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  • 1
    Online Resource
    Online Resource
    Milton :Taylor & Francis Group,
    Keywords: Chemometrics. ; Electronic books.
    Description / Table of Contents: Presenting a clear bridge between theory and application, this volume provides a thorough description of the mechanism of support vector machines (SVMs) from the point of view of chemists and biologists. Topics discussed include elements and algorithms of support vector classification (SVC) machines and support vector regression machines (SVR), the kernel function for solving nonlinear problems, ensemble learning of SVMs, applications of SVMs to near-infrared data, SVMs and quantitative structure-activity/property relationships (QSAR/QSPR), quality control of traditional Chinese medicine by means of the chromatography fingerprint technique, and the use of SVMS in exploring the biological data produced in OMICS study.
    Type of Medium: Online Resource
    Pages: 1 online resource (206 pages)
    Edition: 1st ed.
    ISBN: 9781439821282
    DDC: 542/.85
    Language: English
    Note: Front Cover -- Contents -- Preface -- Author Biographies -- Chapter 1: Overview of support vector machines -- Chapter 2: Support vector machines for classification and regression -- Chapter 3: Kernel methods -- Chapter 4: Ensemble learning of support vector machines -- Chapter 5: Support vector machines applied to near-infrared spectroscopy -- Chapter 6: Support vector machines and QSAR/QSPR -- Chapter 7: Support vector machines applied to traditional Chinese medicine -- Chapter 8: Support vector machines applied to OMICS study -- Back Cover.
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  • 2
    Online Resource
    Online Resource
    Hauppauge :Nova Science Publishers, Incorporated,
    Keywords: Retinoids. ; Tretinoin. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (216 pages)
    Edition: 1st ed.
    ISBN: 9781621006565
    Series Statement: Microbiology Research Advances
    DDC: 615.5
    Language: English
    Note: Intro -- RETINOIC ACIDSTRUCTURE, MECHANISMS AND ROLES IN DISEASE -- MICROBIOLOGY RESEARCH ADVANCES -- CELL BIOLOGY RESEARCH PROGRESS -- RETINOIC ACIDSTRUCTURE, MECHANISMS AND ROLES IN DISEASE -- Library of Congress Cataloging-in-Publication Data -- CONTENTS -- PREFACE -- CHAPTER 1. RETINOID SIGNALING IN MAMMALIAN INNER EAR DEVELOPMENT -- ABSTRACT -- INTRODUCTION -- TRANSDUCTION OF THE RA SIGNAL -- Expression Domains of Retinoid Receptors in the Developing Inner Ear -- Cellular Retinoid Binding Proteins -- MOLECULAR CONTROL OF RA ACTIVITY IN THE EMBRYONIC INNER EAR -- Alcohol and Retinol Dehydrogenases -- Retinaldehyde Dehydrogenases -- Cyp26 Enzymes -- REQUIREMENT FOR OPTIMAL RA CONCENTRATIONS DURING INNER EAR DEVELOPMENT -- Effects of Retinoid Deficiency in Inner Ear Development -- Effects of Excess Retinoids in Inner Ear Development -- MODES OF RA ACTION ON THE INNER EAR -- RA Signaling and Hindbrain Segmentation -- RA Signaling from Somitic Mesoderm -- RA Signaling Intrinsic to the Otocyst -- SIGNALING PATHWAYS UNDER RA CONTROL -- Fibroblast Growth Factor Signaling -- Dlx5/6signaling -- Transforming Growth Factor-Beta Signaling -- Bone Morphogenetic Protein Signaling -- Tbx1signaling -- RA AND SPECIFICATION OF SENSORY ORGAN DEVELOPMENT -- CONCLUSION -- REFERENCES -- CHAPTER 2. ARE NUCLEAR RECEPTORS FOR RETINOIDS INVOLVED IN THE CONTROL OF THE EXPRESSION AND ACTIVITY OF P-GLYCOPROTEIN? -- ABSTRACT -- 