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  • 1
    Keywords: Medicine ; Human Genetics ; Bioinformatics ; Biomedicine ; Human Genetics ; Bioinformatics ; Biomedicine general ; Springer eBooks
    Description / Table of Contents: Part I: Overview.-℗ History of DNA Sequencing Technologies -- Clinical Molecular Diagnostic Techniques: A Brief Review -- Part II: The Technologies and Bioinformatics -- Methods of Gene Enrichment and Massively Parallel Sequencing Technologies -- Sequence Alignment, Analysis, and Bioinformatics Pipelines -- Protein Structural Based Analysis for Variant Interpretation of Missense Variants at the Genomics Era: Using MNGIE Disease as an Example -- Algorithms and Guidelines for Interpretation of DNA Variants -- Part III: Application to Clinical Diagnostics -- NGS-based Clinical Diagnosis of Genetically Heterogeneous Disorders -- Molecular Diagnosis of Congenital Disorders of Glycosylation (CDG) -- NGS Improves the Diagnosis of X-Linked Intellectual Disability (XLID) -- NGS Analysis of Heterogeneous Retinitis Pigmentosa -- Next Generation Sequencing of the Whole Mitochondrial Genome -- Application of Next-Generation Sequencing of Nuclear Genes for Mitochondrial Disorders -- Noninvasive Prenatal Diagnosis Using Next Generation Sequencing -- Part IV: Compliance with CAP/CLIA Regulations -- Guidelines and Approaches to Compliance with Regulatory and Clinical Standards: Quality Control Procedures and Quality Assurance -- Validation of NGS-based Test and Implementation of Quality Control Procedures -- Frequently Asked Questions about the Clinical Utility of Next Generation Sequencing in Molecular Diagnosis of Human Genetic Diseases -- Index
    Abstract: In recent years, owing to the fast development of a variety of sequencing technologies in the post human genome project era, sequencing analysis of a group of target genes, entire protein coding regions of the human genome, and the whole human genome has become a reality.℗ ℗ Next Generation Sequencing (NGS) or Massively Parallel Sequencing (MPS) technologies offers a way to screen for mutations in many different genes in a cost and time efficient manner by deep coverage of the target sequences.℗ This novel technology has now been applied to clinical diagnosis of Mendelian disorders of well characterized or undefined diseases, discovery of new disease genes, noninvasive prenatal diagnosis using maternal blood, and population based carrier testing of severe autosomal recessive disorders.℗ This book covers topics of these applications, including potential limitations and expanded application in the future.℗ ℗ ℗ ℗
    Pages: : digital.
    ISBN: 9781461470014
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  • 2
    Keywords: Life sciences ; Human Genetics ; Biostatistics ; Microbial genetics ; Microbial genomics ; Life sciences ; Microbial Genetics and Genomics ; Human Genetics ; Biostatistics ; Springer eBooks
    Description / Table of Contents: Part I: overview -- 1. NGS, The new gold standard of identification of defective genes -- 2. Principles of target gene enrichments, pros and cons -- 3. Criteria for clinical application: Full validation and performance characteristics -- 4. Clinical requirements: variant interpretation, confirmation, and turnaround time -- Part II: Experiences in various applications -- 5. The metabolic pathways: GSD, CDG, cobalamin metabolism, and others -- 6. The eye gene panels -- 7. The otogenes -- 8. The immunodeficiency disorders -- 9. The bone density and skeletal related disorders -- 10.The hereditary cancer genes -- 11.The molecular diagnosis of cancers and implications in treatment: Marilyn Li -- 12. Neuromuscular disorders -- 13. The cardiac panel: YuXin Fan, GeneDx or Harvard Partner -- 14. The mitochondrial genome -- 15. The Nuclear Mitomes
    Abstract: Next Generation Sequencing technology has been applied to clinical diagnoses in the past three to five years using various approaches, including target gene panels and whole exomes. The purpose of this book is to summarize the experiences, the results, advantages and disadvantages, along with future development in the area of NGS-based molecular diagnosis. This up-to-date volume will not only provide the readers working with Next Generation Sequencing the basics on how to apply the technology to molecular diagnosis, but will present the results and experience of practical application
    Pages: VIII, 364 p. 23 illus., 17 illus. in color. : online resource.
