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  1. Article ; Online: Noboru Mizushima: All about autophagy. Interview by Caitlin Sedwick.

    Mizushima, Noboru

    The Journal of cell biology

    2010  Volume 190, Issue 6, Page(s) 946–947

    MeSH term(s) Animals ; Autophagy ; Cell Biology/history ; History, 20th Century ; History, 21st Century ; Japan ; Mice
    Language English
    Publishing date 2010-09-13
    Publishing country United States
    Document type Autobiography ; Biography ; Historical Article ; Interview ; Portrait
    ZDB-ID 218154-x
    ISSN 1540-8140 ; 0021-9525
    ISSN (online) 1540-8140
    ISSN 0021-9525
    DOI 10.1083/jcb.1906pi
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: Featuring...Dr. Noboru Mizushima Winner of the 2007 FEBS Letters Young Scientist Award. Interview by Daniela Ruffell.

    Mizushima, Noboru

    FEBS letters

    2007  Volume 581, Issue 15, Page(s) 2750

    MeSH term(s) Animals ; Autophagy/physiology ; Awards and Prizes ; Cell Line ; Cell Size ; Europe ; Humans ; Societies, Scientific
    Language English
    Publishing date 2007-06-19
    Publishing country England
    Document type Interview
    ZDB-ID 212746-5
    ISSN 1873-3468 ; 0014-5793
    ISSN (online) 1873-3468
    ISSN 0014-5793
    DOI 10.1016/j.febslet.2007.04.026
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Ubiquitin in autophagy and non-protein ubiquitination.

    Mizushima, Noboru

    Nature structural & molecular biology

    2024  Volume 31, Issue 2, Page(s) 208–209

    MeSH term(s) Ubiquitin/metabolism ; Ubiquitination ; Signal Transduction ; Autophagy ; Ubiquitin-Protein Ligases/metabolism
    Chemical Substances Ubiquitin ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
    Language English
    Publishing date 2024-02-16
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-024-01217-6
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: SnapShot: Organelle degradation.

    Mizushima, Noboru

    Molecular cell

    2022  Volume 82, Issue 8, Page(s) 1604–1604.e1

    Abstract: Organelles are continuously turned over as part of cellular homeostasis and adaptation. Most organelles, even including the nucleus, are degraded by lysosomes via different pathways, such as macroautophagy, microautophagy, organelle-derived vesicle ... ...

    Abstract Organelles are continuously turned over as part of cellular homeostasis and adaptation. Most organelles, even including the nucleus, are degraded by lysosomes via different pathways, such as macroautophagy, microautophagy, organelle-derived vesicle degradation, and crinophagy. In some specific cases-for example, in lens fiber cells-organelles are degraded by cytosolic phospholipases. To view this SnapShot, open or download the PDF.
    MeSH term(s) Autophagy ; Cytosol ; Lens, Crystalline/metabolism ; Lysosomes ; Organelles/metabolism
    Language English
    Publishing date 2022-04-22
    Publishing country United States
    Document type Journal Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2022.03.015
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: SnapShot: Organelle degradation

    Mizushima, Noboru

    Molecular cell. 2022 Apr. 21, v. 82, no. 8

    2022  

    Abstract: Organelles are continuously turned over as part of cellular homeostasis and adaptation. Most organelles, even including the nucleus, are degraded by lysosomes via different pathways, such as macroautophagy, microautophagy, organelle-derived vesicle ... ...

    Abstract Organelles are continuously turned over as part of cellular homeostasis and adaptation. Most organelles, even including the nucleus, are degraded by lysosomes via different pathways, such as macroautophagy, microautophagy, organelle-derived vesicle degradation, and crinophagy. In some specific cases—for example, in lens fiber cells—organelles are degraded by cytosolic phospholipases. To view this SnapShot, open or download the PDF.
    Keywords homeostasis ; lysosomes ; macroautophagy ; phospholipases
    Language English
    Dates of publication 2022-0421
    Size p. 1604-1604.e1.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1415236-8
    ISSN 1097-4164 ; 1097-2765
    ISSN (online) 1097-4164
    ISSN 1097-2765
    DOI 10.1016/j.molcel.2022.03.015
    Database NAL-Catalogue (AGRICOLA)

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  6. Article ; Online: Ubiquitination of non-protein substrates.

