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  1. Article ; Online: Towards bioprocess engineering of cable bacteria: Establishment of a synthetic sediment.

    Stiefelmaier, Judith / Keller, Joshua / Neupert, Wiebke / Ulber, Roland

    MicrobiologyOpen

    2024  Volume 13, Issue 3, Page(s) e1412

    Abstract: Cable bacteria, characterized by their multicellular filamentous growth, are prevalent in both freshwater and marine sediments. They possess the unique ability to transport electrons over distances of centimeters. Coupled with their capacity to fix ... ...

    Abstract Cable bacteria, characterized by their multicellular filamentous growth, are prevalent in both freshwater and marine sediments. They possess the unique ability to transport electrons over distances of centimeters. Coupled with their capacity to fix CO
    MeSH term(s) Geologic Sediments/microbiology ; Bioreactors/microbiology
    Language English
    Publishing date 2024-05-07
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2661368-2
    ISSN 2045-8827 ; 2045-8827
    ISSN (online) 2045-8827
    ISSN 2045-8827
    DOI 10.1002/mbo3.1412
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  2. Book ; Thesis: Pharmakokinetische und -dynamische Effekte als Ursache der Variabilität in der Wirkung von 2-Arylpropionsäuren

    Neupert, Werner

    1997  

    Author's details vorgelegt von Werner Neupert
    Language German
    Size 92 Bl. : graph. Darst.
    Edition [Mikrofiche-Ausg.]
    Document type Book ; Thesis
    Thesis / German Habilitation thesis Erlangen-Nürnberg, Univ., Diss., 1997
    Note Mikrofiche-Ausg.: 1 Mikrofiche : 24x
    HBZ-ID HT008188661
    Database Catalogue ZB MED Medicine, Health

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    In stock of ZB MED Cologne/Königswinter

    Shelf markLoan statusLocation
    1998 MB 411 order for loan Magazin

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  3. Article ; Online: Mitochondrial Gene Expression: A Playground of Evolutionary Tinkering.

    Neupert, Walter

    Annual review of biochemistry

    2016  Volume 85, Page(s) 65–76

    Abstract: This article introduces the Mitochondria theme of the Annual Review of Biochemistry, Volume 85. ...

    Abstract This article introduces the Mitochondria theme of the Annual Review of Biochemistry, Volume 85.
    MeSH term(s) Animals ; Biological Evolution ; DNA, Mitochondrial/genetics ; DNA, Mitochondrial/metabolism ; Electron Transport/genetics ; Gene Expression Regulation ; Genome, Mitochondrial ; Humans ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Proteins/genetics ; Mitochondrial Proteins/metabolism ; Mitochondrial Ribosomes/chemistry ; Mitochondrial Ribosomes/metabolism ; Organelle Biogenesis ; Protein Biosynthesis ; Signal Transduction
    Chemical Substances DNA, Mitochondrial ; Mitochondrial Proteins
    Language English
    Publishing date 2016-06-02
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev-biochem-011116-110824
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  4. Article ; Online: A perspective on transport of proteins into mitochondria: a myriad of open questions.

    Neupert, Walter

    Journal of molecular biology

    2015  Volume 427, Issue 6 Pt A, Page(s) 1135–1158

    Abstract: Mitochondria are the central hub of key cellular processes such as energy conversion, cell signaling, cell cycle regulation and cell differentiation. Therefore, in particular, mitochondrial biogenesis and protein translocation have been the focus of ... ...

    Abstract Mitochondria are the central hub of key cellular processes such as energy conversion, cell signaling, cell cycle regulation and cell differentiation. Therefore, in particular, mitochondrial biogenesis and protein translocation have been the focus of intense research for now nearly half a century. In spite of remarkable progress the field has made, many of the proposed mechanisms remain controversial and none of the translocation pathways is yet understood at the high-resolution level. In this context, the present article is intended to identify and discuss current major open questions and unresolved issues in the field in hope that it will stimulate and engage the pursuit of current efforts and expose new directions.
    MeSH term(s) Animals ; Carrier Proteins/metabolism ; Cytosol/metabolism ; Humans ; Intracellular Signaling Peptides and Proteins/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/metabolism ; Mitochondria/metabolism ; Mitochondrial Proteins/metabolism ; Multiprotein Complexes/metabolism ; Protein Precursors/metabolism ; Protein Transport ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism ; Tumor Suppressor Proteins/metabolism
    Chemical Substances Carrier Proteins ; Intracellular Signaling Peptides and Proteins ; MIM1 protein, S cerevisiae ; Membrane Proteins ; Mitochondrial Proteins ; Multiprotein Complexes ; Protein Precursors ; Saccharomyces cerevisiae Proteins ; Sam50 protein, S cerevisiae ; TOB1 protein, human ; TOM translocase ; Tumor Suppressor Proteins
    Language English
    Publishing date 2015-03-27
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2015.02.001
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  5. Article ; Online: A mitochondrial odyssey.

