ArticleNature methods2012
Facile backbone structure determination of human membrane proteins by NMR spectroscopy.
Article in Nature methods, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 90 citations in OpenAlex.
- The SLC-ome of membrane transport: from molecular discovery to physiology and clinical applications.Physiological reviews · 2026Review
- Genetic or pharmacological inhibition of hepatic TMEM141 attenuates MASH and fibrosis via the ROS-HNF4α signaling pathway.Nature communications · 2026Article
- Transmembrane association of DDR1 and DDR2 mediated by Leucine zipper motifs.Magnetic resonance letters · 2025Article
- The potential antitumor mechanism and clinical potential of Higd-1a in colorectal cancer.Scientific reports · 2025Article
- Broken silence: 22,841 predicted deleterious synonymous variants identified in the human exome through computational analysis.Genetics and molecular biology · 2024Article
- Transmembrane protein 14A protects glomerular filtration barrier integrity.Physiological reports · 2023Article
- TmAlphaFold database: membrane localization and evaluation of AlphaFold2 predicted alpha-helical transmembrane protein structures.Nucleic acids research · 2023Article
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- Fatty acid export (FAX) proteins contribute to oil production in the green microalgaFrontiers in molecular biosciences · 2022Article
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- Regulation of Heme Synthesis by Mitochondrial Homeostasis Proteins.Frontiers in cell and developmental biology · 2022Review
- The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes.Nucleic acids research · 2021Article
- HIGD-Driven Regulation of CytochromeCells · 2020Review
- Amino-acid selective isotope labeling enables simultaneous overlapping signal decomposition and information extraction from NMR spectra.Journal of biomolecular NMR · 2020Article
- CombLabel: rational design of optimized sequence-specific combinatorial labeling schemes. Application to backbone assignment of membrane proteins with low stability.Journal of biomolecular NMR · 2019Article
- Reconstitution and NMR Characterization of the Ion-Channel Accessory Subunit Barttin in Detergents and Lipid-Bilayer Nanodiscs.Frontiers in molecular biosciences · 2019Article
- Solution NMR structure of yeast Rcf1, a protein involved in respiratory supercomplex formation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Cell-free production and characterisation of human uncoupling protein 1-3.Biochemistry and biophysics reports · 2017Article
- Structural basis of mitochondrial dysfunction in response to cytochromeProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Highly Coarse-Grained Representations of Transmembrane Proteins.Journal of chemical theory and computation · 2017Article
Corrections and comments
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Authors and funding
16 authors at 4 institutions in 3 countries.
Funding
Abstract
Although nearly half of today's major pharmaceutical drugs target human integral membrane proteins (hIMPs), only 30 hIMP structures are currently available in the Protein Data Bank, largely owing to inefficiencies in protein production. Here we describe a strategy for the rapid structure determination of hIMPs, using solution NMR spectroscopy with systematically labeled proteins produced via cell-free expression. We report new backbone structures of six hIMPs, solved in only 18 months from 15 initial targets. Application of our protocols to an additional 135 hIMPs with molecular weight <30 kDa yielded 38 hIMPs suitable for structural characterization by solution NMR spectroscopy without additional optimization.
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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.