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  1. Book: Difference gel electrophoresis

    Ohlendieck, Kay

    methods and protocols

    (Methods in molecular biology ; 2596 ; Springer protocols)

    2023  

    Author's details edited by Kay Ohlendieck
    Series title Methods in molecular biology ; 2596
    Springer protocols
    Collection
    Keywords Two-Dimensional Difference Gel Electrophoresis ; Electrophoresis, Polyacrylamide Gel / methods ; Proteomics / methods ; Laboratory Manual ; Proteomics ; Gel electrophoresis
    Subject code 572.6
    Language English
    Size xii, 485 Seiten, Illustrationen, 26 cm
    Edition Second edition
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    Note Previous edition: published as Difference gel electrophoresis (DIGE). New York: Humana Press, 2012. - Formerly CIP.
    HBZ-ID HT021687496
    ISBN 978-1-0716-2830-0 ; 9781071628317 ; 1-0716-2830-5 ; 1071628313
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    Zs A 7042 -2596- not available for loan Lesesaal EG

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  2. Book: Difference gel electrophoresis

    Ohlendieck, Kay

    methods and protocols

    (Methods in molecular biology ; 1664 ; Springer protocols)

    2018  

    Author's details edited by Kay Ohlendieck
    Series title Methods in molecular biology ; 1664
    Springer protocols
    Collection
    Keywords DIGE ; fluorescence image analysis ; proteomic profiling ; PTM analysis ; Immunoblot
    Subject code 570
    Language English
    Size x, 315 Seiten, Illustrationen, 25.4 cm x 17.8 cm
    Publisher Humana Press
    Publishing place New York, NY
    Publishing country United States
    Document type Book
    HBZ-ID HT019404448
    ISBN 978-1-4939-7267-8 ; 1-4939-7267-7 ; 9781493972685 ; 1493972685
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    Zs A 7042 -1664- verfügbar in Königswinter Königswinter

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  3. Article ; Online: Two-CyDye-Based 2D-DIGE Analysis of Aged Human Muscle Biopsy Specimens.

    Ohlendieck, Kay

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2596, Page(s) 265–289

    Abstract: The gradual loss of skeletal muscle mass during aging and associated decline in contractile strength can result in reduced fitness, frailty, and loss of independence. In order to better understand the molecular and cellular mechanisms that underlie ... ...

    Abstract The gradual loss of skeletal muscle mass during aging and associated decline in contractile strength can result in reduced fitness, frailty, and loss of independence. In order to better understand the molecular and cellular mechanisms that underlie sarcopenia of old age and the frailty syndrome, as well as identify novel therapeutic targets to treat age-related fiber wasting, it is crucial to develop a comprehensive biomarker signature of muscle aging. Fluorescence two-dimensional gel electrophoresis (2D-DIGE) in combination with sensitive mass spectrometry presents an ideal bioanalytical tool for biomarker discovery in biogerontology. This chapter outlines the application of the 2D-DIGE method for the comparative analysis of human biopsy specimens from middle-aged versus senescent individuals using a two-CyDye-based method.
    MeSH term(s) Middle Aged ; Aged ; Humans ; Two-Dimensional Difference Gel Electrophoresis/methods ; Frail Elderly ; Electrophoresis, Gel, Two-Dimensional/methods ; Muscle, Skeletal ; Biomarkers ; Biopsy
    Chemical Substances Biomarkers
    Language English
    Publishing date 2022-11-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2831-7_19
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Comparative 3-Sample 2D-DIGE Analysis of Skeletal Muscles.

    Ohlendieck, Kay

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2596, Page(s) 127–146

    Abstract: The skeletal muscle proteome consists of a large number of diverse protein species with a broad and dynamic concentration range. Since mature skeletal muscles are characterized by a distinctive combination of contractile cells with differing ... ...

    Abstract The skeletal muscle proteome consists of a large number of diverse protein species with a broad and dynamic concentration range. Since mature skeletal muscles are characterized by a distinctive combination of contractile cells with differing physiological and biochemical properties, it is essential to determine specific differences in the protein composition of fast, slow, and hybrid fibers. Fluorescence two-dimensional difference gel electrophoresis (2D-DIGE) is a powerful comparative tool to analyze fiber type-specific differences between predominantly fast contracting versus slower twitching muscles. In this chapter, the application of the 2D-DIGE method for the comparative analysis of different subtypes of skeletal muscles is outlined in detail. A standardized proteomic workflow is described, involving sample preparation, protein extraction, differential fluorescence labeling using a 3-CyDye system, first-dimension isoelectric focusing, second-dimension slab gel electrophoresis, 2D-DIGE image analysis, protein digestion, and mass spectrometry.
    MeSH term(s) Two-Dimensional Difference Gel Electrophoresis/methods ; Proteomics/methods ; Isoelectric Focusing ; Proteome ; Muscle, Skeletal ; Electrophoresis, Gel, Two-Dimensional/methods
    Chemical Substances Proteome
    Language English
    Publishing date 2022-11-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2831-7_11
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Top-Down Proteomics and Comparative 2D-DIGE Analysis.

