Nuclear Structure and Function: Volume 53
Published on 24. November 1997
Book
Hardback
625 pages
978-0-12-564155-5 (ISBN)
Description
This volume is a comprehensive guide to the methodologies used in the study of structural domains of cell nuclei. The text covers chromatin, the karyoskeleton, the soluble domain, and the nucleolus. It details methods that are used to isolate components from these domains and techniques used to assemble and disassemble nuclear elements. There is also coverage of three-dimensional mapping and localization of nuclear processes.
Reviews / Votes
"Nuclear Structure and Function is remarkably up to date, and all of the authors have produced clear and very useful contributions.This handbook is highly recommended and will be essential for researchers investigating all aspects of the nucleus, from the biochemistry of specific processes through to nuclear architecture. It will also be very helpful to all those who want to use some of these techniques as part of their research, perhaps to investigate the function of a particular gene product or the control of its expression."
--TIBS
More details
Series
Language
English
Place of publication
San Diego
United States
Publishing group
Elsevier Science Publishing Co Inc
Target group
Professional and scholarly
Graduate students, technicians, postdoctoral, and experienced researchers. Cell, developmental, and molecular biologists, geneticists, human genome researchers, and others studying nuclear structure and organization.
Dimensions
Height: 235 mm
Width: 191 mm
Weight
1430 gr
ISBN-13
978-0-12-564155-5 (9780125641555)
Copyright in bibliographic data and cover images is held by Nielsen Book Services Limited or by the publishers or by their respective licensors: all rights reserved.
Schweitzer Classification
Other editions
Additional editions
Miguel Berrios
Nuclear Structure and Function: Volume 53
Book
12/1997
Academic Press
€142.37
Withdrawn from sale
Persons
University of California, Santa Barbara, USA
Content
M. Berrios, Introduction.
Cell Fractionation Preparation and Characterization of Probes:
M. Berrios, Isolation and Characterization of Nuclear Pore Complex-Lamina Fractions from Vertebrates.
P.A. Fisher,Preparation and Characterization of Karyoskeletal Protein-Enriched Fractions from Drosophila melanogaster.
J.P. Aris, Isolation of Nuclei and Nucleoli from Yeast Saccharomyces cerevisiae.
Structural Analysis of the Interphase Nucleus:
M.R. Paddy, Qualitative and Quantitative Approaches to the Spatial Localization of Nuclear Proteins with the Fluorescence Light Microscope.
U. Kubitscheck and R. Peters, Localization of Single Nuclear Pore Complexes by Confocal Laser Scanning Microscopy and Analysis of their Distribution.
A.S. Belmont, Nuclear Ultrastructure Transmission Electron Microscopy and Image Analysis.
T.D. Allen, S.A. Rutherford, G.R. Bennion, M.W. Goldberg, and E. Kiseleva, Three-Dimensional Surface Structure Analysis of the Nucleus.
J. Hainfeld and J. Wall, Scanning Transmission Electron Microscopy of Nucleic Acid-Protein Complexes.
Chromatin and Sub-Nuclear Structures:
C.L. Woodcock and R.A. Horowitz, Chromatin and Nucleosomal Assemblies.
A.F. Dernburg and J.W. Sedat, Mapping the Architecture of Interphase Nucleus.
A.J. Solari, Structural Analysis of Meiotic Chromosomes and Synaptonemal Complexes in Higher Vertebrates.
J. Engebrecht, F. Klein, and J. Loidl, Genetic and Morphological Approaches for the Analysis of Meiotic Chromosomes in Yeast.
M. Grote and R. Peters, Mapping Proteins to Nuclear Pore Complexes by Immunogold Electron Microscopy.
R.L. Ochs, Methods to Study the Structure and Function of the Nucleolus.
T. Kohwi-Shigematsu, I. DeBelle, L.A. Dickinson, S. Galande, and Y. Kowi, Identification of Base-Unpairing Region (BUR)-Binding Proteins and Characterization of their In Vivo Binding Sequences.
Nuclear Assembly/Disassembly Cell-Free Systems:
B. Burke, Mammalian Systems to Study Nuclear Assembly.
M.J. Lohka and D.A. Warren, Analysis of Nuclear Envelope Assembly Using Extracts of Xenopus Eggs.
P.A. Fisher and M. Berrios, Methods for Studying Nuclear Assembly and Disassembly Using Drosophila Cell-Free Systems.
P. Collas and D.L. Poccia, Methods for Studying in Vitro Assembly of Male Pronuclei Using Oocyte Extracts from Marine Invertebrates Sea Urchins and Surf Clams.