1. INTRODUCTION -- 2. NUCLEAR RETINOID/REXINOID RECEPTORS -- 3. NUCLEAR RETINOID AND REXINOID RECEPTORS IN SELECTED MALIGNANCIES -- 4. P-GLYCOPROTEIN-MEDIATED MDR -- 5. MOLECULAR PROPERTIES AND THE REGULATION OF THEEXPRESSION OF P-GLYCOPROTEIN -- 6. INTERPLAY BETWEEN P-GP TRANSCRIPTIONAL CONTROL AND NUCLEAR RECEPTORS FOR RETINOIDS -- 7. POSSIBLE MECHANISM OF ALL-TRANS RETINOIC ACID-INDUCED DOWNREGULATION OF P-GP -- CONCLUSION -- ACKNOWLEDGMENTS. , REFERENCES -- CHAPTER 3. MRNA DIVERSITY OF GENES BY ALTERNATIVE SPLICING DURING NEURONAL DIFFERENTIATION OF NT2 PLURIPOTENTIAL HUMAN EMBRYONAL CARCINOMA CELLS BY ALL-TRANS RETINOIC ACID -- ABSTRACT -- ABBREVIATIONS -- INTRODUCTION -- OVERVIEW OF RA-INDUCED ALTERATION IN EXPRESSION OF GENES IN NT2 CELLS -- MRNA DIVERSITY OF RA-RESPONSIVE GENES SELECTED EXPRESSION PROFILES -- Examples of Alt. N-Term Genes -- Examples of Alt. Cassette-Exon Genes -- Examples of Alt. C-Term Genes -- MRNA DIVERSITY OF GENES CONTAINING MULTIPLE TSSS FROM CLONED SPLICING VARIANT CDNAS -- Examples of Alt. N-Term Genes -- ALTERNATIVE SPLICING VARIANTS AND THE USEFULNESS FOR GENE FUNCTIONAL ANALYSES -- CONCLUSION -- ACKNOWLEDGMENTS -- REFERENCES -- CHAPTER 4. RETINOIC ACID SIGNALING AND IMMUNOTHERAPY OF CANCER -- ABSTRACT -- REFERENCES -- CHAPTER 5. RETINOIC ACID INDUCIBLE-1 GENE (RAI1) AND CLINICAL SUBTYPES OF SCHIZOPHRENIA -- ABSTRACT -- INTRODUCTION -- METHODS -- Subjects -- DNA Analysis -- Statistical Analysis -- RESULTS -- DISCUSSION -- ACKNOWLEDGMENTS -- REFERENCES -- DATABASE -- CHAPTER 6. TRETINOIN-CYCLODEXTRIN COMPLEX IN SKIN REJUVENATION THERAPY -- ABSTRACT -- INTRODUCTION -- 1. MECHANISMS OF AGING SKIN AND TRETINOIN TREATMENT -- 1.1. Retinoic Acid in the Body -- 1.2. Mechanisms of Skin Aging -- 1.3. Mechanism of Biological Action of Tretinoin -- 1.4. Clinical Use of Retinoic Acid for Acne, Pigmentation, Wrinkles, and Other Diseases -- 1.5. Clinical Use of Tretinoin for Photoaging Therapy -- 1.6. Adverse Effects of Tretinoin Therapy and Its Countermeasures -- 2. STRUCTURE OF TRETINOIN/CYCLODEXTRIN COMPLEX -- 2.1. Cyclodextrin Properties -- 2.2. Hydroxypropyl-CyDs and Other Modified CyDs -- 2.3. Properties and Structure of the ATRA/HP-β-CyD Complex in Water -- 3. DEVELOPMENT OF CYCLODEXTIN-INCLUSION TYPE TRETINOIN IN CLINICAL USE. , 3.1. Preparation of ATRA/HP-β-CyD Moisturizing Base -- 3.2. Clinical Use of Tretinoin/HP-β-CyD Complex -- 3.2.1. Comparative Evaluation of ATRA and the ATRA/HP-β-CyD Complex -- 3.2.2. A Case of Wrinkle Treatment -- 3.2.3. A Case of Pigmentation Treatment -- 3.2.4. Effects of Cyclodextrin-Inclusion Tretinoin after Long-Term Use -- 3.3. Potential of the ATRA/HP-β-CyD Complex in Aesthetic Plastic Medicine -- CONCLUSION -- ACKNOWLEDGMENTS -- REFERENCES -- CHAPTER 7. RETINOIC ACID: AN OLD COMPOUND WITH A POTENTIAL FOR FUTURE USE IN PERSONALIZED MOLECULAR MEDICINE -- CANCER CELLS TAKE UP THE RA AGENT -- TUMOR XENOGRAFTS TAKE UP THE RA AGENT -- REAL-TIME MONITORING AGENT DISTRIBUTION IN THE WHOLE BODY -- DETERMINING THE BIOLOGICALLY EFFECTIVE DOSE -- PREDICTION OF SYSTEMIC AND/OR ORGAN-SPECIFIC TOXICITY -- CONCLUSION -- ACKNOWLEDGMENTS -- REFERENCES -- CHAPTER 8. RETINOL/VITAMIN A SIGNALING AND SELF RENEWAL OF STEM CELLS -- ABSTRACT -- INTRODUCTION -- RETINOL IS METABOLIZED TO RETINOIC ACID IN NORMAL CELL -- RETINOL SIGNALING AND SELF RENEWAL OF ES CELLS -- ES CELLS LACK THE MACHINERY TO METABOLIZE RETINOL INTO RETINOIC ACID -- CONCLUSION -- REFERENCES -- CHAPTER 9. RETINOIC ACID REGULATES SOX2 