    Neupert, Walter

    Annual review of biochemistry

    2012  Volume 81, Page(s) 1–33

    Abstract: Good fortune let me be an innocent child during World War II, a hopeful adolescent with encouraging parents during the years of German recovery, and a self-determined adult in a period of peace, freedom, and wealth. My luck continued as a scientist who ... ...

    Abstract Good fortune let me be an innocent child during World War II, a hopeful adolescent with encouraging parents during the years of German recovery, and a self-determined adult in a period of peace, freedom, and wealth. My luck continued as a scientist who could entirely follow his fancy. My mind was always set on understanding how things are made. At a certain point, I found myself confronted with the question of how mitochondria and organelles, which cannot be formed de novo, are put together. Intracellular transport of proteins, their translocation across the mitochondrial membranes, and their folding and assembly were the processes that fascinated me. Now, after some 30 years, we have wonderful insights, unimagined views of a complex and at the same time simple machinery and its workings. We have glimpses of how orderly processes are established in the cell to assemble from single molecules our beautiful mitochondria that every day make some 50 kg of ATP for each of us. At the same time, we have learned amazing lessons from the tinkering of evolution that developed mitochondria from bacteria.
    MeSH term(s) Animals ; Cell Biology/history ; Germany ; History, 20th Century ; Mitochondria/chemistry ; Mitochondria/genetics ; Mitochondria/metabolism ; Mitochondrial Proteins/metabolism ; Protein Folding ; Protein Transport ; Proteins/metabolism
    Chemical Substances Mitochondrial Proteins ; Proteins
    Language English
    Publishing date 2012
    Publishing country United States
    Document type Biography ; Historical Article ; Journal Article ; Portraits
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev-biochem-083109-171531
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  6. Article ; Online: SnapShot: Mitochondrial architecture.

    Neupert, Walter

    Cell

    2012  Volume 149, Issue 3, Page(s) 722–722.e1

    MeSH term(s) Animals ; Humans ; Mitochondria/metabolism ; Mitochondria/ultrastructure ; Mitochondrial Proteins/metabolism ; Saccharomyces cerevisiae/cytology
    Chemical Substances Mitochondrial Proteins
    Language English
    Publishing date 2012-04-27
    Publishing country United States
    Document type Journal Article
    ZDB-ID 187009-9
    ISSN 1097-4172 ; 0092-8674
    ISSN (online) 1097-4172
    ISSN 0092-8674
    DOI 10.1016/j.cell.2012.04.010
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  7. Article: A Perspective on Transport of Proteins into Mitochondria: A Myriad of Open Questions

    Neupert, Walter

    Journal of Molecular Biology. 2015 Mar. 27, v. 427

    2015  

    Abstract: Mitochondria are the central hub of key cellular processes such as energy conversion, cell signaling, cell cycle regulation and cell differentiation. Therefore, in particular, mitochondrial biogenesis and protein translocation have been the focus of ... ...

    Abstract Mitochondria are the central hub of key cellular processes such as energy conversion, cell signaling, cell cycle regulation and cell differentiation. Therefore, in particular, mitochondrial biogenesis and protein translocation have been the focus of intense research for now nearly half a century. In spite of remarkable progress the field has made, many of the proposed mechanisms remain controversial and none of the translocation pathways is yet understood at the high-resolution level. In this context, the present article is intended to identify and discuss current major open questions and unresolved issues in the field in hope that it will stimulate and engage the pursuit of current efforts and expose new directions.
    Keywords biogenesis ; cell cycle ; cell differentiation ; energy conversion ; mitochondria ; protein transport ; transport proteins
    Language English
    Dates of publication 2015-0327
    Size p. 1135-1158.
    Publishing place Elsevier Ltd
    Document type Article
    ZDB-ID 80229-3
    ISSN 1089-8638 ; 0022-2836
    ISSN (online) 1089-8638
    ISSN 0022-2836
    DOI 10.1016/j.jmb.2015.02.001
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  8. Article ; Online: Cell biology: Architecture of a protein entry gate.

    Mokranjac, Dejana / Neupert, Walter

    Nature

    2015  Volume 528, Issue 7581, Page(s) 201–202

    MeSH term(s) Mitochondrial Membrane Transport Proteins/chemistry ; Saccharomyces cerevisiae Proteins/chemistry
    Chemical Substances Mitochondrial Membrane Transport Proteins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2015-12-10
    Publishing country England
    Document type Comment ; Journal Article
    ZDB-ID 120714-3
    ISSN 1476-4687 ; 0028-0836
    ISSN (online) 1476-4687
    ISSN 0028-0836
    DOI 10.1038/nature16318
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  9. Article: Protein import into mitochondria.

