A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation by M. F. Symmons and others 2026-11-05
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M. F. Symmons, G. H. Jones, B. F. Luisi; Structure8(11),1215–1226(2000), DOI10.1016/S0969-2126(00)00521-9. Publisher primary abstract www.sciencedirect.com/science/article/pii/S0969212600005219 : X-ray structure of Streptomyces antibioticus PNPase without bound RNA but with tungstate at catalytic sites, trimer and central channel. A possible channel role in processivity is proposed, not direct observation of RNA transit. No initials expanded.
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Running rings around RNA: a superfamily of phosphate-dependent RNases by Martyn F. Symmons and others 2026-11-05
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Verified locator: Original authors own 2002 account, Trends Biochem Sci27(1),11–18, DOI10.1016/S0968-0004(01)01999-5. Published full names Martyn F Symmons, Ben F Luisi and George H Jones verified; no middle initials expanded. Used as primary byline/identity evidence, with 2000 primary experimental paper for structure claims.
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