    Ohlendieck, Kay

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2596, Page(s) 19–38

    Abstract: The combination of large-scale protein separation techniques, sophisticated mass spectrometry, and systems bioinformatics has led to the establishment of proteomics as a distinct discipline within the wider field of protein biochemistry. Both discovery ... ...

    Abstract The combination of large-scale protein separation techniques, sophisticated mass spectrometry, and systems bioinformatics has led to the establishment of proteomics as a distinct discipline within the wider field of protein biochemistry. Both discovery proteomics and targeted proteomics are widely used in biological and biomedical research, whereby the analytical approaches can be broadly divided into proteoform-centric top-down proteomics versus peptide-centric bottom-up proteomics. This chapter outlines the scientific value of top-down proteomics and describes how fluorescence two-dimensional difference gel electrophoresis can be combined with the systematic analysis of crucial post-translational modifications. The concept of on-membrane digestion following the electrophoretic transfer of proteins and the usefulness of comparative two-dimensional immunoblotting are discussed.
    MeSH term(s) Two-Dimensional Difference Gel Electrophoresis/methods ; Proteomics/methods ; Mass Spectrometry ; Proteins/chemistry ; Protein Processing, Post-Translational ; Electrophoresis, Gel, Two-Dimensional/methods
    Chemical Substances Proteins
    Language English
    Publishing date 2022-11-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2831-7_2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Sample Preparation and Protein Determination for 2D-DIGE Proteomics.

    Gargan, Stephen / Ohlendieck, Kay

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2596, Page(s) 325–337

    Abstract: Fluorescence two-dimensional difference gel electrophoresis (2D-DIGE) is a widely employed method for efficient protein separation and the determination of abundance changes in distinct proteoforms. This makes this gel-based method a key technique of ... ...

    Abstract Fluorescence two-dimensional difference gel electrophoresis (2D-DIGE) is a widely employed method for efficient protein separation and the determination of abundance changes in distinct proteoforms. This makes this gel-based method a key technique of comparative approaches in top-down proteomics. For the appropriate screening of proteome-wide alterations, initial preparative steps involve sample handling, homogenization, subcellular fractionation, and the determination of protein concentration, which makes the optimal application of these techniques a crucial part of a successful initiation of a new 2D-DIGE-based analysis. This chapter describes sample homogenization and a standardized protein assay for the preparation of homogenates with a known protein concentration for subsequent differential fluorescent tagging and two-dimensional gel electrophoretic separation.
    MeSH term(s) Two-Dimensional Difference Gel Electrophoresis/methods ; Proteomics/methods ; Electrophoresis, Gel, Two-Dimensional/methods ; Proteome ; Specimen Handling
    Chemical Substances Proteome
    Language English
    Publishing date 2022-11-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2831-7_22
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: DIGE Analysis of Immunodepleted Plasma.

    Dowling, Paul / Ohlendieck, Kay

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2596, Page(s) 363–375

    Abstract: This chapter focuses on upstream immunodepletion of high-abundance proteins from plasma samples and subsequent analysis by fluorescence two-dimensional difference gel electrophoresis (2D-DIGE). The abundances of proteins in biofluid proteomes, such as ... ...

    Abstract This chapter focuses on upstream immunodepletion of high-abundance proteins from plasma samples and subsequent analysis by fluorescence two-dimensional difference gel electrophoresis (2D-DIGE). The abundances of proteins in biofluid proteomes, such as serum, plasma, saliva, and bronchoalveolar lavage fluid (BALF), can exceed ten orders of magnitude. This substantial dynamic range is problematic for the detection of medium and low-abundance proteins by 2D-DIGE analysis. To increase the detection, quantification, and identification of medium-low-abundance proteins, the targeted depletion of known abundant proteins with antibody columns has been successfully employed. From the literature, it is clear that the performance of abundant protein depletion with immunodepletion columns has been successful in broadening the coverage of the biofluid proteome and facilitating the identification of disease-specific biomarkers. The task for a successful biomarker strategy involves the combination of a reproducible and robust fractionation method, coupled with a highly accurate quantitative method, a task that is exemplified by combining both immunodepletion and 2D-DIGE together to discover significant proteins associated with the disease phenotype.
    MeSH term(s) Blood Proteins/analysis ; Proteomics/methods ; Two-Dimensional Difference Gel Electrophoresis/methods ; Proteome/analysis ; Biomarkers ; Electrophoresis, Gel, Two-Dimensional/methods
    Chemical Substances Blood Proteins ; Proteome ; Biomarkers
    Language English
    Publishing date 2022-11-15
    Publishing country United States
    Document type Journal Article
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2831-7_25
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  8. Article: How Can Proteomics Help to Elucidate the Pathophysiological Crosstalk in Muscular Dystrophy and Associated Multi-System Dysfunction?

