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Addressing the implementation challenge of the global biodiversity framework

Biodiversity and conservation, 2020-08, Vol.29 (9-10), p.3061-3066

2020

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Corrigendum to “Priorities to inform research on marine plastic pollution in Southeast Asia” [Sci. Total Environ. volume 841 (2022) Article 156704]

The Science of the total environment, 2023-01, Vol.857, p.159595-159595, Article 159595

2023

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A Future for the Inland Fish and Fisheries Hidden Within the Sustainable Development Goals

Frontiers in environmental science, 2022-05, Vol.10

2022

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Inland recreational fisheries contribute nutritional benefits and economic value but are vulnerable to climate change

Nature food, 2024-05, Vol.5 (5), p.433

2024

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Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC

PloS one, 2017-06, Vol.12 (6), p.e0178307

2017

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Phospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channels

PloS one, 2013-08, Vol.8 (8), p.e72560-e72560

2013

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SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels

FEMS microbiology letters, 2018-08, Vol.365 (15)

2018

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A global perspective on the influence of the COVID-19 pandemic on freshwater fish biodiversity

Biological conservation, 2021-01, Vol.253, p.108932, Article 108932

2021

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Dimeric SecA couples the preprotein translocation in an asymmetric manner

PloS one, 2011-01, Vol.6 (1), p.e16498-e16498

2011

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Reconstitution of functionally efficient SecA-dependent protein-conducting channels: Transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels

Biochemical and biophysical research communications, 2013-02, Vol.431 (3), p.388-392

2013

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SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity

The Journal of biological chemistry, 2011-12, Vol.286 (52), p.44702-44709

2011

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The structure of SecB/OmpA as visualized by electron microscopy: The mature region of the precursor protein binds asymmetrically to SecB

Biochemical and biophysical research communications, 2010-03, Vol.393 (4), p.698-702

2010

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Full-length Escherichia coli SecA Dimerizes in a Closed Conformation in Solution as Determined by Cryo-electron Microscopy

The Journal of biological chemistry, 2008-10, Vol.283 (43), p.28783-28787

2008

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Ring-like Pore Structures of SecA: Implication for Bacterial Protein-Conducting Channels

Proceedings of the National Academy of Sciences - PNAS, 2003-04, Vol.100 (7), p.4221-4226

2003

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Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels

Biochemical and biophysical research communications, 2013-07, Vol.437 (2), p.212-216

2013

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Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDFYajC

PloS one, 2017-06, Vol.12 (6), p.e0178307

2017

Volltextzugriff (PDF)

The active ring-like structure of SecA revealed by electron crystallography: Conformational change upon interaction with SecB

Journal of structural biology, 2007-07, Vol.159 (1), p.149-153

2007

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Electron microscopic visualization of asymmetric precursor translocation intermediates: SecA functions as a dimer

Science China. Life sciences, 2010-09, Vol.53 (9), p.1049-1056

2010

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SecA Alone Can Promote Protein Translocation and Ion Channel Activity

The Journal of biological chemistry, 2011-12, Vol.286 (52), p.44702-44709

2011

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Full-length Escherichia coli SecA Dimerizes in a Closed Conformation in Solution as Determined by Cryo-electron Microscopyce:sup

The Journal of biological chemistry, 2008-10, Vol.283 (43), p.28783-28787

2008

Volltextzugriff (PDF)

Full-length Escherichia coli SecA Dimerizes in a Closed Conformation in Solution as Determined by Cryo-electron MicroscopyS

The Journal of biological chemistry, 2008-10, Vol.283 (43), p.28783-28787

2008

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Addressing the implementation challenge of the global biodiversity framework

Corrigendum to “Priorities to inform research on marine plastic pollution in Southeast Asia” [Sci. Total Environ. volume 841 (2022) Article 156704]

A Future for the Inland Fish and Fisheries Hidden Within the Sustainable Development Goals

Inland recreational fisheries contribute nutritional benefits and economic value but are vulnerable to climate change

Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDF•YajC

Phospholipids induce conformational changes of SecA to form membrane-specific domains: AFM structures and implication on protein-conducting channels

SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels

A global perspective on the influence of the COVID-19 pandemic on freshwater fish biodiversity

Dimeric SecA couples the preprotein translocation in an asymmetric manner

Reconstitution of functionally efficient SecA-dependent protein-conducting channels: Transformation of low-affinity SecA-liposome channels to high-affinity SecA-SecYEG-SecDF·YajC channels

SecA alone can promote protein translocation and ion channel activity: SecYEG increases efficiency and signal peptide specificity

The structure of SecB/OmpA as visualized by electron microscopy: The mature region of the precursor protein binds asymmetrically to SecB

Full-length Escherichia coli SecA Dimerizes in a Closed Conformation in Solution as Determined by Cryo-electron Microscopy

Ring-like Pore Structures of SecA: Implication for Bacterial Protein-Conducting Channels

Specificity of SecYEG for PhoA precursors and SecA homologs on SecA protein-conducting channels

Dissecting structures and functions of SecA-only protein-conducting channels: ATPase, pore structure, ion channel activity, protein translocation, and interaction with SecYEG/SecDFYajC

The active ring-like structure of SecA revealed by electron crystallography: Conformational change upon interaction with SecB

Electron microscopic visualization of asymmetric precursor translocation intermediates: SecA functions as a dimer

SecA Alone Can Promote Protein Translocation and Ion Channel Activity

Full-length Escherichia coli SecA Dimerizes in a Closed Conformation in Solution as Determined by Cryo-electron Microscopyce:sup

Full-length Escherichia coli SecA Dimerizes in a Closed Conformation in Solution as Determined by Cryo-electron MicroscopyS

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