ArticleJournal of synchrotron radiation2016
Synchrotron X-ray footprinting as a method to visualize water in proteins.
Article in Journal of synchrotron radiation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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.
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Who cites it
20 citing papers in PubMed, 25 citations in OpenAlex.
- Design and commissioning of a new synchrotron beamline dedicated to X-ray footprinting mass spectrometry.Journal of synchrotron radiation · 2026Article
- Recommendations and considerations for hydroxyl radical protein footprinting-mass spectrometry.Nature methods · 2026Review
- Enabling simultaneous photoluminescence spectroscopy and X-ray footprinting mass spectrometry to study protein conformation and interactions.Analytical methods : advancing methods and applications · 2025Article
- Residue-Specific Epitope Mapping of the PD-1/Nivolumab Interaction Using X-ray Footprinting Mass Spectrometry.Antibodies (Basel, Switzerland) · 2024Article
- Comparative Pore Structure and Dynamics for Bacterial Microcompartment Shell Protein Assemblies in Sheets or Shells.ACS omega · 2024Article
- Two DOT1 enzymes cooperatively mediate efficient ubiquitin-independent histone H3 lysine 76 tri-methylation in kinetoplastids.Nature communications · 2024Article
- Comparative Pore Structure and Dynamics for Bacterial Microcompartment Shell Protein Assemblies in Sheets or Shells.bioRxiv : the preprint server for biology · 2024Article
- The Solvation of theInternational journal of molecular sciences · 2022Article
- An automated liquid jet for fluorescence dosimetry and microsecond radiolytic labeling of proteins.Communications biology · 2022Article
- Hydroxyl radical mediated damage of proteins in low oxygen solution investigated using X-ray footprinting mass spectrometry.Journal of synchrotron radiation · 2021Article
- An ultrapotent synthetic nanobody neutralizes SARS-CoV-2 by stabilizing inactive Spike.Science (New York, N.Y.) · 2020Article
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- Beamline B21: high-throughput small-angle X-ray scattering at Diamond Light Source.Journal of synchrotron radiation · 2020Article
- An ultra-potent synthetic nanobody neutralizes SARS-CoV-2 by locking Spike into an inactive conformation.bioRxiv : the preprint server for biology · 2020Article
- Development of Container Free Sample Exposure for Synchrotron X-ray Footprinting.Analytical chemistry · 2020Article
- Water molecules mediate zinc mobility in the bacterial zinc diffusion channel ZIPB.The Journal of biological chemistry · 2019Article
- X-ray radiolytic labeling reveals the molecular basis of orange carotenoid protein photoprotection and its interactions with fluorescence recovery protein.The Journal of biological chemistry · 2019Article
- Using X-ray Footprinting and Mass Spectrometry to Study the Structure and Function of Membrane Proteins.Protein and peptide letters · 2019Review
- Recent Advances in X-Ray Hydroxyl Radical Footprinting at the Advanced Light Source Synchrotron.Protein and peptide letters · 2019Article
- Real-space analysis of radiation-induced specific changes with independent component analysis.Journal of synchrotron radiation · 2018Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The vast majority of biomolecular processes are controlled or facilitated by water interactions. In enzymes, regulatory proteins, membrane-bound receptors and ion-channels, water bound to functionally important residues creates hydrogen-bonding networks that underlie the mechanism of action of the macromolecule. High-resolution X-ray structures are often difficult to obtain with many of these classes of proteins because sample conditions, such as the necessity of detergents, often impede crystallization. Other biophysical techniques such as neutron scattering, nuclear magnetic resonance and Fourier transform infrared spectroscopy are useful for studying internal water, though each has its own advantages and drawbacks, and often a hybrid approach is required to address important biological problems associated with protein-water interactions. One major area requiring more investigation is the study of bound water molecules which reside in cavities and channels and which are often involved in both the structural and functional aspects of receptor, transporter and ion channel proteins. In recent years, significant progress has been made in synchrotron-based radiolytic labeling and mass spectroscopy techniques for both the identification of bound waters and for characterizing the role of water in protein conformational changes at a high degree of spatial and temporal resolution. Here the latest developments and future capabilities of this method for investigating water-protein interactions and its synergy with other synchrotron-based methods are discussed.
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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.