Výsledky vyhledávání - "Kirstin Model"

Structural and Functional Fingerprint of the Mitochondrial ATP-binding Cassette Transporter Mdl1 from Saccharomyces cerevisiae

Autor: Simone Gompf, Ariane Zutz, Chris van der Does, Kirstin Model, Chiara Presenti, Robert Tampé, Matthias Hofacker, Winfried Haase

Publikováno v: Journal of Biological Chemistry. 282:3951-3961

The ATP-binding cassette half-transporter Mdl1 from Saccharomyces cerevisiae has been proposed to be involved in the quality control of misassembled respiratory chain complexes by exporting degradation products generated by the m-AAA proteases from t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d59a4dc5a08e32d5a7f43e9d59239a30
https://doi.org/10.1074/jbc.m609899200

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Preprotein Translocase of the Outer Mitochondrial Membrane: Reconstituted Tom40 Forms a Characteristic TOM Pore

Autor: Rita Casadio, Richard Wagner, Lars Becker, Georg E. Schulz, Kerstin Hill, Kaye N. Truscott, Kirstin Model, Nikolaus Pfanner, Thomas Krimmer, Michael Bannwarth, Chris Meisinger

Publikováno v: Journal of Molecular Biology. 353:1011-1020

Tom40 is the central pore-forming component of the translocase of the outer mitochondrial membrane (TOM complex). Different views exist about the secondary structure and electrophysiological characteristics of Tom40 from Saccharomyces cerevisiae and

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8486ddd57590f31644810460a111186a
https://doi.org/10.1016/j.jmb.2005.09.019

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Two-substrate association with the 20S proteasome at single-molecule level

Autor: Kirstin Model, Robert Tampé, Ali Tinazli, Silke Hutschenreiter

Publikováno v: The EMBO Journal. 23:2488-2497

The bipartite structure of the proteasome raises the question of functional significance. A rational design for unraveling mechanistic details of the highly symmetrical degradation machinery from Thermoplasma acidophilum pursues orientated immobiliza

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::52c0ec262a6554746f6813f31bacb4a0
https://doi.org/10.1038/sj.emboj.7600262

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Consensus Structural Features of Purified Bacterial TatABC Complexes

Autor: Joanne Oates, Colin Robinson, Dorothea Mangels, Werner Kühlbrandt, Kirstin Model, Joanne E. Mathers

Publikováno v: Journal of Molecular Biology. 330:277-286

The twin-arginine translocation (Tat) system transports folded proteins across bacterial plasma membranes and the chloroplast thylakoid membrane. Here, we investigate the composition and structural organization of three different purified Tat complex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72089e0bc6b5f5634316145d0e44db43
https://doi.org/10.1016/s0022-2836(03)00621-1

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[Untitled]

Autor: Nils Wiedemann, Nikolaus Pfanner, Michael T. Ryan, Chris Meisinger, Thorsten Prinz, Kaye N. Truscott, Kirstin Model

Publikováno v: Nature Structural Biology. 8:361-370

Proteins targeted to mitochondria are transported into the organelle through a high molecular weight complex called the translocase of the outer mitochondrial membrane (TOM). At the core of this machinery is a multisubunit general import pore (GIP) o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::b74e9172e8caa9586848fa5b504af2d7
https://doi.org/10.1038/86253

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The preprotein translocase of the outer mitochondrial membrane: receptors and a general import pore

Autor: Chris Meisinger, Michael T. Ryan, Jan Brix, Nikolaus Pfanner, Kirstin Model

Publikováno v: Scopus-Elsevier
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Cytosol-synthesized preproteins destined for the mitochondria are transported across the outer membrane by the translocase of the mitochondrial outer membrane (TOM complex). This dynamic transport machinery can be divided into receptors that recogniz

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b378038d445b2c6335a32873154e72a
https://doi.org/10.1007/s000180050028

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Strategy for membrane protein crystallization exemplified with OmpA and OmpX

Autor: Alex Pautsch, Georg E. Schulz, Joachim Vogt, Kirstin Model, Christian Siebold

Publikováno v: Proteins: Structure, Function, and Genetics. 34:167-172

The bacterial outer membrane proteins OmpA and OmpX were modified in such a manner that they yielded bulky crystals diffracting X-rays isotropically beyond 2 A resolution and permitting detailed structural analyses. The procedure involved semi-direct

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0c0ae4d29c52a2858d8b54aaa4865727
https://doi.org/10.1002/(sici)1097-0134(19990201)34:2<167::aid-prot2>3.0.co

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Cryo-electron microscopy structure of a yeast mitochondrial preprotein translocase

Autor: Chris Meisinger, Werner Kühlbrandt, Kirstin Model

Publikováno v: Journal of molecular biology. 383(5)

The translocase of the outer mitochondrial membrane (TOM) complex is the main entry gate for proteins imported into mitochondria. We determined the structure of the native, unstained approximately 550-kDa core-Tom20 complex from Saccharomycescerevisi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b47572822993b525f8670ee839cd90a9
https://pubmed.ncbi.nlm.nih.gov/18706915

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