ISSN (Print): 1389-2037
ISSN (Online): 1875-5550
Volume 20, 12 Issues, 2019
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ISSN (Print): 1389-2037
ISSN (Online): 1875-5550
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Ben M. Dunn Department of Biochemistry and Molecular Biology
University of Florida, College of Medicine,
P.O. Box 100245, Gainesville Florida, FL 32610-0245 USA
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Editor(s): Michel Goldberg
eISBN: 978-1-60805-171-7, 2010
ISBN: 978-1-60805-606-4 ISSN: 2589-3076 (Print) ISSN: 2210-2841 (Online)
This volume is the 1st in a series of Ebooks that bridges the gap between advances in science and clinical practice in odontology. Recent advances in biology, materials science and tissue engineering are increasingly viewed as being of enormous clinical potential. Stem cell research has opened up the possibility of reconstructing teeth from the association of epithelial and mesanchymal embryonic or adult cells, as an exciting alternative to metal implants. This Ebook will examine the multifunctional nature of a group of proteins known as the amelogenins. Latest studies indicate that this protein regulates the initiation and growth of hydroxyapatite crystals during the mineralization of enamel. In addition, amelogenins organize enamel rods during tooth development, and also aid in the development of cementum by directing cells that form the cementum to the root surface of the teeth. The aim of this book is to serve as a bridge between basic biology and biomaterial sciences, and to inform clinicians about the implications of recent advances within these fields for clinical practice.
Author(s): Joseph Z. Zaretsky and Daniel H. Wreschner
eISBN: 978-1-60805-454-1, 2013
ISBN: 978-1-60805-516-6 ISSN: 2589-2983 (Print) ISSN: 2214-0824 (Online)
Mucins are glycoproteins that are expressed in cells of different types and fulfill multiple functions that determine participation of these proteins in such processes as signal transduction, regulation of gene expression, cell proliferation, embryogenesis, cell differentiation, immunity, apoptosis and cancer development. This E-book series on mucins presents critical reviews on modern data concerning structures and functions of mucins, their roles in cell physiology and pathology as well as molecular aspects of therapy of mucin-associated diseases. Mucins are represented by two types of molecules: secreted mucins and membrane-bound (receptor) mucins. This e-book series represents a unique attempt to describe the molecular nature of mucin multifunctionality in separate volumes. Chapters in each volume demonstrate the central role of mucins as connectors and regulators of different signaling pathways and their participation metastatic processes. Clinical aspects of mucins, such as their role as diagnostic markers as well as possible applications in mucin-based immuno- and gene-therapies are also discussed.
This is the first volume of the series. This volume introduces readers to the general properties of mucins, followed by chapters on specific variants of gel-forming and soluble mucins. The volume concludes with information on the functions of secreted mucins.
Editor(s): Ben Dunn
eISBN: 978-1-60805-862-4, 2014
ISBN: 978-1-60805-863-1 ISSN: 2213-9877 (Print)
Frontiers in Protein and Peptide Sciences is a book series focused on leading-edge research on the structure, physical properties, and functions of proteins and peptides. Authors of contributions in this series have updated their work with new experimental data and references following their initial research. Each volume highlights a number of important topics in current research in the field of protein and peptide chemistry and molecular biology, including membrane proteins and their interactions with ligands, computational methods, and proteins in disease and biotechnology. The series is essential reading for protein chemists and researchers seeking the latest information about protein and peptide research.
Author(s): Carlos Polanco
eISBN: 978-1-68108-269-1, 2016
Polarity is a physico-chemical property that characterizes the electromagnetic stability of a protein and can be used to predict its plausible pathogenic action. For this reason, polarity is regarded as a major factor in most mathematical-computational algorithms that seek to characterize peptides and proteins. The Polarity Index Method makes it possible to reproduce the main classification of peptide proteins found in different databases, with a high degree of discriminative efficiency.
Polarity Index In Proteins is a brief monograph that explains the foundations of the polarity index method and presents examples of the application of this method for identifying the structural and functional relationships of different types of proteins (including cell penetrating peptides and natively unfolded proteins).
The monograph is divided into sections that cover basic protein biochemistry, the computational mathematical foundations of the polarity index method, the application of the method on different protein structures, and the evaluation of the results of famous experiments on biogenesis (Miller & Urey, Fox & Harada, Rode) by the same method.
Polarity Index In Proteins serves as an essential handbook for students and researchers in the field of bioinformatics, proteomics as well as for studies on the role of proteins in the origin of life.
Editor(s): Mario D. Galigniana
eISBN: 978-1-68108-615-6, 2018
ISBN: 978-1-68108-616-3 ISSN: 2589-4366 (Print) ISSN: 2589-4374 (Online)
The book provides an updated panorama of the functional relevance of molecular chaperones in the proper folding of client factors, protein-protein interactions, the regulation of key biological functions, the development of ligand-based structural complexes and the consequent pharmacological or biotechnological applications of these processes. The involvement of molecular chaperones in several processes ranging from regulation of transcription factors and protein-protein interactions in bacteria to proteostasis, signaling pathways and cancer are also addressed. The book is an essential consulting tool for researchers, working professionals in academia or industry, and students of all levels who wish to obtain the most relevant and updated information currently available about protein folding and chaperones.