Singapore Science News API

{
    "totalArticles": 17020,
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        {
            "id": "6ec35dff79329d5d64eb8baac4f898b0",
            "title": "Scientists may have found the source of the most powerful neutrino ever detected",
            "description": "A mysterious particle from deep space has scientists buzzing after the most energetic neutrino ever detected slammed through the Mediterranean Sea. Now, researchers think they may have identified the cosmic “culprits” behind it: blazars — supermassive black holes blasting jets of matter straight toward Earth.",
            "content": "Now, a new study published in the Journal of Cosmology and Astroparticle Physics (JCAP) suggests the particle may have originated from blazars, some of the universe's most extreme objects. Blazars are active galactic nuclei powered by supermassive bl... [5297 chars]",
            "url": "https://www.sciencedaily.com/releases/2026/05/260523103912.htm",
            "image": "https://www.sciencedaily.com/images/1920/active-black-hole-jet.webp",
            "publishedAt": "2026-05-24T10:58:42Z",
            "lang": "en",
            "source": {
                "id": "81a05fd2712964dbdb32b1c6a27646fd",
                "name": "ScienceDaily",
                "url": "https://www.sciencedaily.com"
            }
        },
        {
            "id": "70a8242b9225a2a3eb3df91974b5ffa2",
            "title": "Scientists Finally Discover Why Gold Never Rusts",
            "description": "Researchers discovered that gold’s unusual resistance to rust comes from protective atomic surface patterns that block oxygen.",
            "content": "A new study explains why the “noble metal” resists oxidation and how surface modifications could unleash its catalytic power.\nGold has long been prized for its stability, but in the world of chemistry, that stability of gold is precisely what has cau... [2024 chars]",
            "url": "https://www.techexplorist.com/gold-never-rusts/103076/",
            "image": "https://www.techexplorist.com/wp-content/uploads/2026/05/gold.webp",
            "publishedAt": "2026-05-23T16:43:46Z",
            "lang": "en",
            "source": {
                "id": "384f05ddf6ed854b082cdea0d2279b35",
                "name": "Tech Explorist",
                "url": "https://www.techexplorist.com"
            }
        },
        {
            "id": "f589d35ecb70efa3192f38e68e923c79",
            "title": "Reconstitution of protein arginylation pathways in bacteria for robust identification and quantification",
            "description": "ATE1 is a conserved enzyme that catalyzes the covalent addition of arginine to proteins bearing N-terminal or mid-chain Asp and Glu residues. N-terminal (Nt) arginylation can also occur on Cys, Asn, and Gln following enzymatic conversion, often marking proteins for degradation. Essential for development, this pathway contributes to protein quality control and stress responses. Despite growing insight into ATE1 structure and function, the mechanisms governing its substrate selectivity and coordination with upstream oxygenase and deamidase remain poorly defined. Here, we reconstitute the human processing cascades that generate Nt-arginylated proteins in E. coli, enabling step-resolved analysis of arginylation outcomes in a cellular context. By co-expressing human ADO, NTAN1, or NTAQ1 with ATE1 in a modular system, we achieved efficient conversion of Nt-Cys, Asn, and Gln into arginylation-permissive forms, recapitulating key features of upstream processing. Using this platform, we demonstrated that N-terminal processing is efficient and that ATE1 preferentially modifies protein N-termini over internal acidic residues. Mid-chain arginylation of α-synuclein was detectable but occurred at low frequency, with no major differences in site selectivity observed across the ATE1 isoforms tested. Together, this bacterial reconstitution system provides a scalable experimental platform for quantitative, protein-level analysis of ATE1 substrate specificity under defined conditions. A bacterial reconstitution system for human arginylation pathways enables quantitative, step-resolved analysis of ATE1 activity, revealing efficient N-terminal arginylation and low-frequency mid-chain modification.",
            "content": "This work was supported by grants from NIH R35 GM150678 to Y.Z., NIH R21 CA292191 to Z.L., NIH R01 HL177113 to Z.L. and B.A.G., Research Education Component (REC) through an NIA grant P30AG066444 to Z.L., Case Comprehensive Cancer Center (P30CA043703... [1262 chars]",
            "url": "https://www.nature.com/articles/s42003-026-10275-z?error=cookies_not_supported&code=4c96dd69-9744-4593-8c0d-1920cff0f70a",
            "image": "https://www.nature.com/static/images/favicons/nature/favicon-48x48-b52890008c.png",
            "publishedAt": "2026-05-23T09:08:21Z",
            "lang": "en",
            "source": {
                "id": "7abf0df285fbe93cdccffcc7c4088737",
                "name": "Nature",
                "url": "https://www.nature.com"
            }
        }
    ]
}