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  1. Book ; Online ; E-Book: Can precision medicine be personal, can personalized medicine be precise?

    Barilan, Yechiel Michael / Brusa, Margherita / Ciechanover, Aaron J.

    2022  

    Abstract: The book provides a multidisciplinary and interdisciplinary discussion of the ethos and ethics of precision/personal medicine, involving scientists who have shaped the field, in dialogue with ethicists, social scientists and philosophers of science. ...

    Author's details edited by Yechiel Michael Barilan, Margherita Brusa, Aaron Ciechanover
    Abstract The book provides a multidisciplinary and interdisciplinary discussion of the ethos and ethics of precision/personal medicine, involving scientists who have shaped the field, in dialogue with ethicists, social scientists and philosophers of science.
    Keywords Medical ethics
    Subject code 174.2
    Language English
    Size 1 online resource (353 pages)
    Publisher Oxford University Press
    Publishing place Oxford, England ; New York, New York
    Document type Book ; Online ; E-Book
    Remark Zugriff für angemeldete ZB MED-Nutzerinnen und -Nutzer
    ISBN 0-19-189591-1 ; 0-19-260867-3 ; 0-19-260868-1 ; 9780198863465 ; 978-0-19-189591-3 ; 978-0-19-260867-3 ; 978-0-19-260868-0 ; 0198863462
    Database ZB MED Catalogue: Medicine, Health, Nutrition, Environment, Agriculture

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  2. Book: Can precision medicine be personal; Can personalized medicine be precise?

    Ciechanover, Aaron / Brusa, Margherita / Barilan, Y. Michael

    2022  

    Author's details Yechiel Michael Barilan was born and educated in Israel. He is an expert in Internal Medicine and js most recently a senior physician in the Covid-19 Dept. and Emergency Dept. Tel Aviv Medical Centre. He is a full professor in the Tel Aviv University School of Medicine, specializing in ethics and social history of medicine. He is also a member of national and international ethics committees and is an author of over a hundred peer reviewed academic publications. Margherita Brusa earned a PhD in bioethics from the University Complutense of Madrid, and a second PhD in paediatric healthcare planning from the University of Padua. She has served in ethics committees in Spain, USA, and Italy, and led the creation of the first ethics committee in the Palestinian Authority. The focus of her research is bioethics and children. Aaron Ciechanover is an Israeli physician and scientist working currently at the Faculty of Medicine of the Technion-Israel Institute of Technology in Haifa, Israel. He
    Size 352 p.
    Publisher Oxford University Press
    Document type Book
    Note PDA Manuell_14
    Format 137 x 214 x 20
    ISBN 9780198863465 ; 0198863462
    Database PDA

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  3. Book: The ubiquitin proteasome proteolytic system

    Ciechanover, Aaron J.

    from classical biochemistry to human diseases

    (Recent advances in human biology ; 9)

    2002  

    Title variant The ubiquitin-proteasome proteolytic system
    Author's details ed. Aaron J. Ciechanover
    Series title Recent advances in human biology ; 9
    Collection
    Keywords Ubiquitin / metabolism ; Cysteine Endopeptidases ; Multienzyme Complexes ; Ubiquitin ; Proteolytic enzymes
    Subject code 572.6
    Language English
    Size XX, 220 S. : Ill.
    Publisher World Scientific
    Publishing place River Edge, NJ u.a.
    Publishing country United States
    Document type Book
    Note Includes bibliographic references and index
    HBZ-ID HT014732827
    ISBN 9812381007 ; 9789812381002
    Database Catalogue ZB MED Medicine, Health

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  4. Article ; Online: Tryptophanyl-Transfer RNA Synthetase Is Involved in a Negative Feedback Loop Mitigating Interferon-γ-Induced Gene Expression.

    Lazar, Ikrame / Livneh, Ido / Ciechanover, Aaron / Fabre, Bertrand

    Cells

    2024  Volume 13, Issue 2

    Abstract: Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes responsible for linking a transfer RNA (tRNA) with its cognate amino acid present in all the kingdoms of life. Besides their aminoacyl-tRNA synthetase activity, it was described that many of these ... ...