    Neupert, W

    Annual review of biochemistry

    1997  Volume 66, Page(s) 863–917

    Abstract: Mitochondria import many hundreds of different proteins that are encoded by nuclear genes. These proteins are targeted to the mitochondria, translocated through the mitochondrial membranes, and sorted to the different mitochondrial subcompartments. ... ...

    Abstract Mitochondria import many hundreds of different proteins that are encoded by nuclear genes. These proteins are targeted to the mitochondria, translocated through the mitochondrial membranes, and sorted to the different mitochondrial subcompartments. Separate translocases in the mitochondrial outer membrane (TOM complex) and in the inner membrane (TIM complex) facilitate recognition of preproteins and transport across the two membranes. Factors in the cytosol assist in targeting of preproteins. Protein components in the matrix partake in energetically driving translocation in a reaction that depends on the membrane potential and matrix-ATP. Molecular chaperones in the matrix exert multiple functions in translocation, sorting, folding, and assembly of newly imported proteins.
    MeSH term(s) Adenosine Triphosphatases/metabolism ; Animals ; Bacterial Proteins/metabolism ; Biological Transport ; Cytosol/metabolism ; Escherichia coli Proteins ; HSP70 Heat-Shock Proteins/metabolism ; Humans ; Membrane Transport Proteins ; Mitochondria/metabolism ; Protein Folding ; Protein Precursors/metabolism ; Proteins/metabolism ; SEC Translocation Channels ; Signal Transduction
    Chemical Substances Bacterial Proteins ; Escherichia coli Proteins ; HSP70 Heat-Shock Proteins ; Membrane Transport Proteins ; Protein Precursors ; Proteins ; SEC Translocation Channels ; SecA protein, Bacteria (119129-39-4) ; Adenosine Triphosphatases (EC 3.6.1.-)
    Language English
    Publishing date 1997
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 207924-0
    ISSN 1545-4509 ; 0066-4154
    ISSN (online) 1545-4509
    ISSN 0066-4154
    DOI 10.1146/annurev.biochem.66.1.863
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  10. Article ; Online: Structure of the Bcs1 AAA-ATPase suggests an airlock-like translocation mechanism for folded proteins.

    Kater, Lukas / Wagener, Nikola / Berninghausen, Otto / Becker, Thomas / Neupert, Walter / Beckmann, Roland

    Nature structural & molecular biology

    2020  Volume 27, Issue 2, Page(s) 142–149

    Abstract: Some proteins require completion of folding before translocation across a membrane into another cellular compartment. Yet the permeability barrier of the membrane should not be compromised and mechanisms have remained mostly elusive. Here, we present the ...

    Abstract Some proteins require completion of folding before translocation across a membrane into another cellular compartment. Yet the permeability barrier of the membrane should not be compromised and mechanisms have remained mostly elusive. Here, we present the structure of Saccharomyces cerevisiae Bcs1, an AAA-ATPase of the inner mitochondrial membrane. Bcs1 facilitates the translocation of the Rieske protein, Rip1, which requires folding and incorporation of a 2Fe-2S cluster before translocation and subsequent integration into the bc1 complex. Surprisingly, Bcs1 assembles into exclusively heptameric homo-oligomers, with each protomer consisting of an amphipathic transmembrane helix, a middle domain and an ATPase domain. Together they form two aqueous vestibules, the first being accessible from the mitochondrial matrix and the second positioned in the inner membrane, with both separated by the seal-forming middle domain. On the basis of this unique architecture, we propose an airlock-like translocation mechanism for folded Rip1.
    MeSH term(s) ATPases Associated with Diverse Cellular Activities/chemistry ; ATPases Associated with Diverse Cellular Activities/metabolism ; Electron Transport Complex III/chemistry ; Electron Transport Complex III/metabolism ; Mitochondrial Membranes/chemistry ; Mitochondrial Membranes/metabolism ; Mitochondrial Proteins/chemistry ; Mitochondrial Proteins/metabolism ; Models, Molecular ; Molecular Chaperones/chemistry ; Molecular Chaperones/metabolism ; Nuclear Pore Complex Proteins/chemistry ; Nuclear Pore Complex Proteins/metabolism ; Protein Conformation ; Protein Domains ; Protein Folding ; Protein Multimerization ; Protein Transport ; Saccharomyces cerevisiae/chemistry ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances BCS1 protein, S cerevisiae ; Mitochondrial Proteins ; Molecular Chaperones ; NUP42 protein, S cerevisiae ; Nuclear Pore Complex Proteins ; Saccharomyces cerevisiae Proteins ; ATPases Associated with Diverse Cellular Activities (EC 3.6.4.-) ; Electron Transport Complex III (EC 7.1.1.8)
    Language English
    Publishing date 2020-01-27
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/s41594-019-0364-1
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