written in English


The Physical Object
Number of Pages360
ID Numbers
Open LibraryOL7406129M
ISBN 100199637458
ISBN 109780199637454

Small GTP-binding proteins (GTPases) serve to regulate a variety of cell signaling pathways and are therefore involved in a wide range of cell functions, processes, and most studied small GTPase proteins are Ras, Rho, Rac, Cdc42, Rap, and regulate molecular events by cycling between an inactive GDP-bound form and an active GTP-bound form.   The Rho GTPases were first discovered due to their homology to Ras GTPase. Approximately 30% of human cancers harbor an activating mutation to Ras, and Ras mutations promote cell growth and survival. Due to their homology to Ras, great enthusiasm has ensued over the discovery of the Rho : Kenneth Van Golen.

Small GTPases of the Ras superfamily are key regulators of diverse cellular and developmental events, including differentiation, cell division, vesicle transport, nuclear assembly, and control of the cytoskeleton. Many Ras-superfamily small GTPases are components of signaling pathways that link extracellular signals viaFile Size: 2MB. The book includes an overview of how Rho GTPases become activated which is complemented by an extensive Chapter by Darerca Owen and Helen Mott who unravel the beautiful molecular details given to Author: Edward Manser.

GTPases are proteins that act as molecular switches to control biochemical pathways within a cell. This book provides a complete guide to the properties and cellular roles of all the major families of GTPases, including the heterotrimeric G proteins and the small GTPases Ras, Rho, Rab, Arf and : Sigma-Aldrich. Ras-superfamily GTPases bound to GTP are active signaling molecules. The intrinsic GTPase activity of the molecule hydrolyzes GTP to GDP, and GDP-bound forms are inactive. GTPase activating proteins (GAPs) enhance GTPase activity and favor the inactive, GDP-bound state. GTP exchange factors (GEFs) faciltiate exchange of GDP with GTP and thus favor the active, Author: Erik A. Lundquist.


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GTPases (Frontiers in Molecular Biology) by Alan Hall Download PDF EPUB FB2

This book includes several chapters dedicated to the review of various classes of proteins that control the localization and activation state of Rho GTPases.

Additional chapters discuss the wide range of biological functions that are controlled by Rho GTPases, including the organization of the actin cytoskeleton, cell proliferation and cell Format: Hardcover. G proteins are the key regulators for a wide range of cellular processes in animals and plants.

In comparison to animals and yeast, plants have a single Rho-GTPase subfamily called Rho-like GTPases (ROPs). The ROP family of monomeric GTPases has emerged as a versatile and GTPases book regulator in plant. small GTPases—GTP hydrolysis to generate GDP and free inorganic phosphate—inactivates the protein.

Thus selectively altering the catalytic function of a small GTPase without disrupting protein structure locks the protein in the “on” state, while promoting enzymatic function hastens inactivation.

Disruption of protein structure with strongFile Size: 2MB. The GTPase domain is the most highly conserved region. Compared with the Ras superfamily, dynamin has an unusually high GTPase GTPases book and low affinity for GTP.

Thus, it has a low basal GTPase activity which is controlled by self-assembly or lipid binding. Mutations in the GTPase domain such as K44A, K44E, and S45N are defective in GTP binding.

The book's chapters were written by the world's most prominent scientists in this field and cover such topics as the structure and properties of ras proteins, ras function, the ras superfamily in general, and the functional regulation of ras and ras-related : Juan Carlos Lacal, Frank Patrick McCormick.

GTPases are a large family of hydrolase enzymes that can bind and hydrolyze guanosine triphosphate (GTP). The GTP binding and hydrolysis takes place in the highly conserved G domain common to all GTPases. The hydrolysis of the γ phosphate of GTP into guanosine diphosphate (GDP) and Pi, inorganic phosphate, occurs by the SN2 mechanism (see Author: Claire Morgan, Romain Derelle, Sina Stern, Ramona Al-Zoairy, Tasnuva Sarowar, Weiliang Lu.

This volume covers the latest technological advances in the characterization of the biosynthesis and functions of Rab GTPases and their regulation by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs).

