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  • 1
    Online Resource
    Online Resource
    Singapore :Springer Singapore Pte. Limited,
    Keywords: Peroxisomes. ; Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (488 pages)
    Edition: 1st ed.
    ISBN: 9789811322334
    Series Statement: Subcellular Biochemistry Series ; v.89
    Language: English
    Note: Intro -- Preface -- References -- Contents -- Mass Spectrometry-Based Organelle Proteomics -- 1 Proteome of Plant Peroxisomes -- Abstract -- 1 Introduction -- 2 MS-Based Peroxisome Proteome Studies in Plants -- 3 An Update on Arabidopsis Peroxisome Proteins and Their Functions -- 3.1 Biogenesis and Dynamics of Peroxisomes -- 3.2 Fatty Acid Catabolism and Hormone Biosynthesis -- 3.3 Photorespiration -- 3.4 The Glyoxylate Cycle -- 3.5 Detoxification of ROS and Methylglyoxal -- 3.6 Biosynthesis of Phylloquinone, Biotin and CoA -- 3.7 The Mevalonic Acid (MVA) Pathway -- 3.8 Catabolism of Polyamines, Urate, Pseudouridine and Sulfite -- 3.9 Amino Acid Metabolism -- 3.10 Pathogen Response -- 3.11 Metabolism of NADPH and NADH -- 3.12 Peroxisomal Transporters for Metabolites and Cofactors -- 3.13 Nucleotide Homeostasis -- 3.14 Phosphoregulation -- 3.15 Molecular Chaperones and Proteases -- 3.16 Other Peroxisomal Proteins -- 4 Conclusions and Perspectives -- Acknowledgements -- References -- 2 Defining the Mammalian Peroxisomal Proteome -- Abstract -- 1 Introduction -- 2 Mass Spectrometry-Based Studies of Mammalian Peroxisomes -- 3 Definition of the Mammalian Peroxisomal Proteome -- 3.1 Proteins That Are Detected in High Frequency in Peroxisomal Fractions -- 3.2 Proteins That Are Detected in Low Frequency in Peroxisomal Fractions -- 4 Conclusions -- Acknowledgements -- References -- 3 Fungal Peroxisomes Proteomics -- Abstract -- 1 Introduction -- 2 Organellar Proteomics on Peroxisomes in Fungi -- 2.1 Organellar Proteomics on Peroxisomes from S. Cerevisiae -- 2.2 The Proteome of Peroxisomes in N. Crassa -- 2.3 Identification of Peroxisomal Matrix Proteins in P. Chrysogenum -- 3 Perspectives -- Acknowledgements -- References -- 4 The Craft of Peroxisome Purification-A Technical Survey Through the Decades -- Abstract -- 1 Introduction. , 2 Isolation of PO from Liver and Kidney -- 2.1 Liver Peroxisomes -- 2.2 Kidney Peroxisomes -- 3 Peroxisome Isolation from Brain Tissue-A Still Unsolved Problem -- 4 Peroxisome Isolation from Yeast and Other Fungi -- 5 Peroxisome/Glyoxysome Purification from Plants -- 6 The Limits of Density Gradient Centrifugation-The Development of Alternative Purification Techniques -- 7 The Era of Proteomics-Opposing Approaches to Characterize Organelle Proteomes -- 8 Challenges for the Future -- Acknowledgements -- References -- Predicting Peroxisomal Proteomes -- 5 Prediction of Peroxisomal Matrix Proteins in Plants -- Abstract -- 1 Prediction of PTS1 Proteins -- 1.1 Canonical Versus Non-canonical PTS1s -- 1.2 Prediction Algorithms for PTS1 Proteins -- 1.3 Prediction and Analysis of Peroxisome Targeting Efficiency -- 2 PTS2 Nonapeptide Definition and Prediction of PTS2 Proteins -- 3 Conclusions and Future Perspectives -- References -- 6 The Obvious and the Hidden: Prediction and Function of Fungal Peroxisomal Matrix Proteins -- Abstract -- 1 Peroxisomes in Fungi -- 2 Predicting