EXPRESSION DURING NEURONAL AND GLIAL DIFFERENTIATION IN MOUSE P19 CELLS -- ABSTRACT -- INTRODUCTION -- MATERIALS AND METHODS -- RESULTS AND DISCUSSION -- REFERENCES -- CHAPTER 10. ALTERNATIVES TO REDUCE THE TOPICAL RETINOIC ACID-INDUCED SKIN IRRITATION -- ABSTRACT -- 1. INTRODUCTION -- 2. RA PRECURSORS -- 2.1. Retinol -- 2.2. Retinaldehyde -- 3. ESTERS OF RA -- 3.1. Retinyl Retinoate -- 3.2. Picolinic Acid-Substituted Ester of 9-cis Retinoic Acid (MDI 301) -- 4. NOVEL RA DELIVERY SYSTEMS -- 4.1. Polymeric Microspheres -- 4.2. Lipid Nanocarriers -- CONCLUSION -- REFERENCES -- INDEX.
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  • 3
    Online Resource
    Online Resource
    La Vergne :Royal Society of Chemistry, The,
    Keywords: Biochemistry. ; Electronic books.
    Description / Table of Contents: Written by a team of experts, this book bridges the gap between the DNA- and RNA- views of protein-nucleic acid recognition which are often treated as separate fields.
    Type of Medium: Online Resource
    Pages: 1 online resource (416 pages)
    Edition: 1st ed.
    ISBN: 9781847558268
    Series Statement: Issn Series
    DDC: 572.86
    Language: English
    Note: Protein-Nucleic Acid Interactions -- Contents -- Chapter 1 Introduction -- 1.1 Overview -- 1.2 Fundamentals of DNA and RNA Structure -- 1.2.1 Stabilizing Forces -- 1.2.2 Chemical Differences between DNA and RNA -- 1.2.3 Canonical A- and B-form Helices -- 1.2.4 Deviation is the Norm -- 1.2.5 Bending and Supercoiling DNA -- 1.2.6 Folded RNA and Noncanonical DNA -- 1.3 Principles of Recognition -- 1.3.1 Forces that Contribute to Complex Formation -- 1.3.2 Site Recognition Overview -- 1.3.3 Recognizing Duplex DNA via Direct and Indirect Readout -- 1.3.4 Recognizing Single-stranded Nucleic Acids -- 1.3.5 Recognizing Folded RNAs -- 1.3.6 Recognizing Noncanonical DNA Structures -- 1.3.7 Conformational Rearrangements -- 1.4 Future Directions -- References -- Chapter 2 Role of Water and Effects of Small Ions in Site-specific Protein-DNA Interactions -- 2.1 Introduction -- 2.2 Affinity and Specificity -- 2.3 Macromolecular Hydration Influences ΔH°, ΔS° and ΔC°P -- 2.4 Water Release Attending Protein-DNA Association -- 2.5 Retained Water Molecules Contribute to Affinity and Specificity -- 2.6 Thermodynamic Effects of Retained Water -- 2.7 Overview of Small Ion Effects on Protein-DNA Interactions -- 2.8 Multiple Physical Phenomena Associated with Salt Dependence -- 2.9 Cation Release Favors Protein-DNA Association -- 2.10 Selective Effects of Anions on Protein-DNA Binding -- 2.11 Divalent Cation Binding at Active Sites Relieves Electrostatic Strain -- 2.12 Ion Effects and Cosolute Effects are Mechanistically Independent -- 2.13 Comparison with Nonspecific Binding: How Water and Ions Affect Specificity -- 2.14 Conclusions -- Acknowledgements -- References -- Chapter 3 Structural Basis for Sequence-specific DNA Recognition by Transcription Factors and their Complexes -- 3.1 Introduction -- 3.2 Transcriptional Regulators that Bind Core DNA Elements. , 3.2.1 Helix-turn-helix and Winged Helix-turn-helix -- 3.2.2 Basic Leucine-zipper and Basic Helix-loop-helix -- 3.2.3 Zinc-binding Domains that Bind as Monomeric Units -- 3.2.4 DNA Recognition by β-Ribbons -- 3.2.5 Immunoglobulin Fold -- 3.2.6 HMG Domain -- 3.3 Transcriptional Regulators that Bind as Dimers to two DNA Half Sites with Different Spacing and Polarity -- 3.3.1 Zn2Cys6 Binuclear Cluster -- 3.3.2 Nuclear Receptors -- 3.4 