ReviewBiochemistry2020
Characterizing Post-Translational Modifications and Their Effects on Protein Conformation Using NMR Spectroscopy.
Review in Biochemistry, 2020. 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
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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.
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Who cites it
21 citing papers in PubMed, 59 citations in OpenAlex.
- Phosphorylation of NLRP6 at Serine 27 site is critical for NLRP6 inflammasome activation and neurological impairment in ischemic stroke.Cell communication and signaling : CCS · 2026Article
- Middle-Down Nuclear Magnetic Resonance for Therapeutic Monoclonal Antibody Glycan Profiling.Current protocols · 2025Article
- Metabolic Rewiring and Post-Translational Modifications: Unlocking the Mechanisms of Bone Turnover in Osteoporosis.Aging and disease · 2025Review
- Neoantigen-based immunotherapy: advancing precision medicine in cancer and glioblastoma treatment through discovery and innovation.Exploration of targeted anti-tumor therapy · 2025Review
- Time-resolved NMR detection of prolyl-hydroxylation in intrinsically disordered region of HIF-1α.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Post-translational modifications in the Protein Data Bank.Acta crystallographica. Section D, Structural biology · 2024Review
- FLiPPR: A Processor for Limited Proteolysis (LiP) Mass Spectrometry Data Sets Built on FragPipe.Journal of proteome research · 2024Article
- Map conformational landscapes of intrinsically disordered proteins with polymer physics quantities.Biophysical journal · 2024Article
- "It's Only a Model": When Protein Structure Predictions Need Experimental Validation, the Case of the HTLV-1 Tax Protein.Pathogens (Basel, Switzerland) · 2024Review
- Mass Spectrometry-Based Strategies for Assessing Human Exposure Using Hemoglobin Adductomics.Chemical research in toxicology · 2023Article
- FLiPPR: A Processor for Limited Proteolysis (LiP) Mass Spectrometry Datasets Built on FragPipe.bioRxiv : the preprint server for biology · 2023Article
- Glycan heterogeneity as a cause of the persistent fraction in HIV-1 neutralization.PLoS pathogens · 2023Article
- AlphaFold2 protein structure prediction: Implications for drug discovery.Current opinion in structural biology · 2023Review
- Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome.Journal of the American Chemical Society · 2022Article
- Pyranose Ring Puckering Thermodynamics for Glycan Monosaccharides Associated with Vertebrate Proteins.International journal of molecular sciences · 2021Article
- Segmental and site-specific isotope labelling strategies for structural analysis of posttranslationally modified proteins.RSC chemical biology · 2021Review
- On the Need to Tell Apart Fraternal Twins eEF1A1 and eEF1A2, and Their Respective Outfits.International journal of molecular sciences · 2021Review
- Phosphorylation Impacts Cu(II) Binding by ATCUN Motifs.Inorganic chemistry · 2021Article
- A deep analysis of the proteomic and phosphoproteomic alterations that occur in skeletal muscle after the onset of immobilization.The Journal of physiology · 2021Article
- ATR-FTIR spectroscopy and spectroscopic imaging for the analysis of biopharmaceuticals.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The diversity of the cellular proteome substantially exceeds the number of genes coded by the DNA of an organism because one or more residues in a majority of eukaryotic proteins are post-translationally modified (PTM) by the covalent conjugation of specific chemical groups. We now know that PTMs alter protein conformation and function in ways that are not entirely understood at the molecular level. NMR spectroscopy has been particularly successful as an analytical tool in elucidating the themes underlying the structural role of PTMs. In this Perspective, we focus on the NMR-based characterization of three abundant PTMs: phosphorylation, acetylation, and glycosylation. We detail NMR methods that have found success in detecting these modifications at a site-specific level. We also highlight NMR studies that have mapped the conformational changes ensuing from these PTMs as well as evaluated their relation to function. The NMR toolbox is expanding rapidly with experiments available to probe not only the average structure of biomolecules but also how this structure changes with time on time scales ranging from picoseconds to seconds. The atomic resolution insights into the biomolecular structure, dynamics, and mechanism accessible from NMR spectroscopy ensure that NMR will continue to be at the forefront of research in the structural biology of PTMs.
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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.