Peroxisomal Proteins -- 3 Cryptic Peroxisomal Proteins -- 3.1 Weak Peroxisomal Targeting Signals Promote Dual Targeting -- 3.2 Differential Splicing and More: Alternative Transcripts Encoding Peroxisomal Isoforms -- 3.3 Translational Stop Codon Readthrough: A Widely Conserved Mechanism to Create Peroxisomal Isoforms -- 3.4 Peroxisomal Matrix Proteins Without PTS: The Really Hidden Ones -- 4 Dual Targeting Reveals a Broader Metabolic Capacity of Fungal Peroxisomes -- References -- 7 Predicting Peroxisomal Targeting Signals to Elucidate the Peroxisomal Proteome of Mammals -- Abstract -- 1 Introduction -- 2 Elucidation of the Peroxisomal Proteome -- 3 Predicting the Peroxisomal Proteome -- 3.1 Concept -- 3.2 Peroxisomal Protein Transport -- 3.3 Peroxisomal Targeting Signals. , 3.3.1 Targeting Signals for Matrix Proteins -- 3.3.2 Targeting Signals for Membrane Proteins -- 3.4 Computational Algorithms to Predict the Subcellular Localization of Proteins -- 3.4.1 Prediction Algorithms to Identify Targeting Signals -- Prediction Algorithms Based on the Conservation Pattern at Individual Positions of the Targeting Signal -- Generating Prediction Algorithms for Targeting Signals by Combining Various Properties and Considering the Context -- 3.4.2 Prediction Algorithms to Classify Proteins into Groups Sharing the Same Subcellular Compartment -- 3.5 Available Prediction Algorithms for the Identification of Peroxisomal Proteins -- 3.5.1 Prediction Algorithms for Targeting Signals -- 3.5.2 Prediction Algorithms Based on Classifiers Using General Properties of Peroxisomal Proteins -- 4 Strengths and Weaknesses of Prediction Algorithms -- 4.1 General Considerations -- 4.2 Incorrect Predictions Based on the Limitations of the Algorithm -- 4.3 Biological Background of the Misevaluation -- 4.4 Evaluation of the Quality of Prediction Algorithms -- 5 Prediction of the Peroxisomal Proteome -- 6 Summary and Outlook -- Acknowledgements -- References -- 8 Multiple Localization by Functional Translational Readthrough -- Abstract -- 1 Dual and Multiple Targeting of Proteins -- 2 Dual and Multiple Targeting to the Peroxisome and Other Organelles -- 3 Identifying the PTS1ome by Bioinformatics -- 4 The Hierarchy of Targeting Signals -- 5 Translational Readthrough -- 6 Functional Translational Readthrough Diversifies Protein Function -- 7 Functional Translational Readthrough Diversifies Protein Targeting -- 8 Omics Approaches for the Identification of Readthrough Proteins -- 9 Readthrough-Omics in Silico -- 10 Translational Readthrough as a Modification of the Genetic Code -- 11 The Physiology of Peroxisomal Malate and Lactate Dehydrogenases. , Acknowledgements -- References -- 9 Evolution of the Peroxisomal Proteome -- Abstract -- 1 Introduction -- 2 Functional Diversity of Extant Peroxisomes -- 3 Diverse but All the Same -- 4 Evolutionary Origin of Peroxisomes -- 5 Current Hypotheses on the Origin of the Peroxisome -- 6 Shaping the Peroxisomal Proteome Through Subcellular Retargeting -- 7 Secondary Loss of Peroxisomes -- 8 Concluding Remarks -- Acknowledgements -- References -- 10 Peroxisome Protein Prediction in Drosophila melanogaster -- Abstract -- 1 Introduction: Drosophila Has Been Used in the Laboratory for over 100 Years -- 2 Early Studies of Drosophila Peroxisomal Proteins -- 2.1 Analysis