Localization of Nuclear Processes:
R. Van Driel, E.M.M. Manders, L. de Jong, and J.A. Aten, Mapping Sites of DNA Replication In Situ.
Y. Osheim and A.L. Beyer, Analysis of RNA Transcription and Processing by Transmission Electron Microscopy.
G.H. Leno, Cell-Free Systems to Study Chromatin Remodeling.
C. Dingwall and I. Palacios, Reconstruction of Nuclear Protein and snRNP Import In Vitro.
D.S. Goldfarb, Measuring Nuclear Transport Efficiency in Saccharomyces cerevisiae Using a Nuclear Localization Signal-Tagged Green Fluorescent Protein.
M.P. Terns and S. Goldfarb, The Nuclear Transport of Microinjected RNAs in Xenopus Oocytes.
R. Benavente and G. Krohne, In Vivo Systems to Study the Dynamics of Nuclear Lamins.
Y. Lazebnik, Apoptosis a Model System to Study the Structural Collapse of the Nucleus.
Subject Index.
Cell Fractionation Preparation and Characterization of Probes:
M. Berrios, Isolation and Characterization of Nuclear Pore Complex-Lamina Fractions from Vertebrates.
P.A. Fisher,Preparation and Characterization of Karyoskeletal Protein-Enriched Fractions from Drosophila melanogaster.
J.P. Aris, Isolation of Nuclei and Nucleoli from Yeast Saccharomyces cerevisiae.
Structural Analysis of the Interphase Nucleus:
M.R. Paddy, Qualitative and Quantitative Approaches to the Spatial Localization of Nuclear Proteins with the Fluorescence Light Microscope.
U. Kubitscheck and R. Peters, Localization of Single Nuclear Pore Complexes by Confocal Laser Scanning Microscopy and Analysis of their Distribution.
A.S. Belmont, Nuclear Ultrastructure Transmission Electron Microscopy and Image Analysis.
T.D. Allen, S.A. Rutherford, G.R. Bennion, M.W. Goldberg, and E. Kiseleva, Three-Dimensional Surface Structure Analysis of the Nucleus.
J. Hainfeld and J. Wall, Scanning Transmission Electron Microscopy of Nucleic Acid-Protein Complexes.
Chromatin and Sub-Nuclear Structures:
C.L. Woodcock and R.A. Horowitz, Chromatin and Nucleosomal Assemblies.
A.F. Dernburg and J.W. Sedat, Mapping the Architecture of Interphase Nucleus.
A.J. Solari, Structural Analysis of Meiotic Chromosomes and Synaptonemal Complexes in Higher Vertebrates.
J. Engebrecht, F. Klein, and J. Loidl, Genetic and Morphological Approaches for the Analysis of Meiotic Chromosomes in Yeast.
M. Grote and R. Peters, Mapping Proteins to Nuclear Pore Complexes by Immunogold Electron Microscopy.
R.L. Ochs, Methods to Study the Structure and Function of the Nucleolus.
T. Kohwi-Shigematsu, I. DeBelle, L.A. Dickinson, S. Galande, and Y. Kowi, Identification of Base-Unpairing Region (BUR)-Binding Proteins and Characterization of their In Vivo Binding Sequences.
Nuclear Assembly/Disassembly Cell-Free Systems:
B. Burke, Mammalian Systems to Study Nuclear Assembly.
M.J. Lohka and D.A. Warren, Analysis of Nuclear Envelope Assembly Using Extracts of Xenopus Eggs.
P.A. Fisher and M. Berrios, Methods for Studying Nuclear Assembly and Disassembly Using Drosophila Cell-Free Systems.
P. Collas and D.L. Poccia, Methods for Studying in Vitro Assembly of Male Pronuclei Using Oocyte Extracts from Marine Invertebrates Sea Urchins and Surf Clams.
Localization of Nuclear Processes:
R. Van Driel, E.M.M. Manders, L. de Jong, and J.A. Aten, Mapping Sites of DNA Replication In Situ.
Y. Osheim and A.L. Beyer, Analysis of RNA Transcription and Processing by Transmission Electron Microscopy.
G.H. Leno, Cell-Free Systems to Study Chromatin Remodeling.
C. Dingwall and I. Palacios, Reconstruction of Nuclear Protein and snRNP Import In Vitro.
D.S. Goldfarb, Measuring Nuclear Transport Efficiency in Saccharomyces cerevisiae Using a Nuclear Localization Signal-Tagged Green Fluorescent Protein.
M.P. Terns and S. Goldfarb, The Nuclear Transport of Microinjected RNAs in Xenopus Oocytes.
R. Benavente and G. Krohne, In Vivo Systems to Study the Dynamics of Nuclear Lamins.
Y. Lazebnik, Apoptosis a Model System to Study the Structural Collapse of the Nucleus.
Subject Index.