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  • 1
    Keywords: Medicine ; Neurosciences ; Physiology / Mathematics ; Consciousness ; Biomedicine ; Biomedicine general ; Neurosciences ; Nonlinear Dynamics ; Physiological, Cellular and Medical Topics ; Cognitive Psychology ; Springer eBooks
    Abstract: This℗ book contains℗ the Proceedings of the 3rd℗ International Conference on Cognitive Neurodynamics held in Japan, June 9-13, 2011. It℗ reviews the progress in this field since℗ the first℗ ICCN℗ in 2007. The participants were treated to an exciting and stimulating conference that left everyone with an enthusiastic℗ vision for the future.℗ The discussed℗ topics℗ in this book include: Neural coding and realistic neural network dynamics, Neural population dynamics, Firing Oscillations and Patterns in Neuronal Networks, Brain imaging, EEG, MEG, Sensory and Motor Dynamics,℗ Global cognitive function, Multi-scalar Neurodynamics - from Physiology to Systems Theory, Neural computing, Emerging Technologies for Brain Computer Interfaces, Neural dynamics of brain disorders
    Pages: : digital.
    ISBN: 9789400747920
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  • 2
    Keywords: Medicine ; Immunology ; Biomedicine ; Immunology ; Springer eBooks
    Description / Table of Contents: High Resolution Crystallographic Analysis of AcrB Using Designed Ankyrin Repeat Proteins (DARPins) -- Crystallographic Analysis of Drug and Inhibitor-Binding Structure of RND-Type Multidrug Exporter AcrB in Physiologically-Relevant Asymmetric Crystals -- Crystallographic Analysis of MATE-Type Multidrug Exporter with Its Inhibitors -- Crystallographic Analysis of the CusBA Heavy-Metal Efflux Complex of℗ Escherichia coli.-℗ Purification of AcrAB-TolC Multidrug Efflux Pump for Cryo-EM Analysis -- NMR Spectroscopy Approach to Study the Structure, Orientation, and Mechanism of the Multidrug Exporter EmrE -- Generation of Conformation-Specific Antibody Fragments for Crystallization of the Multidrug Resistance Transporter MdfA -- Biochemical Reconstitution and Characterization of Multi-Component Drug Efflux Transporters -- Covalently Linked Trimers of RND (Resistance-Nodulation-Division) Efflux Transporters to Study Their Mechanism of Action:℗ Escherichia coli℗ AcrB Multidrug Exporter as an Example -- Determining Ligand Path through a Major Drug Transporter, AcrB, in℗ Escherichia coli.-℗ Molecular Modeling of Multi-Drug Properties of Resistance Nodulation Division (RND) Transporters -- A Transcriptomic Approach to Identify Novel Drug Efflux Pumps in Bacteria -- Regulation of the Expression of Bacterial Multidrug Exporters by Two-Component Signal Transduction Systems -- Study of the Expression of Bacterial Multidrug Efflux Pumps in Anaerobic Conditions -- Identification of a℗ Staphylococcus aureusEfflux Pump Regulator Using a DNA-Protein Affinity Technique -- High Throughput Flow Cytometry Screening of Multidrug Efflux Systems -- Single-Molecule Analysis of Membrane Transporter Activity by Means of a Microsystem -- Large Scale Femtoliter Droplet Array for Single Cell Efflux Assay of Bacteria -- Reconstitution and Transport Analysis of Eukaryotic Transporters in the Post-Genomic Era
    Abstract: This detailed volume utilizes our current understanding of the structural basis of multidrug recognition and multidrug efflux mechanisms to provide protocols involving these vital intrinsic membrane proteins widely distributed in bacteria. Beginning with protocols for the structural analysis of bacterial multidrug exporters, the book continues with sections on biochemical and bioengineering analysis, computational analysis, biomedical approaches, as well as advanced technologies expected to be applied to multidrug efflux transport studies. Written in the highly successful℗ Methods in Molecular Biology℗ series format, chapters include introductions to their respective chapters, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical,℗ Bacterial Multidrug Exporters: Methods and Protocols serves as an ideal guide to this fast moving field of study
    Pages: XII, 355 p. 91 illus., 53 illus. in color. : online resource.
