The outer membrane vesicles (OMVs) produced by diderm bacteria have important roles in cell envelope homeostasis, secretion, interbacterial communication, and pathogenesis. The facultative intracellular pathogen Salmonella enterica Typhimurium (STm) activates OMV biogenesis inside the acidic vacuoles of host cells by upregulating the expression of the outer membrane (OM) protein PagC, one of the most robustly activated genes in a host environment. Here, we used solid-state nuclear magnetic...
[NMR paper] 129Xe NMR-Protein Sensor Reveals Cellular Ribose Concentration.
129Xe NMR-Protein Sensor Reveals Cellular Ribose Concentration.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles 129Xe NMR-Protein Sensor Reveals Cellular Ribose Concentration.
Anal Chem. 2020 Sep 08;:
Authors: Zemerov SD, Roose BW, Farenhem KL, Zhao Z, Stringer MA, Goldman A, Speicher DW, Dmochowski IJ
Abstract
Dysregulation of cellular ribose uptake can be indicative of metabolic abnormalities or tumorigenesis. However, analytical methods are...
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09-13-2020 09:18 AM
[ASAP] High-Resolution In Situ NMR Spectroscopy of Bacterial Envelope Proteins in Outer Membrane Vesicles
High-Resolution In Situ NMR Spectroscopy of Bacterial Envelope Proteins in Outer Membrane Vesicles
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.9b01123/20200406/images/medium/bi9b01123_0004.gif
Biochemistry
DOI: 10.1021/acs.biochem.9b01123
http://feeds.feedburner.com/~r/acs/bichaw/~4/2_SiKyocUYc
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04-07-2020 07:35 PM
[NMR paper] High-resolution in-situ NMR spectroscopy of bacterial envelope proteins in outer membrane vesicles.
High-resolution in-situ NMR spectroscopy of bacterial envelope proteins in outer membrane vesicles.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles High-resolution in-situ NMR spectroscopy of bacterial envelope proteins in outer membrane vesicles.
Biochemistry. 2020 Apr 01;:
Authors: Thoma J, Burmann BM
Abstract
The cell envelope of Gram-negative bacteria is an elaborate cellular environment, consisting of two lipid membranes separated by the aqueous...
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04-03-2020 09:41 PM
[NMR paper] Solid-state NMR Study of the YadA Membrane-Anchor Domain in the Bacterial Outer Membrane.
Solid-state NMR Study of the YadA Membrane-Anchor Domain in the Bacterial Outer Membrane.
Related Articles Solid-state NMR Study of the YadA Membrane-Anchor Domain in the Bacterial Outer Membrane.
Angew Chem Int Ed Engl. 2015 Aug 31;
Authors: Shahid SA, Nagaraj M, Chauhan N, Franks TW, Bardiaux B, Habeck M, Orwick-Rydmark M, Linke D, van Rossum BJ
Abstract
MAS-NMR was used to study the structure and dynamics at ambient temperatures of the membrane-anchor domain of YadA (YadA-M) in a pellet of the outer membrane of E. coli in...
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09-04-2015 12:45 PM
[NMR paper] High-resolution NMR reveals secondary structure and folding of amino Acid transporter from outer chloroplast membrane.
High-resolution NMR reveals secondary structure and folding of amino Acid transporter from outer chloroplast membrane.
Related Articles High-resolution NMR reveals secondary structure and folding of amino Acid transporter from outer chloroplast membrane.
PLoS One. 2013;8(10):e78116
Authors: Zook JD, Molugu TR, Jacobsen NE, Lin G, Soll J, Cherry BR, Brown MF, Fromme P
Abstract
Solving high-resolution structures for membrane proteins continues to be a daunting challenge in the structural biology community. In this study we report our...
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11-11-2013 01:30 AM
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
Mammalian production of an isotopically enriched outer domain of the HIV-1 gp120 glycoprotein for NMR spectroscopy.
J Biomol NMR. 2011 Jun 12;
Authors: Sastry M, Xu L, Georgiev IS, Bewley CA, Nabel GJ, Kwong PD
NMR spectroscopic characterization of the structure or the dynamics of proteins generally requires the production of samples isotopically enriched in (15)N, (13)C, or (2)H. The bacterial expression systems currently in use to...
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06-15-2011 01:15 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA.
J Am Chem Soc. 2011 Mar 1;
Authors: Renault M, Bos MP, Tommassen J, Baldus M
Multidomain proteins constitute a large part of prokaryotic and eukaryotic proteomes and play fundamental roles in various physiological processes. However, their structural characterization is challenging because of their large size and...
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03-03-2011 12:34 PM
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Solid-State NMR on a Large Multidomain Integral Membrane Protein: The Outer Membrane Protein Assembly Factor BamA
Marie Renault, Martine P. Bos, Jan Tommassen and Marc Baldus
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja109469c/aop/images/medium/ja-2010-09469c_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja109469c
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/9XN1qiW-S-I
In situ NMR reveals a pH sensor motif in an outer membrane protein that drives bacterial vesicle production
Linear Mode
