ArticleJournal of biomolecular NMR2004
A novel way of amino acid-specific assignment in (1)H-(15)N HSQC spectra with a wheat germ cell-free protein synthesis system.
Article in Journal of biomolecular NMR, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed.
- Easy Synthesis of Complex Biomolecular Assemblies: Wheat Germ Cell-Free Protein Expression in Structural Biology.Frontiers in molecular biosciences · 2021Review
- Review
- Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus.Journal of biomolecular NMR · 2016Article
- Active-site structure of the thermophilic Foc-subunit ring in membranes elucidated by solid-state NMR.Biophysical journal · 2014Article
- Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets.Journal of biomolecular NMR · 2013Article
- Biosynthetically directed ²H labelling for stereospecific resonance assignments of glycine methylene groups.Journal of biomolecular NMR · 2013Article
- Combinatorial triple-selective labeling as a tool to assist membrane protein backbone resonance assignment.Journal of biomolecular NMR · 2012Article
- Hydrogen exchange during cell-free incorporation of deuterated amino acids and an approach to its inhibition.Journal of biomolecular NMR · 2011Article
- A simplified recipe for assigning amide NMR signals using combinatorial 14N amino acid inverse-labeling.Journal of structural and functional genomics · 2011Article
- Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O.Journal of biomolecular NMR · 2011Article
- Functional expression of a two-transmembrane HtrII protein using cell-free synthesis.Biophysics (Nagoya-shi, Japan) · 2011Article
- An economical method for producing stable-isotope labeled proteins by the E. coli cell-free system.Journal of biomolecular NMR · 2010Article
- Engineering of a wheat germ expression system to provide compatibility with a high throughput pET-based cloning platform.Journal of structural and functional genomics · 2010Article
- Advances in protein NMR provided by the NIGMS Protein Structure Initiative: impact on drug discovery.Current opinion in drug discovery & development · 2010Review
- Practical cell-free protein synthesis system using purified wheat embryos.Nature protocols · 2010Article
- Cell-free expression and stable isotope labelling strategies for membrane proteins.Journal of biomolecular NMR · 2010Article
- NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system.Protein science : a publication of the Protein Society · 2009Article
- Cell-free translation of integral membrane proteins into unilamelar liposomes.Methods in enzymology · 2009Review
- A simple method for amino acid selective isotope labeling of recombinant proteins in E. coli.Journal of biomolecular NMR · 2008Article
- 1-13C amino acid selective labeling in a 2H15N background for NMR studies of large proteins.Journal of biomolecular NMR · 2007Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
For high-throughput protein structural analyses, it is indispensable to develop a reliable protein overexpression system. Although many protein overexpression systems, such as ones utilizing E. coli cells, have been developed, a lot of proteins functioning in solution still were synthesized as insoluble forms. Recently, a novel wheat germ cell-free protein synthesis system was developed, and many of such proteins were synthesized as soluble forms. This means that the applicability of this protein synthesis method to determination of the functional structures of soluble proteins. In our previous work, we synthesized (15)N-labeled proteins with this wheat germ cell-free system, and confirmed this applicability on the basis of the strong similarity between the (1)H-(15)N HSQC spectra for native proteins and the corresponding ones for synthesized ones. In this study, we developed a convenient and reliable method for amino acid selective assignment in (1)H-(15)N HSQC spectra of proteins, using several inhibitors for transaminases and glutamine synthase in the process of protein synthesis. Amino acid selective assignment in (1)H-(15)N HSQC spectra is a powerful means to monitor the features of proteins, such as folding, intermolecular interactions and so on. This is also the first direct experimental evidence of the presence of active transaminases and glutamine synthase in wheat germ extracts.
Indexed as
Identifiers
15452433What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.