ArticleJournal of structural and functional genomics2004
NMR for structural proteomics of Thermotoga maritima: screening and structure determination.
Article in Journal of structural and functional genomics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 33 citations in OpenAlex.
- Proteomic perspectives on thermotolerant microbes: an updated review.Molecular biology reports · 2022Review
- Identification of a Novel Epoxyqueuosine Reductase Family by Comparative Genomics.ACS chemical biology · 2017Article
- NMR in structural genomics to increase structural coverage of the protein universe: Delivered by Prof. Kurt Wüthrich on 7 July 2013 at the 38th FEBS Congress in St. Petersburg, Russia.The FEBS journal · 2016Article
- Screening proteins for NMR suitability.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Electrospray ionization-induced protein unfolding.Journal of the American Society for Mass Spectrometry · 2012Article
- Rapid, robotic, small-scale protein production for NMR screening and structure determination.Protein science : a publication of the Protein Society · 2010Article
- The impact of extremophiles on structural genomics (and vice versa).Extremophiles : life under extreme conditions · 2008Review
- Magnetic susceptibility-induced alignment of proteins in reverse micelles.Journal of the American Chemical Society · 2006Article
- Expression, purification, and characterization of Thermotoga maritima membrane proteins for structure determination.Protein science : a publication of the Protein Society · 2006Article
- Length-dependent prediction of protein intrinsic disorder.BMC bioinformatics · 2006Article
- Automated protein NMR structure determination in crude cell-extract.Journal of biomolecular NMR · 2006Article
- Towards miniaturization of a structural genomics pipeline using micro-expression and microcoil NMR.Journal of structural and functional genomics · 2005Article
- NMR structure of the conserved hypothetical protein TM0487 from Thermotoga maritima: implications for 216 homologous DUF59 proteins.Protein science : a publication of the Protein Society · 2005Article
- Structural genomics of the severe acute respiratory syndrome coronavirus: nuclear magnetic resonance structure of the protein nsP7.Journal of virology · 2005Article
- Optimization of resolution and sensitivity of 4D NOESY using multi-dimensional decomposition.Journal of biomolecular NMR · 2005Article
- NMR screening and crystal quality of bacterially expressed prokaryotic and eukaryotic proteins in a structural genomics pipeline.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Shotgun crystallization strategy for structural genomics II: crystallization conditions that produce high resolution structures for T. maritima proteins.Journal of structural and functional genomics · 2005Article
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 at 3 institutions in 1 country.
Funding
Abstract
This paper describes the NMR screening of 141 small (<15 kDa) recombinant Thermotoga maritima proteins for globular folding. The experimental data shows that approximately 25% of the screened proteins are folded under our screening conditions, which makes this procedure an important step for selecting those proteins that are suitable for structure determination. A comparison of screening based either on 1D 1H NMR with unlabeled proteins or on 2D [1H,15N]-COSY with uniformly 15N-labeled proteins is presented, and a comprehensive analysis of the 1D 1H NMR screening data is described. As an illustration of the utility of these methods to structural proteomics, the NMR structure determination of TM1492 (ribosomal protein L29) is presented. This 66-residue protein consists of a N-terminal 3(10)-helix and two long alpha-helices connected by a tight turn centered about glycine 35, where conserved leucine and isoleucine residues in the two alpha-helices form a small hydrophobic core.
Indexed as
Identifiers
What 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.