REFERENCES CITING FB REAGENTS PRODUCTS AND SERVICES
2021
Nerli, Santrupti, et al. "Backbone-independent NMR resonance assignments of methyl probes in large proteins." Nature communications 12.1 (2021): 1-13.
Dubey, Abhinav, et al. "Local Deuteration Enables NMR Observation of Methyl Groups in Proteins from Eukaryotic and Cell‐Free Expression Systems." Angewandte Chemie International Edition (2021).
Gaussmann, Stefan, et al. "Membrane interactions of the peroxisomal proteins PEX5 and PEX14." Frontiers in cell and developmental biology 9 (2021)
Nimerovsky, Evgeny, et al. "Proton Detected Solid-State NMR of Membrane Proteins at 28 Tesla and 100 Khz Magic-Angle Spinning." (2021).
2020
Scheidt, Holger A., et al. "Light-induced lipid mixing implies a causal role of lipid splay in membrane fusion." Biochimica et Biophysica Acta (BBA)-Biomembranes 1862.11 (2020): 183438.
Schuster, Matthias, et al. "Optimizing the α1B-adrenergic receptor for solution NMR studies." Biochimica et Biophysica Acta (BBA)-Biomembranes(2020):183354 https://doi.org/10.1016/j.bbamem.2020.183354
Bibow, Stefan, et al. "Detergent titration as an efficient method for NMR resonance assignments of membrane proteins in lipid-bilayer nanodiscs." Analytical Chemistry 2020
Piai, Alessandro, et al. "Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein." Nature Communications 2020, 11.1, 1-12 https://doi.org/10.1038/s41467-020-16165-0
Taylor et al. Structure and physiological function of the human KCNQ1 channel voltage sensor intermediate state. eLife 2020;9:e53901 DOI: 10.7554/eLife.53901
Böhm et al. The Structural Basis for Low Conductance in the Membrane Protein VDAC upon β-NADH Binding and Voltage Gating. Structure 2019, 28, 1-9 https://doi.org/10.1016/j.str.2019.11.015
Movelan et al. Imidazole–Imidazole Hydrogen Bonding in the pH-Sensing Histidine Side Chains of Influenza A M2. J Am Chem Soc 2020, Article ASAP DOI: 10.1021/jacs.9b10984
2019
Bibow, S. “Opportunities and challenges of backbone, sidechain and RDC experiments to study membrane protein dynamics in a detergent-free lipid environment using solution state NMR” Frontiers in molecular biosciences 2019, 6, 103.
Bayrhuber, Monika, et al. "NMR solution structure and functional behavior of the human proton channel." Biochemistry (2019). https://doi.org/10.1021/acs.biochem.9b00471
Toyama, Yuki and Ichio Shimada. "Frequency selective coherence transfer NMR spectroscopy to study the structural dynamics of high molecular weight proteins." Journal of Magnetic Resonance (2019). https://doi.org/10.1016/j.jmr.2019.05.004
Boeszoermenyi, A., Chhabra, S., Dubey, A., Radeva, D. L., Burdzhiev, N. T., Chanev, C. D., Petrov, O. I., Gelev, V. M., Zhang, M., Anklin, C., Kovacs, H., Wagner, G., Kuprov, I., Takeuchi, K., Arthanari, H. Aromatic 19 F-13 C TROSY: a background-free approach to probe biomolecular structure, function, and dynamics. Nature methods (2019) https://doi.org/10.1038/s41592-019-0334-x
2018
Brazin, K. N., Mallis, R. J. et al. The T cell antigen receptor α transmembrane domain coordinates triggering through regulation of bilayer immersion and CD3 subunit associations. Immunity (2018). https://doi.org/10.1016/j.immuni.2018.09.007
O’Brien, E.S., Lin, D.W., Fuglestad, B. et al. Improving yields of deuterated, methyl labeled protein by growing in H2O. J Biomol NMR 2018. https://doi.org/10.1007/s10858-018-0200-7
2017
Cuevas Arenas R, Danielczak B, Martel A, et al. Fast Collisional Lipid Transfer Among Polymer-Bounded Nanodiscs. Scientific Reports. 2017 ;7:45875. doi:10.1038/srep45875.
Hagn, F., Nasr, M. and Wagner, G. (2017). Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR. Nature Protocols, 13(1), pp.79-98.
Chadwick et al. NMR Structure of the C-Terminal Transmembrane Domain of the HDL Receptor, SR-BI, and a Functionally Relevant Leucine Zipper Motif. Structure 25 (3) (2017), 446-457.
Bibow et al. Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I. Nat. Struct. Mol. Biol. 24 (2017), 187–193.
2016
Laguerre A, Löhr F, Henrich E, et al. From nanodiscs to isotropic bicelles: a procedure for solution NMR studies of detergent sensitive integral membrane proteins. Structure . 2016; 24(10):1830-1841. doi:10.1016/j.str.2016.07.017.
Bugge et al. A combined computational and structural model of the full-length human prolactin receptor. Nature Communications 2016, 7:11578 | DOI: 10.1038/ncomms11578.
2015
Andreas, Loren B., et al. Structure and mechanism of the influenza A M218–60 dimer of dimers. J. Am. Chem. Soc. 137. 47 (2015), 14877-14886.
Brady et al. (2015). A conserved amphipathic helix is required for membrane tubule formation by Yop1p. PNAS IUE639–E648, doi: 10.1073/pnas.1415882112.
2014
Brazin, Kristine N. et al. Constitutively oxidized CXXC motifs within the CD3 heterodimeric ectodomains of the T cell receptor complex enforce the conformation of juxtaposed segments. Journal of Biological Chemistry 289.27 (2014): 18880-18892.
Linser, Rasmus, et al. Selective methyl labeling of eukaryotic membrane proteins using cell-free expression. J. Am. Chem. Soc. 136.32 (2014): 11308-11310.
2013
Hagn et al. (2013). Optimized Phospholipid Bilayer Nanodiscs Facilitate High-Resolution Structure Determination of Membrane Proteins. J Am Chem Soc, 135, 1919.
2012
Yu et al. (2012) Solution NMR Spectroscopic Characterization of Human VDAC-2 in Detergent Micelles and Lipid Bilayer Nanodiscs. Biochim Biophys Acta 1818, 1562.
Klammt, C. et al. Facile backbone structure determination of human membrane proteins by NMR spectroscopy Nature Methods May 20 2012; doi:10.1038/nmeth.2033.
2009
Hiller, S. et al. Coupled Decomposition of Four-Dimensional NOESY Spectra. J. Am. Chem. Soc. 2009, 131, 12970.
Hiller, S. et al. Backbone and ILV side chain methyl group assignments of the integral human membrane protein VDAC-1 J. Biomol. NMR. Nov. 22 2009.
2008-2003
Hiller, S. et al. Solution Structure of the integral human membrane protein VDAC-1 in detergent micelles. Science 2008, 321, 1206.
Reibarkh, M. et al. Identification of individual protein-ligand NOEs in the limit of intermediate exchange. J. Biomol. NMR 2006, 36, 1.
Park, S. et al. Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 2005, 13, 995.
Ito, T. et al. Solution structure of human initiation factor eIF2alpha reveals homology to the elongation factor eEF1B. Structure 2004, 12, 1693.
Gross, J. D. et al. A sensitive and robust method for obtaining intermolecular NOEs between side chains in large protein complexes. J. Biomol. NMR 2003, 25, 235.
We support Sci-Hub!