    Abstract Aminoacyl-tRNA synthetases (aaRSs) are essential enzymes responsible for linking a transfer RNA (tRNA) with its cognate amino acid present in all the kingdoms of life. Besides their aminoacyl-tRNA synthetase activity, it was described that many of these enzymes can carry out non-canonical functions. They were shown to be involved in important biological processes such as metabolism, immunity, development, angiogenesis and tumorigenesis. In the present work, we provide evidence that tryptophanyl-tRNA synthetase might be involved in a negative feedback loop mitigating the expression of certain interferon-γ-induced genes. Mining the available TCGA and Gtex data, we found that
    MeSH term(s) Humans ; Tryptophan-tRNA Ligase/genetics ; Interferon-gamma/pharmacology ; Feedback ; Melanoma/genetics ; Skin Neoplasms ; Amino Acyl-tRNA Synthetases ; RNA, Transfer ; Gene Expression ; Apolipoprotein L1
    Chemical Substances Tryptophan-tRNA Ligase (EC 6.1.1.2) ; Interferon-gamma (82115-62-6) ; Amino Acyl-tRNA Synthetases (EC 6.1.1.-) ; RNA, Transfer (9014-25-9) ; APOL1 protein, human ; Apolipoprotein L1
    Language English
    Publishing date 2024-01-17
    Publishing country Switzerland
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661518-6
    ISSN 2073-4409 ; 2073-4409
    ISSN (online) 2073-4409
    ISSN 2073-4409
    DOI 10.3390/cells13020180
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Book: Cellular proteolytic systems

    Ciechanover, Aaron J.

    (Modern cell biology ; 15)

    1994  

    Author's details ed. Aaron J. Ciechanover
    Series title Modern cell biology ; 15
    Collection
    Keywords Proteins / metabolism ; Lysosomes / physiology ; Ubiquitin / physiology ; Ubiquitin ; Zelle ; Proteasen
    Subject EC 3.4 ; Proteinasen ; Peptidasen ; Proteolytisches Enzym ; Peptid-Hydrolasen ; ATP-abhängiger Proteolysefaktor 1
    Language English
    Size X, 233 S. : Ill., graph. Darst.
    Publisher Wiley-Liss
    Publishing place New York u.a.
    Publishing country United States
    Document type Book
    HBZ-ID HT006634715
    ISBN 0-471-02189-X ; 978-0-471-02189-6
    Database Catalogue ZB MED Medicine, Health

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  6. Article ; Online: Intracellular protein degradation: From a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting.

    Ciechanover, Aaron

    Best practice & research. Clinical haematology

    2017  Volume 30, Issue 4, Page(s) 341–355

    Abstract: Between the 1950s and 1980s, scientists were focusing mostly on how the genetic code is transcribed to RNA and translated to proteins, but how proteins are degraded has remained a neglected research area. With the discovery of the lysosome by Christian ... ...

    Abstract Between the 1950s and 1980s, scientists were focusing mostly on how the genetic code is transcribed to RNA and translated to proteins, but how proteins are degraded has remained a neglected research area. With the discovery of the lysosome by Christian de Duve it was assumed that cellular proteins are degraded within this organelle. Yet, several independent lines of experimental evidence strongly suggested that intracellular proteolysis is largely non-lysosomal, but the mechanisms involved remained obscure. The discovery of the ubiquitin-proteasome system resolved the enigma. We now recognize that degradation of intracellular proteins is involved in regulation of a broad array of cellular processes, such as cell cycle and division, regulation of transcription factors, and assurance of the cellular quality control. Not surprisingly, aberrations in the system have been implicated in the pathogenesis of human disease, such as malignancies and neurodegenerative disorders, which led subsequently to an increasing effort to develop mechanism-based drugs.
    MeSH term(s) Animals ; Cell Cycle ; Humans ; Lysosomes/metabolism ; Lysosomes/pathology ; Neoplasms/metabolism ; Neoplasms/pathology ; Neoplasms/therapy ; Neurodegenerative Diseases/metabolism ; Neurodegenerative Diseases/pathology ; Neurodegenerative Diseases/therapy ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Ubiquitin/metabolism
    Chemical Substances Ubiquitin ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2017-09-22
    Publishing country Netherlands
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 2048027-1
    ISSN 1532-1924 ; 1521-6926
    ISSN (online) 1532-1924
    ISSN 1521-6926
    DOI 10.1016/j.beha.2017.09.001
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: The unravelling of the ubiquitin system.

    Ciechanover, Aaron

    Nature reviews. Molecular cell biology

    2015  Volume 16, Issue 5, Page(s) 322–324

    Abstract: Today, many scientific discoveries are made using a top-down experimental approach. The ubiquitin system was discovered using a 'classic' bottom-up approach to tackle the question: 'how are cellular proteins selectively degraded?' A simple proteolytic ... ...

