Authors : Kanonenberg K; Institute of Biochemistry, Heinrich-Heine-University Duesseldorf, Universitaetsstr. 1, 40225, Duesseldorf, Germany.; CNRS, UMR5086 'Molecular Microbiology and Structural Biochemistry', Université de Lyon, 7 Passage du vercors, 69007, Lyon, France.

Subjects: Escherichia coli/Escherichia coli/Escherichia coli/*metabolism ; Escherichia coli Proteins/Escherichia coli Proteins/Escherichia coli Proteins/*biosynthesis ; Lipids/Lipids/Lipids/*chemistry

Source: Microbial cell factories [Microb Cell Fact] 2019 Aug 10; Vol. 18 (1), pp. 131. Date of Electronic Publication: 2019 Aug 10.Publisher: BioMed Central Country of Publication: England NLM ID: 101139812 Publication Model: Electronic Cited Medium: Internet ISSN: 1475-2859

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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.

Authors : Hsieh YH; Department of Biology, Center for Biotechnology and Drug Design, Georgia State University, Atlanta, GA, United States of America.; Huang YJ

Subjects: Adenosine Triphosphatases/Adenosine Triphosphatases/Adenosine Triphosphatases/*metabolism ; Bacterial Proteins/Bacterial Proteins/Bacterial Proteins/*metabolism ; Escherichia coli/Escherichia coli/Escherichia coli/*metabolism

Source: PloS one [PLoS One] 2017 Jun 02; Vol. 12 (6), pp. e0178307. Date of Electronic Publication: 2017 Jun 02 (Print Publication: 2017).Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet

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Crystal structure of Escherichia coli YidC, a membrane protein chaperone and insertase.

Authors : Kumazaki K; 1] Department of Biological Sciences, Graduate School of Science, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan [2] Global Research Cluster, RIKEN, 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan.; Kishimoto T

Subjects: Escherichia coli/Escherichia coli/Escherichia coli/*metabolism ; Escherichia coli Proteins/Escherichia coli Proteins/Escherichia coli Proteins/*chemistry ; Membrane Proteins/Membrane Proteins/Membrane Proteins/*chemistry

Source: Scientific reports [Sci Rep] 2014 Dec 03; Vol. 4, pp. 7299. Date of Electronic Publication: 2014 Dec 03.Publisher: Nature Publishing Group Country of Publication: England NLM ID: 101563288 Publication Model: Electronic Cited Medium: Internet ISSN:

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Unexpected oligomeric structure of the FocA formate channel of Escherichia coli : a paradigm for the formate-nitrite transporter family of integral membrane proteins.

Authors : Falke D; Institute for Biology/Microbiology, Martin-Luther University Halle-Wittenberg, Halle, Germany.; Schulz K

Subjects: Protein Multimerization*; Escherichia coli/Escherichia coli/Escherichia coli/*chemistry ; Escherichia coli Proteins/Escherichia coli Proteins/Escherichia coli Proteins/*chemistry

Source: FEMS microbiology letters [FEMS Microbiol Lett] 2010 Feb; Vol. 303 (1), pp. 69-75. Date of Electronic Publication: 2009 Nov 23.Publisher: Oxford University Press Country of Publication: England NLM ID: 7705721 Publication Model: Print-Electronic Cited Medium: Internet ISSN:

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Biochemistry. A missing link in membrane protein evolution.

Authors : Poolman B; Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, and Zernike Institute for Advanced Materials, University of Groningen, Nijenborgh 4, 9747 AG Groningen, Netherlands. ; Geertsma ER

Subjects: Evolution, Molecular*; Antiporters/Antiporters/Antiporters/*chemistry ; Cell Membrane/Cell Membrane/Cell Membrane/*chemistry

Source: Science (New York, N.Y.) [Science] 2007 Mar 02; Vol. 315 (5816), pp. 1229-31.Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 0404511 Publication Model: Print Cited Medium:

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YidC mediates membrane protein insertion in bacteria.

Authors : Samuelson JC; Department of Chemistry, The Ohio State University, Columbus 43210, USA.; Chen M

Subjects: Capsid Proteins* ; Escherichia coli Proteins* ; Membrane Transport Proteins*

Source: Nature [Nature] 2000 Aug 10; Vol. 406 (6796), pp. 637-41.Publisher: Nature Publishing Group Country of Publication: England NLM ID: 0410462 Publication Model: Print Cited Medium: Print ISSN: 0028-0836

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The structure of the ferric siderophore binding protein FhuD complexed with gallichrome.

Authors : Clarke TE; Department of Biological Sciences, University of Calgary, 2500 University Drive N.W., Calgary, Alberta, Canada T2N 1N4.; Ku SY

Subjects: Escherichia coli Proteins* ; Membrane Transport Proteins* ; Periplasmic Binding Proteins*

Source: Nature structural biology [Nat Struct Biol] 2000 Apr; Vol. 7 (4), pp. 287-91.Publisher: Nature Pub. Co Country of Publication: United States NLM ID: 9421566 Publication Model: Print Cited Medium: Print ISSN: 1072-8368

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Substrate-induced assembly of a contiguous channel for protein export from E.coli: reversible bridging of an inner-membrane translocase to an outer membrane exit pore.

Authors : Thanabalu T; Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QP, UK.; Koronakis E

Subjects: Carrier Proteins* ; Escherichia coli Proteins* ; Membrane Proteins*

Source: The EMBO journal [EMBO J] 1998 Nov 16; Vol. 17 (22), pp. 6487-96.Publisher: Nature Publishing Group Country of Publication: England NLM ID: 8208664 Publication Model: Print Cited Medium: Print ISSN: 0261-4189

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Evidence for chloramphenicol/H+ antiport in Cmr (MdfA) system of Escherichia coli and properties of the antiporter.

Authors : Mine T; Department of Microbiology, Faculty of Pharmaceutical Sciences, Okayama University, Tsushima, Okayama, 700-8530, Japan.; Morita Y

Subjects: Bacterial Proteins* ; Escherichia coli Proteins* ; Membrane Transport Proteins*

Source: Journal of biochemistry [J Biochem] 1998 Jul; Vol. 124 (1), pp. 187-93.Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print Cited Medium: Print ISSN: 0021-924X

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Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles.

Authors : Mori H; School of Life Science, Tokyo University of Pharmacy and Life Science, Hachioji, Tokyo, 192-0392, Japan.; Sugiyama H

Subjects: Escherichia coli Proteins* ; Membrane Transport Proteins*; Adenosine Triphosphatases/Adenosine Triphosphatases/Adenosine Triphosphatases/*metabolism

Source: Journal of biochemistry [J Biochem] 1998 Jul; Vol. 124 (1), pp. 122-9.Publisher: Oxford University Press Country of Publication: England NLM ID: 0376600 Publication Model: Print Cited Medium: Print ISSN: 0021-924X

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