    Sakamaki, Jun-Ichi / Mizushima, Noboru

    Trends in cell biology

    2023  Volume 33, Issue 11, Page(s) 991–1003

    Abstract: The covalent attachment of ubiquitin is a common regulatory mechanism in various proteins. Although it has long been thought that the substrates of ubiquitination are limited to proteins, recent studies have changed this view: ubiquitin can be conjugated ...

    Abstract The covalent attachment of ubiquitin is a common regulatory mechanism in various proteins. Although it has long been thought that the substrates of ubiquitination are limited to proteins, recent studies have changed this view: ubiquitin can be conjugated to lipids, sugars, and nucleotides. Ubiquitin is linked to these substrates by the action of different classes of ubiquitin ligases that have distinct catalytic mechanisms. Ubiquitination of non-protein substrates likely serves as a signal for the recruitment of other proteins to bring about specific effects. These discoveries have expanded the concept of ubiquitination and have advanced our insight into the biology and chemistry of this well-established modification process. In this review we describe the molecular mechanisms and roles of non-protein ubiquitination and discuss the current limitations.
    Language English
    Publishing date 2023-04-27
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 30122-x
    ISSN 1879-3088 ; 0962-8924
    ISSN (online) 1879-3088
    ISSN 0962-8924
    DOI 10.1016/j.tcb.2023.03.014
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: ER-Phagy: Quality and Quantity Control of the Endoplasmic Reticulum by Autophagy.

    Chino, Haruka / Mizushima, Noboru

    Cold Spring Harbor perspectives in biology

    2023  Volume 15, Issue 1

    Abstract: The endoplasmic reticulum (ER) is the largest organelle and has multiple roles in various cellular processes such as protein secretion, lipid synthesis, calcium storage, and organelle biogenesis. The quantity and quality of this organelle are controlled ... ...

    Abstract The endoplasmic reticulum (ER) is the largest organelle and has multiple roles in various cellular processes such as protein secretion, lipid synthesis, calcium storage, and organelle biogenesis. The quantity and quality of this organelle are controlled by the ubiquitin-proteasome system and autophagy (termed "ER-phagy"). ER-phagy is defined as the degradation of part of the ER by the vacuole or lysosomes, and there are at least two types of ER-phagy: macro-ER-phagy and micro-ER-phagy. In macro-ER-phagy, ER fragments are enclosed by autophagosomes, which is mediated by ER-phagy receptors. In micro-ER-phagy, a portion of the ER is engulfed directly by the vacuole or lysosomes. In these two pathways, some proteins in the ER lumen can be recognized selectively and subjected to ER-phagy. This review summarizes our current knowledge of ER-phagy, focusing on its membrane dynamics, molecular mechanisms, substrate specificity, and physiological significance.
    MeSH term(s) Endoplasmic Reticulum Stress/physiology ; Endoplasmic Reticulum/metabolism ; Autophagy/physiology ; Carrier Proteins/metabolism ; Lysosomes/metabolism
    Chemical Substances Carrier Proteins
    Language English
    Publishing date 2023-01-03
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ISSN 1943-0264
    ISSN (online) 1943-0264
    DOI 10.1101/cshperspect.a041256
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Cell biology of protein-lipid conjugation.

    Sakamaki, Jun-Ichi / Mizushima, Noboru

    Cell structure and function

    2023  Volume 48, Issue 1, Page(s) 99–112

    Abstract: Protein-lipid conjugation is a widespread modification involved in many biological processes. Various lipids, including fatty acids, isoprenoids, sterols, glycosylphosphatidylinositol, sphingolipids, and phospholipids, are covalently linked with proteins. ...