    ISBN: 9781493974542
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  • 3
    Keywords: Medicine ; Human Genetics ; Neurosciences ; Pharmacology ; Metabolic Diseases ; Cell Biology ; Biomedicine ; Human Genetics ; Cell Biology ; Pharmacology/Toxicology ; Neurosciences ; Metabolic Diseases ; Springer eBooks
    Abstract: Most biological pathways, physical and neurological properties are highly conserved between humans and Drosophila and nearly 75% of human disease-causing genes have a functional homologue in Drosophila. This volume provides recent advances in Drosophila models for various human diseases, with each chapter providing a review of studies involving Drosophila models, as well as detailed protocols commonly used in laboratories. Starting with a review of Drosophila’s value as a highly tractable model organism for studying human diseases, subsequent chapters present Drosophila models for specific human diseases. The book provides a useful resource for all scientists who are starting to use the Drosophila model in their studies, and for researchers working in the pharmaceutical industry and using new screening models to develop new medicines for various diseases
    Pages: X, 308 p. 79 illus., 64 illus. in color. : online resource.
    ISBN: 9789811305290
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  • 4
    Keywords: Life sciences ; Immunology ; Toxicology ; Chemistry, Organic ; Biochemistry ; Cytology ; Life sciences ; Biochemistry, general ; Cell Biology ; Organic Chemistry ; Immunology ; Pharmacology/Toxicology ; Springer eBooks
    Description / Table of Contents: Part 1 Glucosyltransferases -- 1 Beta-1,3-glucosyltransferase (B3GALTL) -- 2 Protein O-glucosyltransferases rumi (RUMI) -- 3 UDP-glucose:ceramide glucosyltransferase (UGCG) -- 4 UDP-glucose:glycoprotein glucosyltransferase 1,2 (UGGT1,2) -- Part 2 Galactosyltransferases -- 5 Alpha 1,3-galactosyltransferase 2, pseudogene (A3GALT2P) -- 6 Core 1 beta 3Galactosyltransferase (C1GalT1, T-synthase) and its Specific Molecular Chaperone Cosmc (C1GalT1C1) -- 7 Glycoprotein alpha 1,3-galactosyltransferase 1, pseudogene (GGTA1P) -- 8 UDP-Gal:betaGal beta 1,3-galactosyltransferase polypeptide 6 (B3GALT6) -- 9 UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase, polypeptide 1,2 (B3GALT1,2) -- 10 UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase, polypeptide 4 (B3GALT4) -- 11 UDP-Gal:betaGlcNAc beta 1,3-galactosyltransferase, polypeptide 5 (B3GALT5) -- 12 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1 (B4GALT1) -- 13 UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 2-6; xylosylprotein beta 1,4-galactosyltransferase, polypeptide 7 (galactosyltransferase I) (B4GALT2-7) -- 14 UDP-Gal:ceramide galactosyltransferase (UGT8) -- 15 UDP-Gal:lactosylceramide alpha 1,4-galactosyltransferase (A4GALT) -- Part 3 Mannosyltransferases -- 16 Protein O-mannosyl-transferase 1,2 (POMT1,2) -- Part 4 N-Acetylglucosaminyltransferases -- 17 Alpha-1,4-N-acetylglucosaminyltransferase (A4GNT) -- 18 Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase 3 (GCNT3) -- 19 Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltrasnsferase 1 (GCNT1) (C2GnT-L)and Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltrasnsferase 3 (GCNT4) (C2GnT-T) -- 20 Fringe (UDP-GlcNAc: O-fucosylpeptide ß1,3 N-acetylglucosaminyltransferase) -- 21 Mannosyl (alpha-1,3-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (MGAT1) -- 22 Mannosyl (alpha-1,3-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme A,B (MGAT4A,B) -- 23 Mannosyl (alpha-1,3[6?]