    Abstract Today, many scientific discoveries are made using a top-down experimental approach. The ubiquitin system was discovered using a 'classic' bottom-up approach to tackle the question: 'how are cellular proteins selectively degraded?' A simple proteolytic assay, which used a crude cell-extract, was all that was required to address this question; it was followed by fractionation and reconstitution experiments to decipher the role of the components in this multi-step process. This 'biochemistry at its best' approach, which was published in a periodical that today would not be regarded as highly visible, provided magnificent findings.
    MeSH term(s) Animals ; Humans ; Lysosomes/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Proteolysis ; Reticulocytes/metabolism ; Ubiquitin/chemistry ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligase Complexes/metabolism
    Chemical Substances Ubiquitin ; Ubiquitin-Protein Ligase Complexes (EC 2.3.2.23) ; Proteasome Endopeptidase Complex (EC 3.4.25.1)
    Language English
    Publishing date 2015
    Publishing country England
    Document type Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2031313-5
    ISSN 1471-0080 ; 1471-0072
    ISSN (online) 1471-0080
    ISSN 1471-0072
    DOI 10.1038/nrm3982
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: A possible non-proteolytic role of ubiquitin conjugation in alleviating the pathology of Huntingtin's aggregation.

    Ziv, Noam E / Ciechanover, Aaron

    Cell death and differentiation

    2020  Volume 28, Issue 2, Page(s) 814–817

    MeSH term(s) Animals ; Humans ; Huntington Disease/metabolism ; Huntington Disease/pathology ; Ubiquitin/metabolism ; Ubiquitination
    Chemical Substances Ubiquitin
    Language English
    Publishing date 2020-09-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1225672-9
    ISSN 1476-5403 ; 1350-9047
    ISSN (online) 1476-5403
    ISSN 1350-9047
    DOI 10.1038/s41418-020-00617-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: A conversation with Aaron Ciechanover. Interview by Ushma S. Neill.

    Ciechanover, Aaron

    The Journal of clinical investigation

    2013  Volume 123, Issue 10, Page(s) 4093–4094

    MeSH term(s) Biochemistry/history ; History, 20th Century ; History, 21st Century ; Israel ; Massachusetts ; Nobel Prize ; Proteolysis
    Language English
    Publishing date 2013-10-01
    Publishing country United States
    Document type Autobiography ; Biography ; Historical Article ; Interview ; Portrait
    ZDB-ID 3067-3
    ISSN 1558-8238 ; 0021-9738
    ISSN (online) 1558-8238
    ISSN 0021-9738
    DOI 10.1172/JCI71859
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Stress-Induced Proteasome Sub-Cellular Translocation in Cardiomyocytes Causes Altered Intracellular Calcium Handling and Arrhythmias.

    Neeman-Egozi, Shunit / Livneh, Ido / Dolgopyat, Irit / Nussinovitch, Udi / Milman, Helena / Cohen, Nadav / Eisen, Binyamin / Ciechanover, Aaron / Binah, Ofer

    International journal of molecular sciences

    2024  Volume 25, Issue 9

    Abstract: The ubiquitin-proteasome system (UPS) is an essential mechanism responsible for the selective degradation of substrate proteins via their conjugation with ubiquitin. Since cardiomyocytes have very limited self-renewal capacity, as they are prone to ... ...

    Abstract The ubiquitin-proteasome system (UPS) is an essential mechanism responsible for the selective degradation of substrate proteins via their conjugation with ubiquitin. Since cardiomyocytes have very limited self-renewal capacity, as they are prone to protein damage due to constant mechanical and metabolic stress, the UPS has a key role in cardiac physiology and pathophysiology. While altered proteasomal activity contributes to a variety of cardiac pathologies, such as heart failure and ischemia/reperfusion injury (IRI), the environmental cues affecting its activity are still unknown, and they are the focus of this work. Following a recent study by Ciechanover's group showing that amino acid (AA) starvation in cultured cancer cell lines modulates proteasome intracellular localization and activity, we tested two hypotheses in human induced pluripotent stem cell-derived cardiomyocytes (iPSC-CMs, CMs): (i) AA starvation causes proteasome translocation in CMs, similarly to the observation in cultured cancer cell lines; (ii) manipulation of subcellular proteasomal compartmentalization is associated with electrophysiological abnormalities in the form of arrhythmias, mediated via altered intracellular Ca
    MeSH term(s) Myocytes, Cardiac/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Humans ; Calcium/metabolism ; Animals ; Arrhythmias, Cardiac/metabolism ; Arrhythmias, Cardiac/etiology ; Induced Pluripotent Stem Cells/metabolism ; Stress, Physiological ; Protein Transport ; Rats ; Amino Acids/metabolism
    Chemical Substances Proteasome Endopeptidase Complex (EC 3.4.25.1) ; Calcium (SY7Q814VUP) ; Amino Acids
    Language English
    Publishing date 2024-04-30
    Publishing country Switzerland
    Document type Journal Article
    ZDB-ID 2019364-6
    ISSN 1422-0067 ; 1422-0067 ; 1661-6596
    ISSN (online) 1422-0067
    ISSN 1422-0067 ; 1661-6596
    DOI 10.3390/ijms25094932
    Database MEDical Literature Analysis and Retrieval System OnLINE

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