Transcription Regulatory Complexes that use a Combination of Different DNA-binding Motifs -- 3.4.1 Combinatorial DNA Interactions -- 3.4.2 ETS Family Ternary Complexes -- 3.4.3 NFAT/Fos-Jun/DNA Quaternary Complex -- 3.5 Conclusions -- References -- Chapter 4 Indirect Readout of DNA Sequence by Proteins -- 4.1 Introduction -- 4.1.1 DNA Sequence Recognition: A Historical Perspective -- 4.2 Indirect Readout -- 4.2.1 Direct vs. Indirect Readout -- 4.2.2 Language of Indirect Readout: DNA Geometry -- 4.2.3 Sequence-dependent Polymorphisms of B-DNA -- 4.2.3.1 Base Stacking -- 4.2.3.2 Hydrogen Bonding -- 4.2.3.3 Steric Repulsion -- 4.2.3.4 DNA Bending -- 4.2.4 Indirect Readout: A Universal Feature of Protein-DNA Interactions -- 4.3 DNA Sequence Recognition by CAP -- 4.3.1 Direct Readout by CAP -- 4.3.2 Indirect Readout by CAP -- 4.3.2.1 Conformation and Flexibility of the DNA Site for CAP -- 4.3.2.2 Indirect Readout at Positions 1-2 -- 4.3.2.3 Indirect Readout at Position 6 -- 4.3.2.4 Comparison with Other Protein-induced Positive Roll Deformations -- 4.3.3 DNA Bending vs. DNA Kinking - A Dynamic Duo? -- 4.4 Conclusions -- Acknowledgements -- References -- Chapter 5 Single-stranded Nucleic Acid (SSNA)-binding Proteins -- 5.1 Introduction -- 5.2 Basic Elements -- 5.2.1 Interaction Types -- 5.2.1.1 Salt Bridges and Electrostatics -- 5.2.1.2 Stacking Interactions -- 5.2.1.3 Steric Packing and van der Waals Interactions. , 5.2.1.4 Hydrogen Bonding -- 5.2.2 Folds, Evolution and Function -- 5.2.2.1 OB-fold -- 5.2.2.2 Sm-fold -- 5.2.2.3 RRM -- 5.2.2.4 KH -- 5.2.2.5 Others: Pumilio, TRAP and Whirly -- 5.3 Emergent Properties -- 5.3.1 Molecular Recognition: Specificity, Adaptability and Degeneracy -- 5.3.1.1 Specific yet Adaptable Recognition by Modular Puf Proteins -- 5.3.1.2 A "Hot-spot" for Recognition of Telomere DNA by Cdc13 -- 5.3.1.3 "Nucleotide Shuffling" and TEBP-α/β -- 5.3.1.4 Degeneracy in Splicing Branch Site Identification -- 5.3.2 Cooperativity -- 5.3.2.1 SSB and Multiple Cooperativity Modes -- 5.3.2.2 Anti-cooperativity and TEBP-α -- 5.3.2.3 Positive Heterotypic Cooperativity at Telomere Ends -- 5.3.3 Allostery -- 5.3.3.1 Small Molecule Effectors and SSNA-binding -- 5.3.3.2 Proteins as Allosteric Effectors for Binding and Release of SSNA -- 5.4 Conclusion and Perspective -- Acknowledgements -- References -- Chapter 6 DNA Junctions and their Interaction with Resolving Enzymes -- 6.1 The Four-way Junction in Genetic Recombination -- 6.2 Structure and Dynamics of DNA Junctions -- 6.2.1 Dynamics of the Four-way Junction -- 6.2.2 Metal Ions and the Electrostatics of the Four-way Junction -- 6.2.3 Branch Migration -- 6.2.4 Comparison with Four-way RNA Junctions -- 6.3 Proteins that Interact with DNA Junctions -- 6.4 Junction-resolving Enzymes -- 6.4.1 Occurrence of the Junction-resolving Enzymes -- 6.4.2 Phylogeny -- 6.4.3 Junction-resolving Enzymes are Dimeric -- 6.4.4 Structures of the Junction-resolving Enzymes -- 6.5 Molecular Recognition and Distortion of the Structure of DNA Junctions by Resolving Enzymes -- 6.5.1 Sequence Specificity of the Junction-resolving Enzymes -- 6.5.2 Structural Distortion of DNA Junctions by the Junction-resolving Enzymes -- 6.5.3 Coordination of the Resolution Process -- 6.6 T7 Endonuclease I -- 6.6.1 Biochemistry of Endonuclease I. , 6.6.2 Structure of Endonuclease I -- 6.6.3 The Active Site -- 6.6.4 Catalysis of Phosphodiester Bond Hydrolysis -- 6.6.5 Interaction between Endonuclease I and DNA Junctions -- 