    ISBN: 9783319564180
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  • 3
    Keywords: Medicine ; Human Genetics ; Biomedicine ; Human Genetics ; Molecular Medicine ; Biomedicine general ; Springer eBooks
    Description / Table of Contents: Part 1: Overview -- The Clinical Spectrum of Nuclear DNA-Related Mitochondrial Disorders -- Biochemical and Molecular Methods for the Study of Mitochondrial Disorders -- Part 2: Genes Involved in Mitochondrial DNA Biogenesis and Maintenance of Mitochondrial DNA Integrity -- Mitochondrial Disorders Associated with the Mitochondrial DNA Polymerase g: A Focus on Intersubunit Interactions -- Alpers-Huttenlocher Syndrome, Polymerase Gamma 1, and Mitochondrial Disease -- Deoxyguanosine Kinase -- 〈i〉MPV17〈/i〉-Associated Hepatocerebral Mitochondrial DNA Depletion Syndrome -- Mitochondrial DNA Multiple Deletion Syndromes, Autosomal Dominant and Recessive (POLG, POLG2, TWINKLE and ANT1) -- Defects in Mitochondrial Dynamics and Mitochondrial DNA Instability -- Depletion of mtDNA with MMA: 〈i〉SUCLA2〈/i〉 and 〈i〉SUCLG1〈/i〉 -- 〈i〉RRM2B〈/i〉-Related Mitochondrial Disease -- Part 3: Complex Subunits and Assembly Genes -- Complex Subunits and Assembly Genes: Complex I -- Mitochondrial Respiratory Chain Complex II -- Mitochondrial Complex III Deficiency of Nuclear Origin: Molecular Basis, Pathophysiological Mechanisms and Mouse Models -- Mitochondrial Cytochrome 〈i〉c〈/i〉 Oxidase Assembly in Health and Human Diseases -- Part 4: Mitochondrial Protein Translation Related Diseases -- Mitochondrial Aminoacyl-tRNA Synthetases -- Mitochondrial Protein Translation Related Disease: Mitochondrial Ribosomal Proteins and Translation Factors -- Disorders of Mitochondrial RNA Modification -- Part 5: Others -- Pyruvate Dehydrogenase Complex Deficiencies.-〈b〉 〈/b〉Nuclear Genes Causing Mitochondrial Cardiomyopathy -- Mitochondrial Diseases Caused by Mutations in Inner Membrane Chaperone Proteins -- Index
    Abstract: Mitochondrial cytopathies are mutations in the inherited maternal mitochondrial genome, or the nuclear DNA-mutation. Mitochondrial respiratory chain disorders (RCD) are a group of genetically and clinically heterogeneous diseases, due to the fact that protein components of the respiratory chain are encoded by both mitochondrial and nuclear genomes and are essential in all cells.℗ In addition, the biogenesis, structure and function of mitochondria, including DNA replication, transcription, and translation, all require nuclear encoded genes.℗ Since mitochondria are present in every cell, every tissue, mitochondrial disorders usually affects multiple organs. 〈i〉Mitochondrial Disorders Caused by Nuclear Genes 〈/i〉discusses the〈i〉 〈/i〉biochemical, molecular, clinical, and genetic aspects〈i〉 〈/i〉of complex dual genome mitochondrial disorders. Chapters include genes involved in mitochondrial DNA biogenesis and maintenance of mitochondrial DNA integrity, complex subunits and assembly genes, and mitochondrial protein translation related diseases
    Pages: XII, 369 p. 32 illus., 20 illus. in color. : digital.