-)-glycoprotein beta-1,4-N-acetylglucosaminyltransferase, isozyme C (putative) (MGAT4C) -- 24 Mannosyl (alpha-1,6-)-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (MGAT2) -- 25 Mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase, isozyme B (MGAT5B) -- 26 Mannosyl (alpha-1,6-)-glycoprotein beta-1,6-N-acetyl-glucosaminyltransferase (MGAT5) -- 27 Mannosyl (beta-1,4-)-glycoprotein beta-1,4-N- acetylglucosaminyltransferase (MGAT3); β1,4-N- Acetylglucosaminyltransferase III (GnT-III, GlcNAc-T III) -- 28 N-acetyllactosaminide beta-1,6-N-acetylglucosaminyl-transferase (GCNT2) (IGnT) -- 29 O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase) (OGT) -- 30 Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (POMGNT1) -- 31 UDP-GlcNAc: beta-Gal beta1,3-N-acetylglucosaminyltransferase 6 (B3GNT6) (Core 3 synthase, C3GnT) -- 32 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1 (B3GNT1), i-enzyme (iGnT) -- 33 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 2 (B3GNT2) -- 34 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 3 (B3GNT3) -- 35 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 (B3GNT5, Lc3Cer synthase) -- 36 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 7 (B3GNT7) -- 37 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 8 (B3GNT8) -- Part 5 N-Acetylgalactosaminyltransferases -- 38 Beta-1,4 N-acetylgalactosaminyltransferase 1,2 (B4GALNT1,2) -- 39 Beta1,3-N-Acetylgalactosaminyltransferase 2 (B3GALNT2) -- 40 Beta1,4-N-acetylgalactosaminyltransferase-3 (B4GALNT3) and beta1,4-N-acetylgalactosaminyltransferase-4 (B4GALNT4) -- 41 Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 (GBGT1) -- 42 Histo-blood Group A and B Transferases, Their Gene Structures, and Common O Group Gene Structures -- 43 Histo-blood Group A Variants, O Variants, and Their Alleles -- 44 UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 4 (B3GNT4) -- 45 UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferases (ppGalNAc-Ts) -- Part 6 Fucosyltransferases -- 46 Fucosyltransferase 3. GDP-fucose lactosamine α1,3/4-fucosyltransferase. Lea and Leb histo-blood groups (FUT3, Lewis enzyme) -- 47 Fucosyltransferase 4. GDP-fucose lactosamine α1,3-fucosyltransferase. Myeloid specific (FUT4) -- 48 Fucosyltransferase 5. GDP-fucose lactosamine α3/4-fucosyltransferase (FUT5) -- 49 Fucosyltransferase 6. GDP-fucose lactosamine α3-fucosyltransferase (FUT6) -- 50 Fucosyltransferase 7. GDP-fucose lactosamine α1,3-fucosyltransferase. Sialyl-Lex specific (FUT7) -- 51 Fucosyltransferase 8. GDP-fucose N-glycan core α6-fucosyltransferase (FUT8) -- 52 Fucosyltransferase 9. GDP-fucose lactosamine α1,3-fucosyltransferase. Lex specific (FUT9) -- 53 Fucosyltransferases 1, 2. GDP-fucose galactoside α2-fucosyltransferases. FUT1 or H blood group, FUT2 or ABH secretor status and Sec1 (FUT1, FUT2, Sec1) -- 54 Fucosyltransferases 10, 11. GDP-fucose N-glycan core α1,3-fucosyltransferases (FUT10, FUT11) -- 55 Fucosyltransferases 12, 13: Protein O-fucosyltransferases 1 and 2 (POFUT1, POFUT2) -- Part 7 Sialyltransferases -- 56 ST3 beta-galactoside alpha-2,3-sialyltransferase 1 (ST3GAL1) -- 57 ST3 beta-galactoside alpha-2,3-sialyltransferase 2 (ST3GAL2) -- 58 ST3 beta-galactoside alpha-2,3-sialyltransferase 3 (ST3GAL3) -- 59 ST3 beta-galactoside alpha-2,3-sialyltransferase 4 (ST3GAL4) -- 60 ST3 beta-galactoside alpha-2,3-sialyltransferase 5 (ST3GAL5) -- 61 ST3 beta-galactoside alpha-2,3-sialyltransferase 6 (ST3GAL6) -- 62 ST6 beta-galactoside alpha-2,6-sialyltranferase 1 (ST6GAL1) -- 63 ST6 beta-galactoside alpha-2,6-sialyltranferase 2 (ST6GAL2) -- 64 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 1 (ST6GALNAC1) -- 65 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 2 (ST6GALNAC2) -- 66 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 3 (ST6GALNAC3) -- 67 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 4 (ST6GALNAC4) -- 68 ST6 N-acetylgalactosaminide alpha-2,6-sialyltransferase 5,6 (ST6GALNAC5,6) -- 69 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 1 (ST8SIA1) -- 70 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 2 (ST8SIA2) -- 71 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 3 (ST8SIA3) -- 72 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4 (ST8SIA4) -- 73 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 5 (ST8SIA5) -- 74 ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 6 (ST8SIA6) -- Part 8 Glucuronyltransferases -- 75 Beta-1,3-glucuronyltransferase 1 (glucuronosyltransferase P); beta-1,3-glucuronyltransferase 2 (B3GAT1,2) -- 76 Beta-1,3-glucuronyltransferase 