6.7 In Conclusion -- Acknowledgements -- References -- Chapter 7 RNA-protein Interactions in Ribonucleoprotein Particles and Ribonucleases -- 7.1 Introduction -- 7.2 Experimental Methods used to Determine RNA-protein Complex Structures -- 7.3 RNA-protein Interactions in Ribonucleoprotein Particles -- 7.3.1 Ribosome -- 7.3.2 RNAi Complexes -- 7.3.3 Signal Recognition Particle -- 7.3.4 s(no)RNPs -- 7.3.5 RNA Editing Complexes -- 7.4 RNA-protein Interactions in Ribonucleases -- 7.4.1 RNase E -- 7.4.2 RNase II -- 7.4.3 RNase III -- 7.4.4 Restrictocin -- 7.4.5 RNA Splicing Endonucleases -- 7.4.6 tRNase Z -- 7.5 Concluding Remarks -- Acknowledgements -- References -- Chapter 8 Bending and Compaction of DNA by Proteins -- 8.1 Introduction -- 8.2 Forces Controlling DNA Rigidity -- 8.2.1 DNA Elasticity and the Influence of DNA Sequence -- 8.2.2 Base Stacking Primarily Controls Helix Rigidity -- 8.2.3 Electrostatic Forces Modulate DNA Bending -- 8.3 Bending of DNA at High Resolution -- 8.3.1 Helix Parameters Controlling DNA Structure -- 8.3.1.1 Roll and Tilt -- 8.3.1.2 Twist -- 8.3.1.3 Propeller Twist, Slide, and Shift -- 8.3.1.4 Changes in DNA Groove Width -- 8.3.2 Influence of Exocyclic Groups on Base Stacking -- 8.3.3 Flexibility of Dinucleotide Steps -- 8.3.3.1 Pyrimidine-purine (Y-R) Steps -- 8.3.3.2 Purine-purine (R-R) or Pyrimidine-pyrimidine (Y-Y) Steps -- 8.3.3.3 Purine-pyrimidine (R-Y) Steps -- 8.4 Examples of DNA Bending Proteins -- 8.4.1 Histone Binding to DNA -- 8.4.2 Phage λ Xis Protein -- 8.4.3 Papillomavirus E2 Protein -- 8.4.4 Escherichia coli Fis Protein -- 8.4.4.1 Long-range DNA Condensation by Fis -- 8.4.5 Escherichia coli CAP Protein. , 8.4.6 Prokaryotic HU/IHF Protein Family -- 8.4.6.1 Single-DNA Molecule Analysis of HU/IHF Protein Binding -- 8.4.7 HMGB Protein Family -- 8.4.7.1 Single DNA Molecule Analyses of HMGB Protein Binding -- 8.4.7.2 DNA Binding by HMGB Shares Features with TBP -- 8.5 Concluding Remarks -- References -- Chapter 9 Mode of Action of Proteins with RNA Chaperone Activity -- 9.1 Introduction -- 9.1.1 RNA Folding -- 9.1.2 Proteins with RNA Chaperone Activity (RCA) -- 9.1.3 Measuring RCA -- 9.2 Mode of Action of Proteins with RCA -- 9.2.1 RNA Annealing Activity -- 9.2.1.1 Annealing of Protein-bound Guide RNAs with Target RNAs -- 9.2.2 Nucleic Acid Melting Activity -- 9.3 RNA Binding and Restructuring -- 9.3.1 Proteins with RCA Interact with RNA only Weakly -- 9.3.2 Proteins with Specific RNA-binding Affinity -- 9.3.3 Protein Structure and RNA Chaperone Activity -- Acknowledgements -- References -- Chapter 10 Structure and Function of DNA Topoisomerases -- 10.1 Introduction -- 10.2 Type IA Topoisomerases -- 10.2.1 Overview -- 10.2.2 Structures and Mechanism -- 10.2.3 Type IA Topoisomerase Paralogs -- 10.2.3.1 Topoisomerase III -- 10.2.3.2 Reverse Gyrase -- 10.3 Type IB Topoisomerases -- 10.3.1 Overview -- 10.3.2 General Architecture -- 10.3.3 DNA Recognition and Cleavage -- 10.3.4 Mechanism -- 10.4 Topoisomerase V - The Defining Member of the Type IC Topoisomerases? -- 10.5 Type IIA Topoisomerases -- 10.5.1 Overview -- 10.5.2 Structural Organization -- 10.5.2.1 ATPase Domain -- 10.5.2.2 DNA Breakage/Reunion Domain and the DNA Binding/Cleavage Core -- 10.5.3 Duplex DNA Transport Mechanism -- 10.5.3.1 Type IIA Topoisomerase Paralogs: Role of the C-terminal Domain in Modulating Duplex Transport -- 10.5.4 Physiological Specialization of Type IIA Topoisomerases -- 10.6 Type IIB Topoisomerases -- 10.6.1 Overview -- 10.6.2 Structure -- 10.6.3 Mechanism -- 10.7 Conclusions. , Acknowledgements.