of Potential Peroxisome Enzymes in Drosophila Organs -- 2.2 Release of the Drosophila Genome Sequence and Peroxisome Protein Predictions -- 3 Systematic Analysis of the Drosophila Peroxisome Proteome -- 3.1 Identification of Drosophila Peroxisome Biogenesis Protein Homologs -- 3.2 Functional Characterization of Predicted Drosophila Pex Proteins -- 3.3 Drosophila Does not Seem to Employ PTS2 Mediated Protein Trafficking -- 3.4 Conservation of Drosophila Peroxisome Membrane Protein (PMP) Trafficking -- 3.5 Drosophila Peroxisome Matrix Proteins -- 4 The Effects of Overexpressing Drosophila Peroxisome Proteins -- 5 Screening for Peroxisome-Associated Proteins  in Drosophila -- 5.1 Large Scale Screens for Novel Protein Interactions -- 5.2 Proteins Regulating Peroxisome Dynamics in Drosophila S2 Cells -- 6 Developing Drosophila as a Model for Human Peroxisome Biogenesis Disorders -- 6.1 Phenotypes Associated with Defective Peroxisome Biogenesis in Drosophila -- 6.2 Analysis of the Drosophila Whole-Animal Response to Pex1 Deficiency -- 6.3 Modelling Single Peroxisome Enzyme Deficiencies Using Drosophila -- 7 Identification of Novel Peroxisome Functions Using Drosophila -- 8 Summary -- References. , Analysis of Peroxisome Proteome Interaction Networks -- 11 Using Pull Down Strategies to Analyze the Interactome of Peroxisomal Membrane Proteins in Human Cells -- Abstract -- 1 Membrane Protein Complexes in Human Peroxisomes -- 1.1 Biogenesis I-de Novo Formation, Proliferation and Division -- 1.2 Biogenesis II-Membrane and Matrix Protein Import -- 1.3 PMPs with Other Functions -- 1.3.1 Metabolite Transport -- 1.3.2 Inter-Organelle Contact Sites -- 1.3.3 Novel Functions of PMPs -- 2 Proteomic Strategies Applied to the Characterization of PMPs from Human Cells -- 2.1 MS-Based Methods for the Characterization of Human PMP Complexes -- 2.1.1 Affinity Purification Combined with High-Resolution Mass Spectrometry (AP-MS) -- 2.1.2 Proximity-Dependent Biotin Identification (BioID) -- 2.2 Critical Aspects to Consider for Experimental Design -- 3 Towards a PMP Interactome -- 3.1 The PEX14 Complex Analysis Revisited -- 3.2 PEX16 Interactome Defined by BioID -- 3.3 Comparing the Peroxin Network of Yeast and Man -- 4 Outlook -- Acknowledgements -- References -- 12 Identification of Peroxisomal Protein Complexes with PTS Receptors, Pex5 and Pex7, in Mammalian Cells -- Abstract -- 1 Introduction -- 2 Approaches to Identifying Peroxisomal Protein Import Complexes in Mammalian Cells -- 3 Identification of Peroxisomal Protein Complexes by Immunoprecipitation -- 3.1 Complexes with PTS1 Receptor Pex5 -- 3.2 Complexes with PTS2 Receptor Pex7 -- 3.3 Substrates of Intraperoxisomal Processing Enzyme, Tysnd1 -- 4 Biochemical Purification of Awp1 -- 5 Concluding Remarks -- Acknowledgements -- References -- 13 Unraveling of the Structure and Function of Peroxisomal Protein Import Machineries -- Abstract -- 1 Peroxisomal Protein Import -- 2 Peroxisomal Matrix Protein Import -- 2.1 Cargo Recognition -- 2.1.1 Pre-import Complexes -- 2.2 Docking at the Peroxisomal Membrane. , 2.3 Peroxisomal Import Pores.
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  • 2
    Online Resource
    Online Resource
    Wiesbaden :Springer Vieweg. in Springer Fachmedien Wiesbaden GmbH,
    Keywords: Electronic books.
