ArticleJournal of proteome research2007
Sulfation, the up-and-coming post-translational modification: its role and mechanism in protein-protein interaction.
Article in Journal of proteome research, 2007. 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
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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
17 citing papers in PubMed, 36 citations in OpenAlex.
- Understanding peptide hormones: from precursor proteins to bioactive molecules.Trends in biochemical sciences · 2025Review
- Substrate binding plasticity revealed by Cryo-EM structures of SLC26A2.Nature communications · 2024Article
- The acetyltransferase BmCBP changes the acetylation modification of BmSP3 and affects its protein expression in silkworm, Bombyx mori.Molecular biology reports · 2023Article
- Small leucine rich proteoglycans: Biology, function and their therapeutic potential in the ocular surface.The ocular surface · 2023Review
- Tyrosine O-sulfation proteoforms affect HIV-1 monoclonal antibody potency.Scientific reports · 2022Article
- Human γS-Crystallin Resists Unfolding Despite Extensive Chemical Modification from Exposure to Ionizing Radiation.The journal of physical chemistry. B · 2022Article
- Functional genetic encoding of sulfotyrosine in mammalian cells.Nature communications · 2020Article
- Negative Ion Mode Collision-Induced Dissociation for Analysis of Protein Arginine Methylation.Journal of the American Society for Mass Spectrometry · 2019Article
- Involvement of sulfated biopolymers in adhesive secretions produced by marine invertebrates.Biology open · 2018Article
- Design and crystal structure of a native-like HIV-1 envelope trimer that engages multiple broadly neutralizing antibody precursors in vivo.The Journal of experimental medicine · 2017Article
- Modulation of Phosphopeptide Fragmentation via Dual Spray Ion/Ion Reactions Using a Sulfonate-Incorporating Reagent.Analytical chemistry · 2016Article
- Role of tyrosine-sulfated proteins in retinal structure and function.Experimental eye research · 2015Review
- novPTMenzy: a database for enzymes involved in novel post-translational modifications.Database : the journal of biological databases and curation · 2015Article
- Imaging of noncovalent complexes by MALDI-MS.Journal of the American Society for Mass Spectrometry · 2013Article
- Discrimination between peptide O-sulfo- and O-phosphotyrosine residues by negative ion mode electrospray tandem mass spectrometry.Journal of the American Society for Mass Spectrometry · 2011Article
- Simultaneous identification of tyrosine phosphorylation and sulfation sites utilizing tyrosine-specific bromination.Journal of the American Society for Mass Spectrometry · 2011Article
- The use of ECD/ETD to identify the site of electrostatic interaction in noncovalent complexes.Journal of the American Society for Mass Spectrometry · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Tyrosine sulfation is a post-translational modification entailing covalent attachment of sulfate to tyrosine residues. It takes place in the trans-Golgi, is necessary for the bioactivity of some proteins, and improves their ability to interact with other proteins. In the present work, we show that a protein containing a sulfated tyrosine with a delocalized negative charge forms a salt bridge with another protein if it has two or more adjacent arginine residues containing positive delocalized charges. These noncovalent complexes are so stable that, when submitted to collision induced dissociation, the peptides forming the complex dissociate. Just one covalent bond fragments, the covalent bond between the tyrosine oxygen and the SO3 sulfur, and is represented by the appearance of a new peak (basic peptide + SO3), suggesting that in some instances covalent bonds will break down before the noncovalent bonds between the arginine guanidinium and SO3 dissociate. The data implies that the dissociation pathway is preferred; however, fragmentation between tyrosine and the sulfate residue is a major pathway.
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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.