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  • 4
    Description / Table of Contents: Written by a team of experts, this book bridges the gap between the DNA- and RNA- views of protein-nucleic acid recognition which are often treated as separate fields, The structural biology of protein-nucleic acid interactions is in some ways a mature field and in others in its infancy. High-resolution structures of protein-DNA complexes have been studied since the mid 1980s and a vast array of such structures has now been determined, but surprising and novel structures still appear quite frequently. High-resolution structures of protein-RNA complexes were relatively rare until the last decade. Propelled by advances in technology as well as the realization of RNA's importance to biology, the number of example structures has ballooned in recent years. New insights are now being gained from comparative studies only recently made possible due to the size of the database, as well as from careful biochemical and biophysical studies. As a result of the explosion of research in this area, it is no longer possible to write a comprehensive review. Instead, current review articles tend to focus on particular subtopics of interest. This makes it difficult for newcomers to the field to attain a solid understanding of the basics. One goal of this book is therefore to provide in-depth discussions of the fundamental principles of protein-nucleic acid interactions as well as to illustrate those fundamentals with up-to-date and fascinating examples for those who already possess some familiarity with the field. The book also aims to bridge the gap between the DNA- and the RNA- views of nucleic acid - protein recognition, which are often treated as separate fields. However, this is a false dichotomy because protein - DNA and protein - RNA interactions share many general principles. This book therefore includes relevant examples from both sides, and frames discussions of the fundamentals in terms that are relevant to both. The monograph approaches the study of protein-nucleic acid interactions in two distinctive ways. First, DNA-protein and RNA-protein interactions are presented together. Second, the first half of the book develops the principles of protein-nucleic acid recognition, whereas the second half applies these to more specialized topics. Both halves are illustrated with important real life examples. The first half of the book develops fundamental principles necessary to understand function. An introductory chapter by the editors reviews the basics of nucleic acid structure. Jen-Jacobsen and Jacobsen discuss how solvent interactions play an important role in recognition, illustrated with extensive thermodynamic data on restriction enzymes. Marmorstein and Hong introduce the zoology of the DNA binding domains found in transcription factors, and describe the combinational recognition strategies used by many multiprotein eukaryotic complexes. Two chapters discuss indirect readout of DNA sequence in detail: Berman and Lawson explain the basic principles and illustrate them with in-depth studies of CAP, while in their chapter on DNA bending and compaction Johnson, Stella and Heiss highlight the intrinsic connections between DNA bending and indirect readout. Horvath lays out the fundamentals of protein recognition of single stranded DNA and single stranded RNA, and describes