    Type of Medium: Online Resource
    Pages: 1 online resource (69 pages)
    Edition: 1st ed.
    ISBN: 9783658365448
    Series Statement: Essentials Series
    Language: German
    Note: Intro -- Was Sie in diesem essential finden können -- Vorwort -- Danksagungen -- Inhaltsverzeichnis -- Tabellenverzeichnis -- 1 Zielsetzung und Planung -- 1.1 Vorgaben und Bearbeitungsumfang -- 1.1.1 Vorgaben durch Bologna -- 1.1.2 Dauer und Umfang -- 1.1.3 Individuelle Zielvorstellungen -- 1.2 Thema und Exposé -- 1.2.1 Themenfindung und Betreuung -- 1.2.2 Ziele und Exposé -- 1.3 Projektplanung -- 1.3.1 Zeitplan und Meilensteine -- 1.3.2 Berichte, Verlängerung -- 1.4 Formale Rahmenbedingungen -- 1.4.1 Anmeldung und Prüfer:innen -- 1.4.2 Deutsch oder Englisch? -- 1.4.3 Geheimhaltung -- 2 Strukturierung verstehen -- 2.1 Konzept und Gliederung -- 2.1.1 Umfang -- 2.1.2 Lesefluss einer naturwissenschaftlichen Arbeit -- 2.1.3 Prinzipieller Aufbau -- 2.1.4 Empfohlene Gliederung -- 2.2 Eingangsübersicht -- 2.2.1 Titelblatt -- 2.2.2 Wissenschaftliche Danksagung, ggf. Vorbemerkungen -- 2.2.3 Inhaltsverzeichnis sowie Zusammenfassung/Abstract -- 2.3 Hauptteil -- 2.3.1 Einleitung und Aufgabenstellung -- 2.3.2 Experimentalteil -- 2.3.3 Ergebnisse und Diskussion -- 2.3.4 Schlussfolgerungen -- 2.4 Verzeichnisse und Anhang -- 2.4.1 Literaturverzeichnis, Zitierweise -- 2.4.2 Weitere Verzeichnisse und ergänzende Daten -- 2.4.3 Persönliche Erklärung -- 3 Bausteine erstellen -- 3.1 Rahmenbedingungen und Ressourcen -- 3.1.1 Software, Apps, Programme -- 3.1.2 Hardware und Sicherungskopien -- 3.1.3 Arbeitsorte -- 3.2 Zentrale Bausteine -- 3.2.1 Text -- 3.2.2 Abbildungen -- 3.2.3 Tabellen -- 3.3 Ergänzende Bausteine -- 3.3.1 Literaturzitate -- 3.3.2 Verzeichnisse -- 4 Fertigstellen und Abschluss -- 4.1 Finale Schreibphase -- 4.1.1 Arbeitsrollen -- 4.1.2 Probleme oder Störungen -- 4.2 Checklisten Hauptteil -- 4.2.1 Übergeordnete Checkliste -- 4.2.2 Checkliste Einleitung -- 4.2.3 Checkliste Experimentalteil -- 4.2.4 Checkliste Ergebnisteil und Diskussion. , 4.2.5 Checkliste Fazit/Conclusion -- 4.3 Checklisten für umgebende Elemente -- 4.3.1 Checklisten Titel, Abstrakt und Struktur -- 4.3.2 Checklisten zu Verzeichnissen -- 4.4 Abgabe Ihrer Arbeit -- 5 Nach der Abgabe -- 5.1 Prüfungsvortrag -- 5.2 Bewertung Ihrer Arbeit -- 5.2.1 Bewertungsvorgang -- 5.2.2 Plagiatsprüfung -- 5.2.3 Bewertungskriterien -- 5.3 Veröffentlichung Ihrer Arbeit -- Was Sie aus diesem essential mitnehmen können -- Literatur -- Stichwortverzeichnis.
