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Transmembrane helix assembly and the role of salt bridges

Current opinion in structural biology, 2014-08, Vol.27, p.63-68

2014

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Folding and Self-Assembly of the TatA Translocation Pore Based on a Charge Zipper Mechanism

Cell, 2013-01, Vol.152 (1-2), p.316-326

2013

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Length matters: Functional flip of the short TatA transmembrane helix

Biophysical journal, 2023-06, Vol.122 (11), p.2125-2146

2023

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Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy

Journal of the American Chemical Society, 2010-11, Vol.132 (45), p.15945-15956

2010

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Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy

Journal of the American Chemical Society, 2010-11, Vol.132 (45), p.15945

2010

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The transient production of anti-TNF-α antibody Adalimumab and a comparison of its characterization to the biosimilar Cinorra

Protein expression and purification, 2019-03, Vol.155, p.59-65

2019

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Structural and functional characterization of the pore-forming domain of pinholin S 21 68

Proceedings of the National Academy of Sciences - PNAS, 2020-11, Vol.117 (47), p.29637-29646

2020

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Structural and functional characterization of the pore-forming domain of pinholin S2168

Proceedings of the National Academy of Sciences - PNAS, 2020-11, Vol.117 (47), p.29637-29646

2020

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Magnetically oriented dodecylphosphocholine bicelles for solid-state NMR structure analysis

Biochimica et biophysica acta, 2012-05, Vol.1818 (5), p.1142-1147

2012

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Structure analysis of the protein translocating channel TatA in membranes using a multi-construct approach

Biochimica et biophysica acta, 2007-10, Vol.1768 (10), p.2627-2634

2007

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Structure analysis of the membrane protein TatC(d) from the Tat system of B. subtilis by circular dichroism

Biochimica et biophysica acta, 2009-10, Vol.1788 (10), p.2238

2009

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Iteratively nafionated water” in its solid phase at room temperature is in fact a mixture of lyophilized biological and non-biological contaminants

Journal of molecular liquids, 2023-09, Vol.385, p.122351, Article 122351

2023

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Key investor documents and their consequences on investor behavior

Zeitschrift für Betriebswirtschaft, 2015-02, Vol.85 (2), p.129-156

Walther, Torsten

2015

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Exploring the functional interaction between POSH and ALIX and the relevance to HIV-1 release

Retrovirology, 2009-09, Vol.6 (S2), p.P92-P92, Article P92

2009

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Flipping Helices: Membrane Insertion of Amphiphilic Helices and Extrusion of Transmembrane Segments

Biophysical journal, 2018-02, Vol.114 (3), p.34a-34a

2018

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Structure analysis of the membrane protein TatCd from the Tat system of B. subtilis by circular dichroism

Biochimica et biophysica acta. Biomembranes, 2009-10, Vol.1788 (10), p.2238-2244

2009

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Membrane Alignment of the Pore-Forming Component TatA d of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy

Journal of the American Chemical Society, 2010-11, Vol.132 (45), p.15945-15956

2010

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Strukturuntersuchungen am porenbildenden translokationsprotein tatad aus b. subtilis

Walther, Torsten Hartwig

2011

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Modeling Assembly of the Tata Pore Forming Complex using an Implicit Membrane Model

Biophysical journal, 2013-01, Vol.104 (2), p.288a-288a

2013

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Folding and Self-Assembly of the Pore-Forming Unit Tat-A of the Bacterial Twin-Arginine Translocase

Biophysical journal, 2011-02, Vol.100 (3), p.345a-345a

2011

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Structure analysis of the membrane protein TatC d from the Tat system of B. subtilis by circular dichroism

Biochimica et biophysica acta. Biomembranes, 2009, Vol.1788 (10), p.2238-2244

2009

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Exploring the functional interaction between POSH and ALIX and the relevance to HIV-1 release

BMC biochemistry, 2009-04, Vol.10 (1), p.12-12, Article 12

2009

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Pore Formation and Structure of the Twin Arginine Translocase Subunit TatA from B. subtilis

Biophysical journal, 2009-02, Vol.96 (3), p.194a-194a

2009

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Structural characterization of the pore forming protein TatAd of the twin-arginine translocase in membranes by solid-state 15N-NMR

Biochimica et biophysica acta. Biomembranes, 2007-12, Vol.1768 (12), p.3071-3079

2007

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Structural characterization of the pore forming protein TatA d of the twin-arginine translocase in membranes by solid-state 15N-NMR

Biochimica et biophysica acta. Biomembranes, 2007, Vol.1768 (12), p.3071-3079

2007

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Transmembrane helix assembly and the role of salt bridges

Folding and Self-Assembly of the TatA Translocation Pore Based on a Charge Zipper Mechanism

Length matters: Functional flip of the short TatA transmembrane helix

Membrane Alignment of the Pore-Forming Component TatAd of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy

Membrane alignment of the pore-forming component TatA(d) of the twin-arginine translocase from Bacillus subtilis resolved by solid-state NMR spectroscopy

The transient production of anti-TNF-α antibody Adalimumab and a comparison of its characterization to the biosimilar Cinorra

Structural and functional characterization of the pore-forming domain of pinholin S 21 68

Structural and functional characterization of the pore-forming domain of pinholin S2168

Magnetically oriented dodecylphosphocholine bicelles for solid-state NMR structure analysis

Structure analysis of the protein translocating channel TatA in membranes using a multi-construct approach

Structure analysis of the membrane protein TatC(d) from the Tat system of B. subtilis by circular dichroism

Iteratively nafionated water” in its solid phase at room temperature is in fact a mixture of lyophilized biological and non-biological contaminants

Key investor documents and their consequences on investor behavior

Exploring the functional interaction between POSH and ALIX and the relevance to HIV-1 release

Flipping Helices: Membrane Insertion of Amphiphilic Helices and Extrusion of Transmembrane Segments

Structure analysis of the membrane protein TatCd from the Tat system of B. subtilis by circular dichroism

Membrane Alignment of the Pore-Forming Component TatA d of the Twin-Arginine Translocase from Bacillus subtilis Resolved by Solid-State NMR Spectroscopy

Strukturuntersuchungen am porenbildenden translokationsprotein tatad aus b. subtilis

Modeling Assembly of the Tata Pore Forming Complex using an Implicit Membrane Model

Folding and Self-Assembly of the Pore-Forming Unit Tat-A of the Bacterial Twin-Arginine Translocase

Structure analysis of the membrane protein TatC d from the Tat system of B. subtilis by circular dichroism

Exploring the functional interaction between POSH and ALIX and the relevance to HIV-1 release

Pore Formation and Structure of the Twin Arginine Translocase Subunit TatA from B. subtilis

Structural characterization of the pore forming protein TatAd of the twin-arginine translocase in membranes by solid-state 15N-NMR

Structural characterization of the pore forming protein TatA d of the twin-arginine translocase in membranes by solid-state 15N-NMR

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