how they apply in a detailed analysis of telomere end binding proteins. Nucleic acids adopt more complex structures - Lilley describes the conformational properties of helical junctions, and how proteins recognize and cleave them. Because RNA readily folds due to the stabilizing role of its 2'-hydroxyl groups, Li discusses how proteins recognize different RNA folds, which include duplex RNA. With the fundamentals laid out, discussion turns to more specialized examples taken from important aspects of nucleic acid metabolism. Schroeder discusses how proteins chaperone RNA by rearranging its structure into a functional form. Berger and Dong discuss how topoisomerases alter the topology of DNA and relieve the superhelical tension introduced by other processes such as replication and transcription. Dyda and Hickman show how DNA transposes mediate genetic mobility and Van Duyne discusses how site-specific recombinases "cut" and "paste" DNA. Horton presents a comprehensive review of the structural families and chemical mechanisms of DNA nucleases, whereas Li in her discussion of RNA-protein recognition also covers RNA nucleases. Lastly, Ferre-D'Amare shows how proteins recognize and modify RNA transcripts at specific sites. The book also emphasises the impact of structural biology on understanding how proteins interact with nucleic acids and it is intended for advanced students and established scientists wishing to broaden their horizons
    Type of Medium: Online Resource
    Pages: 416 p , Online-Ressource , 109 b&w, ill
    Edition: RSC eBook Collection 1968-2009
    Language: English
    Note: Ebook , Chapter 1: Introduction-- Chapter 2: The role of water and effects of small ions in site-specific protein-DNA interactions-- Chapter 3: Structural Basis for Sequence-Specific DNA Recognition by Transcription Factors and their Complexes-- Chapter 4: Indirect Readout Of DNA Sequence by Proteins-- Chapter 5: Single-stranded Nucleic Acid (SSNA)-binding Proteins-- Chapter 6: DNA junctions and their interaction with resolving enzymes-- Chapter 7: RNA-protein Interactions in Ribonucleoprotein Particles and Ribonucleases-- Chapter 8: Bending and compaction of DNA by proteins-- Chapter 9: Mode of Action of Proteins with RNA Chaperone Activity-- Chapter 10: Structure and Function of DNA Topoisomerases-- Chapter 11: DNA Transposases-- Chapter 12: Site-Specific Recombinases-- Chapter 13: DNA Nucleases-- Chapter 14: RNA-modifying enzymes.
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  • 5
    Publication Date: 2024-03-02
    Description: The here presented data comprises the dry bulk density in g/cc, the total organic content (TOC) in %, the total inorganic content (TIC) in %, the total carbon content (TC) in %, the calcium carbonate content (CaCO3) in %, the terrigenous influx rate in g kyr-1 cm-2 and the z-score normalised XRF data counts for the elements Si, K, Ti, Mn, Fe, Br, Rb, Sr and Zr from sediment core ORI-891-16-P1 (19° 33.36'N, 116° 6.77'E; 1595 m water depth). Data is provided against age.
    Keywords: ORI-891-16-P1; PC; Piston corer
    Type: Dataset
    Format: application/zip, 3 datasets
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  • 6
    Publication Date: 2024-03-02
    Description: The here presented data comprises the z-score normalised XRF data counts for the elements Si, K, Ti, Mn, Fe, Br, Rb, Sr and Zr from sediment core ORI-891-16-P1 (19° 33.36'N, 116° 6.77'E; 1595 m water depth). Data is provided against age.
