{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T15:26:35Z","timestamp":1781105195042,"version":"3.54.1"},"reference-count":34,"publisher":"National Academy of Sciences","issue":"16","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1998,8,4]]},"abstract":"<jats:p>\n                    Small heat shock proteins (sHSPs) belong to a family of 12- to 43-kDa proteins that are ubiquitous and are conserved in amino acid sequence among all organisms. A sHSP homologue of\n                    <jats:italic>Methanococcus jannaschii<\/jats:italic>\n                    , a hyperthermophilic Archaeon, forms a homogeneous multimer comprised of 24 monomers with a molecular mass of 400 kDa in contrast to other sHSPs that show heterogeneous oligomeric complexes. Electron microscopy analysis revealed a spherically shaped oligomeric structure \u224815\u201320 nm in diameter. The protein confers thermal protection of other proteins\n                    <jats:italic>in vitro<\/jats:italic>\n                    as found in other sHSPs.\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    cell extracts containing the protein were protected from heat-denatured precipitation when heated up to 100\u00b0C, whereas extracts from cells not expressing the protein were heat-sensitive at 60\u00b0C. Similar results were obtained when purified sHSP protein was added to an\n                    <jats:italic>E. coli<\/jats:italic>\n                    cell lysate. The protein also prevented the aggregation of two purified proteins: single-chain monellin (SCM) at 80\u00b0C and citrate synthase at 40\u00b0C.\n                  <\/jats:p>","DOI":"10.1073\/pnas.95.16.9129","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T10:31:39Z","timestamp":1027679499000},"page":"9129-9133","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":125,"title":["Small heat shock protein of\n                    <i>Methanococcus jannaschii<\/i>\n                    , a hyperthermophile"],"prefix":"10.1073","volume":"95","author":[{"given":"Rosalind","family":"Kim","sequence":"first","affiliation":[{"name":"Physical Biosciences Division of Lawrence Berkeley, National Laboratory and Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720-5230"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kyeong Kyu","family":"Kim","sequence":"additional","affiliation":[{"name":"Physical Biosciences Division of Lawrence Berkeley, National Laboratory and Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720-5230"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hisao","family":"Yokota","sequence":"additional","affiliation":[{"name":"Physical Biosciences Division of Lawrence Berkeley, National Laboratory and Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720-5230"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sung-Hou","family":"Kim","sequence":"additional","affiliation":[{"name":"Physical Biosciences Division of Lawrence Berkeley, National Laboratory and Department of Chemistry, University of California, Berkeley, Berkeley, CA 94720-5230"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1998,8,4]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1038\/355033a0"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.bi.62.070193.002025"},{"key":"e_1_3_3_3_2","first-page":"457","volume-title":"The Biology of Heat Shock Proteins and Molecular Chaperones","author":"Parsell D A","year":"1994","unstructured":"D A Parsell, S Lindquist The Biology of Heat Shock Proteins and Molecular Chaperones, eds R I Morimoto, A Tissieres, C Georgopoulos (Cold Spring Harbor Lab. 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