    Abstract Protein-lipid conjugation is a widespread modification involved in many biological processes. Various lipids, including fatty acids, isoprenoids, sterols, glycosylphosphatidylinositol, sphingolipids, and phospholipids, are covalently linked with proteins. These modifications direct proteins to intracellular membranes through the hydrophobic nature of lipids. Some of these membrane-binding processes are reversible through delipidation or by reducing the affinity to membranes. Many signaling molecules undergo lipid modification, and their membrane binding is important for proper signal transduction. The conjugation of proteins to lipids also influences the dynamics and function of organellar membranes. Dysregulation of lipidation has been associated with diseases such as neurodegenerative diseases. In this review, we first provide an overview of diverse forms of protein-lipid conjugation and then summarize the catalytic mechanisms, regulation, and roles of these modifications.Key words: lipid, lipidation, membrane, organelle, protein modification.
    MeSH term(s) Proteins ; Fatty Acids/metabolism ; Phospholipids/metabolism ; Lipid Metabolism ; Sterols/metabolism ; Cell Membrane/metabolism
    Chemical Substances Proteins ; Fatty Acids ; Phospholipids ; Sterols
    Language English
    Publishing date 2023-04-06
    Publishing country Japan
    Document type Review ; Journal Article
    ZDB-ID 197293-5
    ISSN 1347-3700 ; 0386-7196
    ISSN (online) 1347-3700
    ISSN 0386-7196
    DOI 10.1247/csf.23016
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: The autophagy pathway beyond model organisms: an evolutionary perspective.

    Zhang, Sidi / Mizushima, Noboru

    Autophagy

    2022  Volume 19, Issue 1, Page(s) 1–2

    Abstract: In this issue, we answer a frequently asked question regarding the evolution of the macroautophagy/autophagy pathway. ...

    Abstract In this issue, we answer a frequently asked question regarding the evolution of the macroautophagy/autophagy pathway.
    MeSH term(s) Autophagy
    Language English
    Publishing date 2022-12-06
    Publishing country United States
    Document type Editorial ; Research Support, Non-U.S. Gov't
    ZDB-ID 2454135-7
    ISSN 1554-8635 ; 1554-8627
    ISSN (online) 1554-8635
    ISSN 1554-8627
    DOI 10.1080/15548627.2022.2153568
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Protocol to purify and detect ubiquitinated phospholipids in budding yeast and human cell lines

    Jun-ichi Sakamaki / Noboru Mizushima

    STAR Protocols, Vol 4, Iss 1, Pp 101935- (2023)

    1480  

    Abstract: Summary: Ubiquitin is covalently conjugated to phospholipids as well as proteins; however, ubiquitinated phospholipids are less abundant than free ubiquitin and ubiquitinated proteins. Here, we describe protocols to purify ubiquitinated phospholipids in ... ...

    Abstract Summary: Ubiquitin is covalently conjugated to phospholipids as well as proteins; however, ubiquitinated phospholipids are less abundant than free ubiquitin and ubiquitinated proteins. Here, we describe protocols to purify ubiquitinated phospholipids in budding yeast and human cells based on their hydrophobicity. Ubiquitinated phospholipids are purified by Triton X-114 phase partitioning and affinity purification and verified by phospholipase D treatment. These protocols enable the detection of tagged as well as endogenous mono- and poly-ubiquitinated phospholipids by immunoblotting.For complete details on the use and execution of this protocol, please refer to Sakamaki et al.1 : Publisher’s note: Undertaking any experimental protocol requires adherence to local institutional guidelines for laboratory safety and ethics.
    Keywords Cell Biology ; Model Organisms ; Molecular Biology ; Protein Biochemistry ; Science (General) ; Q1-390
    Subject code 500
    Language English
    Publishing date 2023-03-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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