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  1. Article ; Online: Protein crowding in the inner mitochondrial membrane.

    Schlame, Michael

    Biochimica et biophysica acta. Bioenergetics

    2020  Volume 1862, Issue 1, Page(s) 148305

    Abstract: The inner membrane of mitochondria is known for its low lipid-to-protein ratio. Calculations based on the size and the concentration of the principal membrane components, suggest about half of the hydrophobic volume of the membrane is occupied by ... ...

    Abstract The inner membrane of mitochondria is known for its low lipid-to-protein ratio. Calculations based on the size and the concentration of the principal membrane components, suggest about half of the hydrophobic volume of the membrane is occupied by proteins. Such high degree of crowding is expected to strain the hydrophobic coupling between proteins and lipids unless stabilizing mechanisms are in place. Both protein supercomplexes and cardiolipin are likely to be critical for the integrity of the inner mitochondrial membrane because they reduce the energy penalty of crowding.
    MeSH term(s) Animals ; Humans ; Mitochondria/metabolism ; Mitochondrial Membranes/metabolism ; Mitochondrial Proteins/metabolism
    Chemical Substances Mitochondrial Proteins
    Keywords covid19
    Language English
    Publishing date 2020-09-08
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 60-7
    ISSN 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2650 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2642 ; 1879-2618
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbabio.2020.148305
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Mitochondrial cristae as insulated transformers of metabolic energy.

    Schlame, Michael

    The EMBO journal

    2019  Volume 38, Issue 22, Page(s) e103472

    Abstract: The mitochondrial inner membrane consists of the inner boundary membrane and invaginations called cristae, which differ in protein composition and likely have distinct functions. In this issue of The EMBO Journal, Wolf et al (2019) report that the ... ...

    Abstract The mitochondrial inner membrane consists of the inner boundary membrane and invaginations called cristae, which differ in protein composition and likely have distinct functions. In this issue of The EMBO Journal, Wolf et al (2019) report that the cristae carry a higher membrane potential than the intervening boundary membranes. Their data suggest electro-chemical discontinuity among segments of the inner membrane, implying that individual cristae may operate with some degree of independence.
    MeSH term(s) Membrane Potentials ; Mitochondria ; Mitochondrial Membranes
    Language English
    Publishing date 2019-10-16
    Publishing country England
    Document type Journal Article ; Comment
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2019103472
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Protein crowding in the inner mitochondrial membrane

    Schlame, Michael

    Biochimica et biophysica acta. 2021 Jan. 01, v. 1862, no. 1

    2021  

    Abstract: The inner membrane of mitochondria is known for its low lipid-to-protein ratio. Calculations based on the size and the concentration of the principal membrane components, suggest about half of the hydrophobic volume of the membrane is occupied by ... ...

    Abstract The inner membrane of mitochondria is known for its low lipid-to-protein ratio. Calculations based on the size and the concentration of the principal membrane components, suggest about half of the hydrophobic volume of the membrane is occupied by proteins. Such high degree of crowding is expected to strain the hydrophobic coupling between proteins and lipids unless stabilizing mechanisms are in place. Both protein supercomplexes and cardiolipin are likely to be critical for the integrity of the inner mitochondrial membrane because they reduce the energy penalty of crowding.
    Keywords cardiolipins ; energy ; hydrophobicity ; mitochondrial membrane ; proteins ; volume
    Language English
    Dates of publication 2021-0101
    Publishing place Elsevier B.V.
    Document type Article
    Note NAL-light
    ZDB-ID 282711-6
    ISSN 0005-2728 ; 0304-4173
    ISSN 0005-2728 ; 0304-4173
    DOI 10.1016/j.bbabio.2020.148305
    Database NAL-Catalogue (AGRICOLA)

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  4. Article ; Online: The mystery of mitochondrial plasticity: TMBIM5 integrates metabolic state and proteostasis.

    Ren, Mindong / Schlame, Michael

    The EMBO journal

    2022  Volume 41, Issue 16, Page(s) e111834

    Abstract: How cellular cues alter the mitochondrial proteome and impact the composition of mitochondrial proteins remains poorly understood. In this issue of The EMBO Journal, Patron et al (2022) identify TMBIM5 as an important link between calcium homeostasis, ... ...