3 (glucuronosyltransferase I) (B3GAT3) -- Part 9 GAG polymerase and related enzymes -- 77 Chondroitin polymerizing factor, chondroitin polymerizing factor 2, chondroitin sulfate synthase 1,3 (CHPF, CHPF2, CHSY1, CHSY3) -- 78 Chondroitin sulfate N-acetylgalactosaminyltransferase 1,2 (CSGALNACT1,2) -- 79 Dermatan sulfate epimerases (DSE, DSEL) -- 80 Exostoses (multiple)-like 1-3 (EXTL1-3) -- 81 Exostosin 1,2(EXT1,2) -- 82 Heparin-heparansulfate related GlcA C5-epimerase -- 83 Hyaluronan synthase 1-3 (HAS1-3) -- 84 Xylosyltransferase I,II (XYLT1,2) -- Part 10 Sulfotransferases -- 85 Carbohydrate sulfotransferase 10 (CHST10) -- 86 Carbohydrate (chondroitin 4) sulfotransferase 11-13 (CHST11-13) -- 87 Carbohydrate (chondroitin 6) sulfotransferase 3; carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 7 (CHST3,7) -- 88 Carbohydrate (keratan sulfate Gal-6) sulfotransferase 1 (CHST1) -- 89 Carbohydrate (N-acetylgalactosamine 4-0) sulfotransferase 14 (CHST14) -- 90 Carbohydrate (N-acetylgalactosamine 4-sulfate 6-O) sulfotransferase 15 (CHST15) -- 91 Carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 4 (CHST4) -- 92 Carbohydrate (N-acetylglucosamine 6-O) sulfotransferase 5 and 6 (CHST5,6) -- 93 Carbohydrate (N-acetylglucosamine-6-O) sulfotransferase 2(CHST2) -- 94 Galactose-3-O-sulfotransferase 1-4 (GAL3ST1-4) -- 95 Heparan sulfate 2-O-sulfotransferase (HS2ST) -- 96 Heparan sulfate (glucosamine) 3-O-sulfotransferase 1-6 (HS3ST1-6) -- 97 Heparan-sulfate 6-O-sulfotransferase 1-3 (HS6ST1-3) -- 98 N-Acetylgalactosamine-4-sulfotransferase-1 (GalNAc-4-ST1, CHST8) and N-Acetylgalactosamine-4-sulfotransferase-2 (GalNAc-4-ST2, CHST9) -- 99 N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 1 (NDST1) -- 100 N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 2 (NDST2) -- 101 N-deacetylase/N-sulfotransferase (heparan glucosaminyl) 3,4 (NDST3,4) -- 102 Uronyl-2-sulfotransferase (UST) -- Part 11 Glycosyltransferase-like proteins (inplicated in alpha-dystrogly) -- 103 Fukutin and fukutin-related protein (FKRP) -- 104 Like-glycosyltransferase; glycosyltransferase-like 1B (LARGE, GYLTL1B) -- Part 12 GPI anchor biosynthesis -- 105 Glycosylp
    Abstract: This handbook, now in a new, second edition, is an essential resource for scientists with an interest in the role of glycosyltransferases and related genes involved in the biosynthesis of glycoproteins, glycolipids, and proteoglycans. The first edition of the Handbook of Glycosyltransferases and Related Genes, published in 2002, contained descriptions of more than 100 mammalian genes by over 100 scientists who originally isolated and/or cloned these genes. Since then, there has been a growing body of evidence concerning the roles of glycosyltransferases, and additional glycosyltransferases have been identified. Now more than 200 glycosyltransferases have been isolated from mammalian tissue, corresponding to approximately 1–2% of the total human genome. Some have been found to be involved in development and reproduction, signal transduction, cell death, higher nervous functioning, immunity, and other important biological processes. Glycosyltransferases have also been implicated in the development of lifestyle diseases such as diabetes, cancer, chronic obstructive lung disease (COPD), neuromuscular diseases, and infectious diseases. A functional glycomics approach using gene targeting in mice and analytical methods utilizing glycan arrays, lectin arrays, HPLC, and mass spectrometry identified the target glycoprotein(s) on which glycans are attached by the catalytic reaction of glycosyltransferases. Most of the target proteins have been shown to be cell surface membrane proteins such as growth factor receptors and transporters. The three-dimensional structures of some glycosyltransferases have also been characterized, making it possible to classify them into retaining and inverting enzymes. Such structural information is also included in this invaluable new edition
    Pages: XXXVIII, 1707 p. 205 illus., 75 illus. in color. eReference. : online resource.