    Dowling, Paul / Trollet, Capucine / Negroni, Elisa / Swandulla, Dieter / Ohlendieck, Kay

    Proteomes

    2024  Volume 12, Issue 1

    Abstract: This perspective article is concerned with the question of how proteomics, which is a core technique of systems biology that is deeply embedded in the multi-omics field of modern bioresearch, can help us better understand the molecular pathogenesis of ... ...

    Abstract This perspective article is concerned with the question of how proteomics, which is a core technique of systems biology that is deeply embedded in the multi-omics field of modern bioresearch, can help us better understand the molecular pathogenesis of complex diseases. As an illustrative example of a monogenetic disorder that primarily affects the neuromuscular system but is characterized by a plethora of multi-system pathophysiological alterations, the muscle-wasting disease Duchenne muscular dystrophy was examined. Recent achievements in the field of dystrophinopathy research are described with special reference to the proteome-wide complexity of neuromuscular changes and body-wide alterations/adaptations. Based on a description of the current applications of top-down versus bottom-up proteomic approaches and their technical challenges, future systems biological approaches are outlined. The envisaged holistic and integromic bioanalysis would encompass the integration of diverse omics-type studies including inter- and intra-proteomics as the core disciplines for systematic protein evaluations, with sophisticated biomolecular analyses, including physiology, molecular biology, biochemistry and histochemistry. Integrated proteomic findings promise to be instrumental in improving our detailed knowledge of pathogenic mechanisms and multi-system dysfunction, widening the available biomarker signature of dystrophinopathy for improved diagnostic/prognostic procedures, and advancing the identification of novel therapeutic targets to treat Duchenne muscular dystrophy.
    Language English
    Publishing date 2024-01-16
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2720995-7
    ISSN 2227-7382
    ISSN 2227-7382
    DOI 10.3390/proteomes12010004
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Protein Digestion for 2D-DIGE Analysis.

    Murphy, Sandra / Ohlendieck, Kay

    Methods in molecular biology (Clifton, N.J.)

    2022  Volume 2596, Page(s) 339–349

    Abstract: In-gel digestion of protein spots derived from two-dimensional gels and their subsequent identification by mass spectrometry is involved in a multitude of mass spectrometry-driven proteomic experiments, including fluorescence two-dimensional difference ... ...

    Abstract In-gel digestion of protein spots derived from two-dimensional gels and their subsequent identification by mass spectrometry is involved in a multitude of mass spectrometry-driven proteomic experiments, including fluorescence two-dimensional difference gel electrophoresis (2D-DIGE). This type of proteomic methodology has been involved in the establishment of comparative proteome maps and in the identification of differentially expressed proteins and their isoforms in health and disease. Most in-gel digestion protocols follow a number of common steps including excision of the protein spots of interest, destaining, reduction and alkylation (for silver-stained gels), and dehydration and overnight digestion with the proteolytic enzyme of choice. While trypsin has been a mainstay of peptide digestion for many years, it does have its shortcomings, particularly related to incomplete peptide digestion, and this has led to a rise in popularity for other proteolytic enzymes either used alone or in combination. This chapter discusses the alternative enzymes available and describes the process of in-gel digestion using the enzyme trypsin.
    MeSH term(s) Two-Dimensional Difference Gel Electrophoresis/methods ; Proteomics/methods ; Trypsin/metabolism ; Proteolysis ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization/methods ; Proteome/metabolism ; Peptides/metabolism ; Gels ; Electrophoresis, Gel, Two-Dimensional/methods
    Chemical Substances Trypsin (EC 3.4.21.4) ; Proteome ; Peptides ; Gels
    Language English
    Publishing date 2022-11-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ISSN 1940-6029
    ISSN (online) 1940-6029
    DOI 10.1007/978-1-0716-2831-7_23
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Novel proteomic biomarkers for skeletal muscle diseases.

    Ohlendieck, Kay

    Biomarkers in medicine

    2017  Volume 11, Issue 5, Page(s) 409–412

    MeSH term(s) Biomarkers/metabolism ; Humans ; Muscle, Skeletal/metabolism ; Muscular Diseases/metabolism ; Proteomics/methods ; Rhabdomyolysis/metabolism ; Sarcopenia/metabolism
    Chemical Substances Biomarkers
    Language English
    Publishing date 2017-06-07
    Publishing country England
    Document type Editorial ; Research Support, Non-U.S. Gov't
    ZDB-ID 2481014-9
    ISSN 1752-0371 ; 1752-0363
    ISSN (online) 1752-0371
    ISSN 1752-0363
    DOI 10.2217/bmm-2017-0069
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    bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
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