    Abstract How cellular cues alter the mitochondrial proteome and impact the composition of mitochondrial proteins remains poorly understood. In this issue of The EMBO Journal, Patron et al (2022) identify TMBIM5 as an important link between calcium homeostasis, proton motive force, and mitochondrial proteolysis, by which the organelle can modify its protein composition. The results may be crucial for our understanding of the plasticity of mitochondria.
    MeSH term(s) Mitochondria/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Proteolysis ; Proteome/metabolism ; Proteostasis
    Chemical Substances Mitochondrial Proteins ; Proteome
    Language English
    Publishing date 2022-08-01
    Publishing country England
    Document type Journal Article
    ZDB-ID 586044-1
    ISSN 1460-2075 ; 0261-4189
    ISSN (online) 1460-2075
    ISSN 0261-4189
    DOI 10.15252/embj.2022111834
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  5. Article: Protein crowding in the inner mitochondrial membrane

    Schlame, Michael

    Biochim Biophys Acta Bioenerg

    Abstract: The inner membrane of mitochondria is known for its low lipid-to-protein ratio. Calculations based on the size and the concentration of the principal membrane components, suggest about half of the hydrophobic volume of the membrane is occupied by ... ...

    Abstract The inner membrane of mitochondria is known for its low lipid-to-protein ratio. Calculations based on the size and the concentration of the principal membrane components, suggest about half of the hydrophobic volume of the membrane is occupied by proteins. Such high degree of crowding is expected to strain the hydrophobic coupling between proteins and lipids unless stabilizing mechanisms are in place. Both protein supercomplexes and cardiolipin are likely to be critical for the integrity of the inner mitochondrial membrane because they reduce the energy penalty of crowding.
    Keywords covid19
    Publisher WHO
    Document type Article
    Note WHO #Covidence: #32916174
    Database COVID19

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  6. Book ; Thesis: Biologisch aktive Phospholipidspezies in Lungensurfactant, Blut und Mitochondrien

    Schlame, Michael

    eine Untersuchung zu biochemischen Grundlagen des Schockgeschehens

    1997  

    Author's details von Michael Schlame
    Language German
    Size Getr. Zählung : graph. Darst.
    Edition [Mikrofiche-Ausg.]
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Berlin, Humboldt-Univ., Habil.-Schr., 1997
    Note Mikrofiche-Ausg.: 3 Mikrofiches : 24x ; Enth. 12 Sonderabdr. aus verschiedenen Zeitschr.
    HBZ-ID HT007829347
    Database Catalogue ZB MED Medicine, Health

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    Shelf markLoan statusLocation
    1997 MB 1660 order for loan Magazin

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  7. Article ; Online: The critical role of cardiolipin in metazoan differentiation, development, and maturation.

    Olivar-Villanueva, Melissa / Ren, Mindong / Schlame, Michael / Phoon, Colin K L

    Developmental dynamics : an official publication of the American Association of Anatomists

    2023  Volume 252, Issue 6, Page(s) 691–712

    Abstract: Cardiolipins are phospholipids that are central to proper mitochondrial functioning. Because mitochondria play crucial roles in differentiation, development, and maturation, we would also expect cardiolipin to play major roles in these processes. Indeed, ...

    Abstract Cardiolipins are phospholipids that are central to proper mitochondrial functioning. Because mitochondria play crucial roles in differentiation, development, and maturation, we would also expect cardiolipin to play major roles in these processes. Indeed, cardiolipin has been implicated in the mechanism of three human diseases that affect young infants, implying developmental abnormalities. In this review, we will: (1) Review the biology of cardiolipin; (2) Outline the evidence for essential roles of cardiolipin during organismal development, including embryogenesis and cell maturation in vertebrate organisms; (3) Place the role(s) of cardiolipin during embryogenesis within the larger context of the roles of mitochondria in development; and (4) Suggest avenues for future research.
    MeSH term(s) Animals ; Humans ; Cardiolipins ; Mitochondria ; Cell Differentiation
    Chemical Substances Cardiolipins
    Language English
    Publishing date 2023-02-09
    Publishing country United States
    Document type Journal Article ; Review ; Research Support, N.I.H., Extramural
    ZDB-ID 1102541-4
    ISSN 1097-0177 ; 1058-8388
    ISSN (online) 1097-0177
    ISSN 1058-8388
    DOI 10.1002/dvdy.567
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  8. Article ; Online: StaR-related lipid transfer-like domain-containing protein CLDP43 affects cardiolipin synthesis and mitochondrial function in Trypanosoma brucei.

    Loffreda, Alessio / Schlame, Michael / Bütikofer, Peter

    PloS one

    2022  Volume 17, Issue 4, Page(s) e0259752

    Abstract: Cardiolipin is known to interact with bacterial and mitochondrial proteins and protein complexes. Unlike in Escherichia coli and Saccharomyces cerevisiae, the synthesis of cardiolipin is essential for growth of Trypanosoma brucei parasites in culture. ... ...