    Edition: 2nd ed. 2014.
    ISBN: 9784431542407
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  • 5
    Keywords: Life sciences ; Plant science ; Botany ; Life sciences ; Plant Sciences ; Springer eBooks
    Description / Table of Contents: Master Regulatory Transcription Factors in Plant Development: A Blooming Perspective -- Application of CRISPR/Cas to Understand Cis- and Trans-Regulatory Elements in Plants -- The Long-Term €˜Ín Naturမ Study Sites of Arabidopsis halleri for Plant Transcription and Epigenetic Modification Analyses in Natural Environments -- Generation of Inducible Transgenic Lines of Arabidopsis Transcription Factors Regulated by MicroRNAs -- A Specific Knockdown of Transcription Factor Activities in Arabidopsis -- Using CRISPR/Cas9 System to Introduce Targeted Mutation in Arabidopsis -- CRISPR/Cas9-Based Genome Editing of Transcription Factor Genes in Marchantia polymorpha -- Cell-Type-Specific Promoter Identification Using Enhancer Trap Lines -- Isolation of Arabidopsis Palisade and Spongy Mesophyll Cells -- Ectopic Vascular Induction in Arabidopsis Cotyledons for Sequential Analysis of Phloem Differentiation -- High Impact Gene Discovery: Simple Strand Specific mRNA Library Construction and Differential Regulatory Analysis Based on Gene Co-Expression Network -- Laser Capture Micro-Dissection Coupled to RNA Sequencing: A Powerful Approach Applied to the Model Legume Medicago truncatula in Interaction with Sinorhizobium meliloti -- nanoCAGE-XL: An Approach to High-Confidence Transcription Start Site Sequencing -- Genome-Wide TSS Identification in Maize -- Three-Dimensional Multiphoton Imaging of Transcription Factor by ClearSee -- Two-Color In Situ Hybridization: A Technique for Simultaneous Detection of Transcripts from Different Loci -- Gene Expression and Transcription Factor Binding Tests Using Mutated-Promoter Reporter Lines -- Rapid and Quantitative CELD Assay to Measure the Specificity of Transcription Factor-DNA Binding Interactions and Identify cis-Elements -- In Situ Proximity Ligation Assay to Detect the Interaction between Plant Transcription Factors and Other Regulatory Proteins -- Cell-Free Protein Synthesis of Plant Transcription Factors -- Application of MNase-Seq in the Global Mapping of Nucleosome Positioning in Plants -- Genome-Wide Mapping of DNase I Hypersensitive Sites in Tomato -- Genome-Wide Identification of Chromatin Domains Anchored at the Nuclear Periphery in Plants
    Abstract: This detailed book provides general protocols and technologies that plant biologists worldwide often utilize for the purpose of accelerating research progress in the field of plant transcription factors. Beginning with a brief introduction, the volume continues by exploring methods in the preparation of plant materials, detection of expression levels, interaction tests, and chromatin analyses. Written for the highly successful Methods in Molecular Biology series, chapters include introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Authoritative and practical, Plant Transcription Factors: Methods and Protocols aims to answer a wide range of questions related to transcription factors commonly raised by plant biologists
    Pages: XII, 396 p. 81 illus., 58 illus. in color. : online resource.