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  • 3
    Keywords: Cytology ; Cytology ; Proteomics ; Biochemistry ; Human genetics ; Cell physiology ; Biochemistry ; Human genetics ; Cell physiology ; Proteomics ; Cell biology. ; Plant biochemistry. ; Peroxisomes ; Proteomics methods
    Description / Table of Contents: This new edited volume in the Springer Subcellular Biochemistry Series presents a comprehensive, state-of-the-art overview of the proteomics of peroxisomes derived from mammalian, Drosophila, fungal, and plant origin, andcontains contributions from leading experts in the field. The development of sensitive proteomics and mass spectrometry technologies, combined with bioinformatics approaches now allow the identification of low-abundance and transient peroxisomal proteins and permits to identify the complete proteome of peroxisomes, with the consequent increase of our knowledge of the metabolic and regulatory networks of these important cellular organelles. The book lines-up with these developments and is organized in four sections including: (i) mass spectrometry-based organelle proteomics; (ii) prediction of peroxisomal proteomes; (iii) analysis of peroxisome proteome interaction networks; and (iv) peroxisomes in relation to other subcellular compartments. The editor Luis A. del Río is Professor ad honorem of the Spanish National Research Council (CSIC) in the Group of Antioxidants, Free Radicals and Nitric Oxide in Biotechnology, Food and Agriculture, Department of Biochemistry and Cell & Molecular Biology of Plants, at the Estación Experimental del Zaidín, Granada, Spain. Del Río’s research group focuses on the metabolism of reactive oxygen species (ROS), reactive nitrogen species (RNS) and antioxidants in plant peroxisomes, and the ROS- and RNS-dependent role of peroxisomes in plant cell signalling. The editor Michael Schrader is Professor of Cell Biology & Cytopathology in the Department of Biosciences at the University of Exeter, UK. Using mammalian peroxisomes as model organelles, Prof. Schrader and his team aim to unravel the molecular machinery and signalling pathways that mediate and regulate the formation, dynamics and abundance of these medically relevant cellular compartments
    Type of Medium: Online Resource
    Pages: Online-Ressource (XIII, 493 p. 55 illus., 49 illus. in color, online resource)
    Edition: Springer eBook Collection. Biomedical and Life Sciences
    ISBN: 9789811322334
    Series Statement: Subcellular Biochemistry volume 89
    Language: English
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  • 4
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 804 (1996), S. 0 
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The immunofluorescence technique has become an important tool for the investigation of peroxisomes in cell culture. We have used this method for the study of peroxisomes in the human hepatoblastoma cell line HepG2. A marked heterogeneity of peroxisomal forms was detected. Besides spherical (about 100 nm) and rod-shaped structures (about 300 nm) many elongated, undulating tubular forms (up to 5 μm) were found. Further observations indicate that the appearance of the peroxisomal forms in immunofluorescence is dependent on the fixation procedure used. Whereas the fixation with methanol-acetone (−20°C) or ethanol results in a punctate pattern with spherical particles, the use of formaldehyde/Triton X-100 fixation shows well-preserved tubules and rods. These observations may be of special importance for studies on the biogenesis of peroxisomes.
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 1573-6865
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The immunofluorescence technique has become an important tool for the investigation of peroxisomes in cell culture. We have used this method for the study of peroxisomes in the human hepatoblastoma cell line HepG2. A marked heterogeneity of peroxisomal forms was detected. Besides spherical (about 100 nm) and rod-shaped structures (about 300 nm) many elongated, undulating tubular forms (up to 5 μm) were found. Further observations indicate that the appearance of the peroxisomal forms in immunofluorescence is dependent on the fixation procedure used. Whereas the fixation with methanol-acetone (−20°C) or ethanol results in a punctate pattern with spherical particles, the use of formaldehyde/Triton X-100 fixation shows well-preserved tubules and rods. These observations may be of special importance for studies on the biogenesis of peroxisomes.
    Type of Medium: Electronic Resource
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