    Abstract Cardiolipin is known to interact with bacterial and mitochondrial proteins and protein complexes. Unlike in Escherichia coli and Saccharomyces cerevisiae, the synthesis of cardiolipin is essential for growth of Trypanosoma brucei parasites in culture. Inhibition of cardiolipin production has been shown to result in major changes in the T. brucei proteome and energy metabolism, with CLDP43, a mitochondrial protein containing a StaR-related lipid transfer (START)-like domain, being depleted in a cardiolipin-dependent way. We now show that in T. brucei procyclic forms lacking CLDP43, cardiolipin metabolism and mitochondrial function are affected. Using quantitative and qualitative lipid analyses, we found that while steady-state levels of cardiolipin were elevated in CLDP43 knock-out parasites compared to parental cells, de novo formation of cardiolipin was down-regulated. In addition, depletion of CLDP43 resulted in partial loss of mitochondrial membrane potential and decreased ATP production via substrate level phosphorylation. Recombinant CLDP43 was found to bind cardiolipin and phosphatidic acid in lipid overlay experiments, suggesting that it may be involved in transport or synthesis of cardiolipin or its precursors in T. brucei.
    MeSH term(s) Cardiolipins/metabolism ; Mitochondria/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Protozoan Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Trypanosoma brucei brucei/genetics
    Chemical Substances Cardiolipins ; Mitochondrial Proteins ; Protozoan Proteins
    Language English
    Publishing date 2022-04-22
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2267670-3
    ISSN 1932-6203 ; 1932-6203
    ISSN (online) 1932-6203
    ISSN 1932-6203
    DOI 10.1371/journal.pone.0259752
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  9. Article ; Online: The Function of Tafazzin, a Mitochondrial Phospholipid-Lysophospholipid Acyltransferase.

    Schlame, Michael / Xu, Yang

    Journal of molecular biology

    2020  Volume 432, Issue 18, Page(s) 5043–5051

    Abstract: Tafazzin is a mitochondrial enzyme that exchanges fatty acids between phospholipids by phospholipid-lysophospholipid transacylation. The reaction alters the molecular species composition and, as a result, the physical properties of lipids. In vivo, the ... ...

    Abstract Tafazzin is a mitochondrial enzyme that exchanges fatty acids between phospholipids by phospholipid-lysophospholipid transacylation. The reaction alters the molecular species composition and, as a result, the physical properties of lipids. In vivo, the most important substrate of tafazzin is the mitochondria-specific lipid cardiolipin. Tafazzin mutations cause the human disease Barth syndrome, which presents with cardiomyopathy, skeletal muscle weakness, fatigue, and other symptoms, probably all related to mitochondrial dysfunction. The reason why mitochondria require tafazzin is still not known, but recent evidence suggests that tafazzin may lower the energy cost associated with protein crowding in the inner mitochondrial membrane.
    MeSH term(s) Animals ; Barth Syndrome/genetics ; Cardiolipins/metabolism ; Humans ; Mitochondria/enzymology ; Mitochondria/metabolism ; Mutation ; Transcription Factors/genetics ; Transcription Factors/metabolism
    Chemical Substances Cardiolipins ; Transcription Factors ; TAFAZZIN protein, human (EC 2.3.1.-)
    Language English
    Publishing date 2020-03-29
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2020.03.026
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  10. Article ; Online: StaR-related lipid transfer-like domain-containing protein CLDP43 affects cardiolipin synthesis and mitochondrial function in Trypanosoma brucei.

    Alessio Loffreda / Michael Schlame / Peter Bütikofer

    PLoS ONE, Vol 17, Iss 4, p e

    2022  Volume 0259752

    Abstract: Cardiolipin is known to interact with bacterial and mitochondrial proteins and protein complexes. Unlike in Escherichia coli and Saccharomyces cerevisiae, the synthesis of cardiolipin is essential for growth of Trypanosoma brucei parasites in culture. ... ...

    Abstract Cardiolipin is known to interact with bacterial and mitochondrial proteins and protein complexes. Unlike in Escherichia coli and Saccharomyces cerevisiae, the synthesis of cardiolipin is essential for growth of Trypanosoma brucei parasites in culture. Inhibition of cardiolipin production has been shown to result in major changes in the T. brucei proteome and energy metabolism, with CLDP43, a mitochondrial protein containing a StaR-related lipid transfer (START)-like domain, being depleted in a cardiolipin-dependent way. We now show that in T. brucei procyclic forms lacking CLDP43, cardiolipin metabolism and mitochondrial function are affected. Using quantitative and qualitative lipid analyses, we found that while steady-state levels of cardiolipin were elevated in CLDP43 knock-out parasites compared to parental cells, de novo formation of cardiolipin was down-regulated. In addition, depletion of CLDP43 resulted in partial loss of mitochondrial membrane potential and decreased ATP production via substrate level phosphorylation. Recombinant CLDP43 was found to bind cardiolipin and phosphatidic acid in lipid overlay experiments, suggesting that it may be involved in transport or synthesis of cardiolipin or its precursors in T. brucei.
    Keywords Medicine ; R ; Science ; Q
    Subject code 570
    Language English
    Publishing date 2022-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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