{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,28]],"date-time":"2026-09-28T19:05:41Z","timestamp":1790622341849,"version":"4.1.0"},"reference-count":42,"publisher":"National Academy of Sciences","issue":"2","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2002,1,22]]},"abstract":"<jats:p>\n                    RING domains act in a variety of essential cellular processes but have no general function ascribed to them. Here, we observe that purified arenaviral protein Z, constituted almost entirely by its RING domain, self-assembles\n                    <jats:italic>in vitro<\/jats:italic>\n                    into spherical structures that resemble functional bodies formed by Z in infected cells. By using a variety of biophysical methods we provide a thermodynamic and kinetic framework for the RING-dependent self-assembly of Z. Assembly appears coupled to substantial conformational reorganization and changes in zinc coordination of site II of the RING. Thus, the rate-limiting nature of conformational reorganization observed in the folding of monomeric proteins can also apply to the assembly of macromolecular scaffolds. These studies describe a unique mechanism of nonfibrillar homogeneous self-assembly and suggest a general function of RINGs in the formation of macromolecular scaffolds that are positioned to integrate biochemical processes in cells.\n                  <\/jats:p>","DOI":"10.1073\/pnas.012317299","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:36:44Z","timestamp":1027679804000},"page":"667-672","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":83,"title":["Self-assembly properties of a model RING domain"],"prefix":"10.1073","volume":"99","author":[{"given":"Alex","family":"Kentsis","sequence":"first","affiliation":[{"name":"Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York University, New York, NY 10029"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald E.","family":"Gordon","sequence":"additional","affiliation":[{"name":"Department of Physiology and Biophysics, Mount Sinai School of Medicine, New York University, New York, NY 10029"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katherine L. 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