The book consists of 28 chapters, and starts with an overview of the Rab GTPase family. Yuren Wang, Kathleen H. Young, in Methods in Enzymology, Single Turnover GTPase Assay. The GTPase activity of the Gα i1 protein is measured by monitoring free, inorganic, radiolabeled phosphate released from bound [γ P]GTP, as described previously (Berman et al., ).Briefly, Gα i1 GTPase activity is initiated by adding 10 mM MgCl 2 and μM GTP.

This volume covers the latest technological advances in the characterization of the biosynthesis and functions of Rab GTPases and their regulation by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs).

The book consists of 28 chapters and starts with an overview of the. The Rho family of GTPases is a family of small (~21 kDa) signaling G proteins, and is a subfamily of the Ras members of the Rho GTPase family have been shown to regulate many aspects of intracellular actin dynamics, and are found in all eukaryotic kingdoms, including yeasts and some plants.

Three members of the family have been studied in detail: Cdc42. About the e-Book Rho GTPases: Molecular Biology in Health and Disease Pdf Rho GTPases control many aspects of cell physiology.

This includes polarity, endo/exocytosis, adhesion, motility, transcriptional activation, cell cycle progression or apoptosis. In view of such pleiotropic activities, Rho-controlled signaling has proven to be of medical.

GTPases (GTP hydrolases, GTP-binding proteins) are enzymes that direct various cellular functions, including signal transduction, protein biosynthesis.

ROP GTPases possess the ability to interact with these multiple regulator and effector molecules that ultimately determines their signaling specificity. Recently, genome wide studies in plants have shown that the Arabidopsis genome enco and rice has nearly 85 small GTPase homologs.

The Rho GTPases in Cancer is the first volume to collect and summarize the current understanding of the Rho GTPases and their involvement in the progression of human cancer.

The critical role of the Rho GTPases, their regulatory proteins, and their effectors in cancer progression has become increasingly evident over the past : Hardcover. GTPases are proteins that act as molecular switches to control biochemical pathways within a cell.

Some GTPases tell a cell to divide and grow, while others cause a cell to move from one location to Read more. Within these genomes can be found GTPases that are not ARFs, ARLs, or SARs, but are clearly close relatives of the GTPases from which the ARF family later arose (Spang et al., ; Klinger et al., ).

Examples of some proteins with domains similar to possible ARF GAPs and GEFs were also found, in some cases fused to the GTPases themselves.

Ras is a family of related proteins which is expressed in all animal cell lineages and organs. All Ras protein family members belong to a class of protein called small GTPase, and are involved in transmitting signals within cells (cellular signal transduction).Ras is the prototypical member of the Ras superfamily of proteins, which are all related in 3D structure and regulate diverse cell InterPro: IPR GTPases represents a successful attempt to gather in a handy, compact book a wealth of information about a field in rapid expansion.

The growing increase in the number of GTPases and their ligands, including hundreds of components of the corresponding signaling pathways, has made it difficult to build up a coherent view of the various GTPase Author: Andrea Parmeggiani.

The binding of GAPs to GTPases stimulates the change of GTPase between its two forms and this is what causes the toggling of the "switch" for the signal transduction chain. GTP-bound is the active form and when it gets hydrolyzed to its inactive GDP-bound form, GTPase is.

This book describes the properties and cellular roles of all the major families of GTPases: the G proteins, Ras, Rho, Rab, Arf, and Ran. All cells use GTPases to regulate the delivery of amino acids to the ribosome during protein synthesis, but eukaryotes, with their complex and compartmentalized environment, have exploited the versatility of.

This e-book provides a timely update on the rapidly developing field and discusses all functional aspects of Ypt/Rab GTPases. The 12 chapters cover well-characterized Ypts/Rabs involved in both exocytic and endocytic pathways as well as newly Cited by: 3. Small GTPases of the Ras superfamily are key regulators of diverse cellular and developmental events, including differentiation, cell division, vesicle transport, nuclear assembly, and control of the cytoskeleton.

The C. elegans genome encodes 56 members of the major Ras GTPase subfamilies, including the Ras/Ral/Rap family, the Rho family, the Rab family, Ran, Author: Erik A. Lundquist.Humans contain more than 20 Rho type GTPases. This volume not only presents a detailed phylogenetic analysis of Rho proteins, but also discusses the possible origins of the human members.

Such an analysis of human Rho GTPases has not previously been book includes an.