ArticleThe EMBO journal2003
Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry.
Article in The EMBO journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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
27 citing papers in PubMed, 53 citations in OpenAlex.
- MEMBRANE PROTEIN STRUCTURES AND INTERACTIONS FROM COVALENT LABELING COUPLED WITH MASS SPECTROMETRY.Mass spectrometry reviews · 2022Review
- Chemical Approaches for Studying the Biology and Pharmacology of Membrane Transporters: The Histidine/Large Amino Acid Transporter SLC7A5 as a Benchmark.Molecules (Basel, Switzerland) · 2021Review
- Free-Radical Membrane Protein Footprinting by Photolysis of Perfluoroisopropyl Iodide Partitioned to Detergent Micelle by Sonication.Angewandte Chemie (International ed. in English) · 2021Article
- Chemical Targeting of Membrane Transporters: Insights into Structure/Function Relationships.ACS omega · 2020Review
- It takes two to tango: The dance of the permease.The Journal of general physiology · 2019Review
- Topological Dissection of the Membrane Transport Protein Mhp1 Derived from Cysteine Accessibility and Mass Spectrometry.Analytical chemistry · 2017Article
- Review
- Fast Photochemical Oxidation of Proteins Maps the Topology of Intrinsic Membrane Proteins: Light-Harvesting Complex 2 in a Nanodisc.Analytical chemistry · 2016Article
- A new window into the molecular physiology of membrane proteins.The Journal of physiology · 2015Review
- Galactoside-binding site in LacY.Biochemistry · 2014Article
- Structure of sugar-bound LacY.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Detergent-free mass spectrometry of membrane protein complexes.Nature methods · 2013Article
- Topological mapping methods for α-helical bacterial membrane proteins--an update and a guide.MicrobiologyOpen · 2013Review
- Integral membrane proteins and bilayer proteomics.Analytical chemistry · 2013Review
- Dissection of mechanistic principles of a secondary multidrug efflux protein.Molecular cell · 2012Article
- Validation of membrane protein topology models by oxidative labeling and mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
- Ultra-thin layer MALDI mass spectrometry of membrane proteins in nanodiscs.Analytical and bioanalytical chemistry · 2012Article
- Mass spectrometry accelerates membrane protein analysis.Trends in biochemical sciences · 2011Review
- Site-directed mutagenesis combined with oxidative methionine labeling for probing structural transitions of a membrane protein by mass spectrometry.Journal of the American Society for Mass Spectrometry · 2010Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Integration of biochemical and biophysical data on the lactose permease of Escherichia coli has culminated in a molecular model that predicts substrate-protein proximities which include interaction of a hydroxyl group in the galactopyranosyl ring with Glu269. In order to test this hypothesis, we studied covalent modification of carboxyl groups with carbodiimides using electrospray ionization mass spectrometry (ESI-MS) and demonstrate that substrate protects the permease against carbodiimide reactivity. Further more, a significant proportion of the decrease in carbodiimide reactivity occurs specifically in a nanopeptide containing Glu269. In contrast, carbodiimide reactivity of mutant Glu269-->Asp that exhibits lower affinity is unaffected by substrate. By monitoring the ability of different substrate analogs to protect against carbodiimide modification of Glu269, it is suggested that the C-3 OH group of the galactopyranosyl ring may play an important role in specificity, possibly by H-bonding with Glu269. The approach demonstrates that mass spectrometry can provide a powerful means of analyzing ligand interactions with integral membrane proteins.
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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.