    ISBN: 9781493986576
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  • 6
    Keywords: Biochemistry ; Biochemistry, general ; Biological and Medical Physics, Biophysics ; Springer eBooks
    Description / Table of Contents: Preface -- Chapter 1: The effect of N-glycans on glycoprotein folding and protein dynamics -- Chapter 2: Synthesis of glycosylated metal complexes for probing carbohydrate-carbohydrate interactions -- Chapter 3: Unraveling of lipid raft organization in cell plasma membranes by single-molecule imaging of ganglioside probes -- Chapter 4: MALDI mass spectrometry imaging of N-linked glycans in tissues -- Chapter 5: Modern-omics technologies for isobaric glycan and glycoconjugate structure determination -- Chapter 6: Synchrotron-radiation vacuum-ultraviolet circular-dichroism spectroscopy for characterizing the structure of saccharides -- Chapter 7: Biophysical analyses for probing glycan-protein interactions -- Chapter 8: Structural aspects of ER glycoprotein quality-control system mediated by glucose tagging -- Chapter 9: Structural basis of protein Asn-glycosylation by oligosaccharyltransferases -- Chapter 10: Visualization of functional structure and kinetic dynamics of cellulases -- Chapter 11: Structure and dynamics of immunoglobulin G glycoproteins -- Chapter 12: Biophysical Approaches to Solve the Structures of the Complex Glycan Shield of Chloroviruses -- Chapter 13: Quantifying weak glycan-protein interactions using a Biolayer Interferometry competition assay: Applications to ECL lectin and X-31 influenza hemagglutinin
    Abstract: This book presents state of the art biophysical approaches to issues in glycobiology that have cutting-edge applications. Despite the importance of glycosylation, the complexity, heterogeneity, and flexibility of the glycans have inhibited their study. Each chapter in this book explains very recent significant advances in biophysical approaches through the use of techniques such as NMR spectroscopy, mass spectrometry, single-molecule imaging, X-ray crystallography, high-speed atomic force microscopy, and computational simulation and their integrative application. Concrete examples are provided of the value of these techniques in addressing key problems in the field. In addition, significant functional glycobiological issues are considered. For example, glycolipids can form dynamic clusters on cell membranes and provide platforms for molecules involved in cell recognition and subsequent signal transduction. The detailed delineation of these molecular systems is discussed, revealing their structural complexity and ability to assemble transiently. This timely book will be of value for graduate students and postdocs interested in frontier topics in glycoscience and also for senior bio-researchers in academic and industrial fields
    Pages: XIII, 277 p. 110 illus., 74 illus. in color. : online resource.
    ISBN: 9789811321580
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  • 7
    ISSN: 0304-8853
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 8
    ISSN: 0304-8853
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Physics
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 1432-1238
    Keywords: Inferior vena cava pressure ; Arterial ketone body ratio ; Hepatic congestion ; Liver viability ; Fontan operation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Objective Abnormally elevated central venous pressure is considered to be an etiological factor in the onset of acute hepatic failure following modified Fontan operation. This paper hypothesises that an increase in inferior vena cava pressure (IVCP) after such an operation has adverse effects on hepatic energy status. Design Various degrees of venous hypertension were produced in 10 mongrel dogs by clamping the thoracic IVC with an active veno-venous shunt and varying its flow rate from 60–2.5 ml/min/kg. Arterial ketone body ratio (KBR), reflecting the hepatic mitochondrial redox state, was measured as an index of hepatic energy status.Measurements and results: The lower the flow rates of the shunt, the higher the pressures of IVC and portal vein, while systolic blood pressure was maintained above 100 mmHg. CO significantly decreased when the pump speed was less than 30 ml/min/kg. KBR showed a negative correlation to IVCP as well as a positive correlation to portal blood flow (p〈0.05). Conclusion From the simple regression line obtained between IVCP and KBR, it was determined that an upper safety limit of IVCP may lie at about 27 cmH2O (20.5 mmHg), and that a IVCP of 35 cmH2O (26.6 mmHg) seems to be the critical level for maintaining liver viability.
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 1433-0350
    Keywords: Akinetic mutism ; Hyperphagia ; Interlaminal nucleus of thalamus ; Dorsomedial nucleus of hypothalamus ; Childhood head injury
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A case of childhood post-traumatic akinetic mutism is presented. The patient showed a hyperphagic condition while recovering from akinetic mutism. He had lesions in the left interlaminal nucleus of the thalamus, right globus pallidus, and right dorsomedial nucleus of the hypothalamus. Laboratory data indicated slightly disturbed hypothalamic functions. In general, akinetic mutism can be seen with bilateral destructive lesions, while hyperphagia may occur after destruction of dorsomedial hypothalamic nucleus, but it is very rare. This is the first reported case of akinetic mutism caused by a unilateral lesion.
    Type of Medium: Electronic Resource
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