    Keywords: AGE; Bromine, normalized; Calcium, normalized; Iron, normalized; Manganese, normalized; ORI-891-16-P1; PC; Piston corer; Potassium, normalized; Rubidium, normalized; Silicon, normalized; Strontium, normalized; Titanium, normalized; X-ray fluorescence (XRF); Zirconium, normalized
    Type: Dataset
    Format: text/tab-separated-values, 7310 data points
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  • 7
    Publication Date: 2024-03-02
    Description: The here presented data contains the ln(Ti/Ca) ratio against core depth (m) and age (kyr) from sediment core ORI-891-16-P1 (19° 33.36'N, 116° 6.77'E; 1595 m water depth). The XRF core scanning measurements were conducted at the National Taiwan University (NTU) using an Itrax Cox XRF core scanner. The measurements were conducted using a generator setting of 30 kV, a current of 50 mA and a count time of 5 s. To eliminate non-linear matrix effects and constant-sum constraints, we used logratios to account for a statistically more robust representation of element ratio. The ln(Ti/Ca) element ratio is considered a proxy for terrigenous input, with Ti being dominated by the presence of various heavy minerals e.g. ilmenite, perovskite, rutile and titanite. In contrast, Ca contents have been related to biogenic carbonate variability which is considered a background pelagic signal.
    Keywords: AGE; DEPTH, sediment/rock; East Asian summer monsoon; ln-Titanium/Calcium ratio; ORI-891-16-P1; PC; Piston corer; South China Sea; X-ray fluorescence (XRF); XRF data
    Type: Dataset
    Format: text/tab-separated-values, 731 data points
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  • 8
    Publication Date: 2024-03-02
    Description: The here presented data comprises the dry bulk density in g/cc, the total organic content (TOC) in %, the total inorganic content (TIC) in %, the total carbon content (TC) in %, the calcium carbonate content (CaCO3) in %, the terrigenous influx rate in g kyr-1 cm-2 from sediment core ORI-891-16-P1 (19° 33.36'N, 116° 6.77'E; 1595 m water depth). Data is provided against age.
    Keywords: AGE; Calcium carbonate; Calculated; Carbon, inorganic, total; Carbon, organic, total; Carbon, total; Density, dry bulk; ORI-891-16-P1; PC; Piston corer; Terrigenous, flux
    Type: Dataset
    Format: text/tab-separated-values, 483 data points
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  • 9
    Publication Date: 2021-07-10
    Description: EXTRACT (SEE PDF FOR FULL ABSTRACT):We have analyzed streamflow variations recorded at 15 USGS gauging stations in California during the past 90 years or so. The anomalies (departures from the 1960-1990 mean discharge) of streamflow on annual-to-decadal time scales are strongly correlated with precipitation anomalies in each drainage basin. ... Although causes of the decadal climate (precipitation) variability are not known with certainty, the use of streamflow records may help us understand the relative strengths of moisture sources and shift of the jet stream in atmospheric circulation.
    Keywords: Atmospheric Sciences ; Limnology ; PACLIM ; hydrology
    Repository Name: AquaDocs
    Type: conference_item
    Format: application/pdf
    Format: application/pdf
    Format: 79-91
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  • 10
    Publication Date: 2022-09-02
    Description: Risk management has reduced vulnerability to floods and droughts globally, yet their impacts are still increasing. An improved understanding of the causes of changing impacts is therefore needed, but has been hampered by a lack of empirical data. On the basis of a global dataset of 45 pairs of events that occurred within the same area, we show that risk management generally reduces the impacts of floods and droughts but faces difficulties in reducing the impacts of unprecedented events of a magnitude not previously experienced. If the second event was much more hazardous than the first, its impact was almost always higher. This is because management was not designed to deal with such extreme events: for example, they exceeded the design levels of levees and reservoirs. In two success stories, the impact of the second, more hazardous, event was lower, as a result of improved risk management governance and high investment in integrated management. The observed difficulty of managing unprecedented events is alarming, given that more extreme hydrological events are projected owing to climate change.
    Repository Name: EPIC Alfred Wegener Institut
    Type: Article , NonPeerReviewed
    Format: application/pdf
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