    ISBN: 9781461437222
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  • 4
    ISSN: 1573-4927
    Keywords: nuclear acetyltransferase ; nonhistone substrate ; high-mobility group acetylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A variety of nonhistone proteins and polyamines has been studied for their substrate activity for nuclear histoneN-acetyltransferase. Nonhistone chromatin high-mobility group (HMG) proteins are found to be as good a substrate for the enzyme as histones. The enzyme also acetylates spermidine and spermine. However, protamine, bovine serum albumin, and ubiquitin are not substrates. Chymotryptic peptides of histone and HMGs retained about 64% of the substrate activity, but trypsin treatment reduced the substrate activity by more than 85%. BothN-acetyltransferase activities for HMGs and histones are copurified through salt extraction, polyethylene glycol fractionation, and chromatography on DEAE-cellulose, phosphocellulose columns, and a HPLC anionic-exchange column. The highly purified nuclear histone acetyltransferase shows similar optimalpH and ping-pong kinetics for both HMGs and histones. TheK m for HMG is 0.25 mg/ml. HMGs are able to accept the acetyl group from isolated acetyl-enzyme intermediate. Denatured gel analysis shows that HMG 1 and HMG 2 are the major proteins acetylated. High salt concentrations, mononucleotides, and DNA, which inhibit histone substrate activity of the enzyme, also inhibit HMG substrate activity. These observations suggest that there is a major nuclearN-acetyltransferase which is responsible for the acetylation of both histones and HMGs and perhaps also of spermine and spermidine. Thus the regulation of the structure and function of chromatin through postsynthetic acetylation can be achieved by a single nuclearN-acetyltransferase.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-4927
    Keywords: nuclear acetyltransferase ; nonhistone substrate ; high-mobility group acetylase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A variety of nonhistone proteins and polyamines has been studied for their substrate activity for nuclear histoneN-acetyltransferase. Nonhistone chromatin high-mobility group (HMG) proteins are found to be as good a substrate for the enzyme as histones. The enzyme also acetylates spermidine and spermine. However, protamine, bovine serum albumin, and ubiquitin are not substrates. Chymotryptic peptides of histone and HMGs retained about 64% of the substrate activity, but trypsin treatment reduced the substrate activity by more than 85%. BothN-acetyltransferase activities for HMGs and histones are copurified through salt extraction, polyethylene glycol fractionation, and chromatography on DEAE-cellulose, phosphocellulose columns, and a HPLC anionic-exchange column. The highly purified nuclear histone acetyltransferase shows similar optimalpH and ping-pong kinetics for both HMGs and histones. TheK m for HMG is 0.25 mg/ml. HMGs are able to accept the acetyl group from isolated acetyl-enzyme intermediate. Denatured gel analysis shows that HMG 1 and HMG 2 are the major proteins acetylated. High salt concentrations, mononucleotides, and DNA, which inhibit histone substrate activity of the enzyme, also inhibit HMG substrate activity. These observations suggest that there is a major nuclearN-acetyltransferase which is responsible for the acetylation of both histones and HMGs and perhaps also of spermine and spermidine. Thus the regulation of the structure and function of chromatin through postsynthetic acetylation can be achieved by a single nuclearN-acetyltransferase.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-4927
    Keywords: histone acetyltransferase ; chromatin activity ; chromatin autoregulation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Nuclear histone acetyltransferase is found to be inhibited by various nucleic acids and components. Of the adenosine phosphates, the order of inhibitory potency is ATP〉ADP〉AMP. Among the nucleoside triphosphates, GTP seems to be the best inhibitor, followed by ATP, CTP, and UTP. Deoxymononucleotides have the same order of inhibition potential as their ribonucleotide counterparts, with inhibition constants in the low millimolar range. Oligonucleotides and polynucleotides are much better inhibitors than mononucleotides. The inhibition constants of the DNA molecules are size dependent. Molecules larger than 40 base pairs have inhibition constants less than 18 µg/ml, whereas molecules with decreasing numbers of base pairs have increasing magnitudes of inhibition constants. However, acetyltransferase has a lower affinity for free DNA molecules than for DNA · histone complexes as revealed by its interaction with DNA-Sepharose and histone · DNA-Sepharose columns. Furthermore, native chromatin depleted of endogenous histone acetyltransferase activity shows no inhibitory effect on the enzyme. Yet heated chromatin not only loses substrate activity but also becomes an inhibitor for the enzyme. Since unmodified sea urchin sperm chromatin has been shown to be a potent acetyltransferase inhibitor, it seems possible that DNA · histone complexes may be the true inhibitory species and that the conformational states of such complexes may serve as a regulatory mechanism in the control of the enzyme activity.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 22 (1983), S. 4637-4641 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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