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Academic Journal

OmpA controls order in the outer membrane and shares the mechanical load.

  • Authors : Benn G; Department of Molecular Biology, Princeton University, Princeton, NJ 08540.; Borrelli C

Subjects: Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/metabolism ; Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/chemistry ; Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/genetics

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Dec 10; Vol. 121 (50), pp. e2416426121. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Hierarchical assembly and environmental enhancement of bacterial ice nucleators.

  • Authors : Renzer G; Department of Molecular Spectroscopy, Max Planck Institute for Polymer Research, Mainz 55128, Germany.; de Almeida Ribeiro I

Subjects: Ice* ; Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/chemistry ; Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/metabolism

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Oct 22; Vol. 121 (43), pp. e2409283121. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Native β-barrel substrates pass through two shared intermediates during folding on the BAM complex.

  • Authors : Dos Santos TMA; Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138.; Thomson BD

Subjects: Protein Folding* ; Escherichia coli Proteins*/Escherichia coli Proteins*/Escherichia coli Proteins*/metabolism ; Escherichia coli Proteins*/Escherichia coli Proteins*/Escherichia coli Proteins*/chemistry

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Oct 15; Vol. 121 (42), pp. e2409672121. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

POTRA domains of the TamA insertase interact with the outer membrane and modulate membrane properties.

  • Authors : Mellouk A; Institut National de la Rechyuerche Scientifique (INRS), Centre Armand-Frappier Santé Biotechnologie, Laval, QC H7V 1B7, Canada.; Regroupement Québécois de recherche sur la fonction, la structure et l'ingénierie des protéines (PROTEO), Université du Québec à Montréal, Montréal, QC H2X 3Y7, Canada.

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

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 Jul 09; Vol. 121 (28), pp. e2402543121. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

YdbH and YnbE form an intermembrane bridge to maintain lipid homeostasis in the outer membrane of Escherichia coli .

  • Authors : Kumar S; Department of Microbiology, The Ohio State University, Columbus, OH 43210.; Davis RM

Subjects: Bacterial Outer Membrane*/Bacterial Outer Membrane*/Bacterial Outer Membrane*/metabolism ; Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/metabolism ; Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/genetics

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2024 May 21; Vol. 121 (21), pp. e2321512121. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

A multidomain connector links the outer membrane and cell wall in phylogenetically deep-branching bacteria.

  • Authors : von Kügelgen A; Structural Studies Division, MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom.; Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.

Subjects: Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/chemistry ; Bacterial Proteins*/Bacterial Proteins*/Bacterial Proteins*/chemistry ; Cell Wall*/Cell Wall*/Cell Wall*/chemistry

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Aug 16; Vol. 119 (33), pp. e2203156119. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Disproportionate investment in Spiralin B production limits in-host growth and favors the vertical transmission of Spiroplasma insect endosymbionts.

  • Authors : Masson F; Global Health Institute, School of Life Sciences, École Polytechnique Fédérale de Lausanne, Lausanne, 1015 Switzerland.; Rommelaere S

Subjects: Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/metabolism ; Drosophila melanogaster*/Drosophila melanogaster*/Drosophila melanogaster*/microbiology ; Drosophila melanogaster*/Drosophila melanogaster*/Drosophila melanogaster*/physiology

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Jul 26; Vol. 119 (30), pp. e2208461119. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

HDX-MS performed on BtuB in E. coli outer membranes delineates the luminal domain's allostery and unfolding upon B12 and TonB binding.

  • Authors : Zmyslowski AM; Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637.; Baxa MC

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

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 May 17; Vol. 119 (20), pp. e2119436119. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Fast slow folding of an outer membrane porin.

  • Authors : Weatherill EE; Department of Chemistry, King's College London, London SE1 1DB, United Kingdom.; Fahie MA

Subjects: Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/Bacterial Outer Membrane Proteins*/chemistry ; Escherichia coli Proteins*/Escherichia coli Proteins*/Escherichia coli Proteins*/chemistry ; Porins*/Porins*/Porins*/chemistry

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 May 17; Vol. 119 (20), pp. e2121487119. Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet

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Academic Journal

Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates.

  • Authors : Chamachi N; B CUBE - Center for Molecular Bioengineering, Technische Universität Dresden, 01307 Dresden, Germany.; Hartmann A

Subjects: Bacterial Outer Membrane Proteins/Bacterial Outer Membrane Proteins/Bacterial Outer Membrane Proteins/*metabolism ; Biopolymers/Biopolymers/Biopolymers/*metabolism ; Molecular Chaperones/Molecular Chaperones/Molecular Chaperones/*metabolism

  • Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Mar 01; Vol. 119 (9).Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print Cited Medium: Internet ISSN:

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