{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,1,15]],"date-time":"2026-01-15T00:08:04Z","timestamp":1768435684619,"version":"3.49.0"},"reference-count":49,"publisher":"Oxford University Press (OUP)","issue":"4","license":[{"start":{"date-parts":[[2023,7,3]],"date-time":"2023-07-03T00:00:00Z","timestamp":1688342400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"name":"Uehara Memorial Foundation, the Mochida Memorial Foundation for Medical and Pharmaceutical Research, the Takeda Science Foundation, and the KUMAYAKU Alumni Research Foundation"},{"name":"Grants-in-Aid for Scientific Research from the Japan Society for the Promotion of Science (JSPS","award":["JP18K06659 and JP21K06529"],"award-info":[{"award-number":["JP18K06659 and JP21K06529"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2023,9,29]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>Transthyretin (TTR) is a homo-tetrameric serum protein associated with sporadic and hereditary systemic amyloidosis. TTR amyloid formation proceeds by the dissociation of the TTR tetramer and the subsequent partial unfolding of the TTR monomer into an aggregation-prone conformation. Although TTR kinetic stabilizers suppress tetramer dissociation, a strategy for stabilizing monomers has not yet been developed. Here, we show that an N-terminal C10S mutation increases the thermodynamic stability of the TTR monomer by forming new hydrogen bond networks through the side chain hydroxyl group of Ser10. Nuclear magnetic resonance spectrometry and molecular dynamics simulation revealed that the Ser10 hydroxyl group forms hydrogen bonds with the main chain amide group of either Gly57 or Thr59 on the DE loop. These hydrogen bonds prevent the dissociation of edge strands in the DAGH and CBEF \u03b2-sheets during the unfolding of the TTR monomer by stabilizing the interaction between \u03b2-strands A and D and the quasi-helical structure in the DE loop. We propose that introducing hydrogen bonds to connect the N-terminal region to the DE loop reduces the amyloidogenic potential of TTR by stabilizing the monomer.<\/jats:p>","DOI":"10.1093\/jb\/mvad049","type":"journal-article","created":{"date-parts":[[2023,7,4]],"date-time":"2023-07-04T04:37:17Z","timestamp":1688445437000},"page":"355-370","source":"Crossref","is-referenced-by-count":1,"title":["Hydrogen bonds connecting the N-terminal region and the DE loop stabilize the monomeric structure of transthyretin"],"prefix":"10.1093","volume":"174","author":[{"given":"Yuki","family":"Inada","sequence":"first","affiliation":[{"name":"Kumamoto University Department of Analytical and Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yuichiro","family":"Ono","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Analytical and Biophysical Chemistry, School of Pharmacy, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kyo","family":"Okazaki","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Analytical and Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Takuma","family":"Yamashita","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Analytical and Biophysical Chemistry, School of Pharmacy, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tomoyuki","family":"Kawaguchi","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Analytical and Biophysical Chemistry, School of Pharmacy, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shingo","family":"Kawano","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Analytical and Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Yoshihiro","family":"Kobashigawa","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Analytical and Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shoko","family":"Shinya","sequence":"additional","affiliation":[{"name":"Institute for Protein Research, Osaka University Laboratory of Molecular Biophysics, , 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Chojiro","family":"Kojima","sequence":"additional","affiliation":[{"name":"Institute for Protein Research, Osaka University Laboratory of Molecular Biophysics, , 3-2 Yamadaoka, Suita, Osaka 565-0871, Japan"},{"name":"Yokohama National University Division of Materials Science and Chemical Engineering, Graduate School of Engineering, , 79-5 Tokiwadai, Hodogaya-ku, Yokohama 240-8501, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Tsuyoshi","family":"Shuto","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hirofumi","family":"Kai","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Hiroshi","family":"Morioka","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Analytical and Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Takashi","family":"Sato","sequence":"additional","affiliation":[{"name":"Kumamoto University Department of Analytical and Biophysical Chemistry, Graduate School of Pharmaceutical Sciences, , 5-1 Oe-honmachi, Chuo-ku, Kumamoto 862-0973, Japan"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"286","published-online":{"date-parts":[[2023,7,3]]},"reference":[{"key":"2023092819590688900_ref1","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1038\/s41582-019-0210-4","article-title":"Hereditary transthyretin amyloidosis: a model of medical progress for a fatal disease","volume":"15","author":"Adams","year":"2019","journal-title":"Nat. Rev. Neurol."},{"key":"2023092819590688900_ref2","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1111\/joim.12585","article-title":"One mutation, two distinct disease variants: unravelling the impact of transthyretin amyloid fibril composition","volume":"281","author":"Suhr","year":"2017","journal-title":"J. Intern. Med."},{"key":"2023092819590688900_ref3","doi-asserted-by":"crossref","first-page":"134","DOI":"10.1007\/s00415-017-8640-7","article-title":"Genetic and clinical characteristics of hereditary transthyretin amyloidosis in endemic and non-endemic areas: experience from a single-referral center in Japan","volume":"265","author":"Yamashita","year":"2018","journal-title":"J. Neurol."},{"key":"2023092819590688900_ref4","doi-asserted-by":"crossref","first-page":"160","DOI":"10.3109\/13506120308998998","article-title":"Tabulation of human transthyretin (TTR) variants, 2003","volume":"10","author":"Connors","year":"2003","journal-title":"Amyloid"},{"key":"2023092819590688900_ref5","doi-asserted-by":"crossref","first-page":"2843","DOI":"10.1073\/pnas.87.7.2843","article-title":"Fibril in senile systemic amyloidosis is derived from normal transthyretin","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"2023092819590688900_ref6","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1016\/j.ijcard.2013.10.033","article-title":"Effect of age and sex differences on wild-type transthyretin amyloid formation in familial amyloidotic polyneuropathy: a proteomic approach","volume":"170","author":"Tasaki","year":"2013","journal-title":"Int. J. Cardiol."},{"key":"2023092819590688900_ref7","doi-asserted-by":"crossref","first-page":"1039","DOI":"10.1126\/science.7754382","article-title":"Structure of a Complex of Two Plasma Proteins: Transthyretin and Retinol-Binding Protein","volume":"268","author":"Monaco","year":"1995","journal-title":"Science"},{"key":"2023092819590688900_ref8","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1016\/0022-2836(78)90368-6","article-title":"Structure of prealbumin: secondary, tertiary and quaternary interactions determined by Fourier refinement at 1.8 \u00c5","volume":"121","author":"Blake","year":"1978","journal-title":"J. Mol. Biol."},{"key":"2023092819590688900_ref9","doi-asserted-by":"crossref","first-page":"649","DOI":"10.1006\/jmbi.2000.4078","article-title":"A comparative analysis of 23 structures of the amyloidogenic protein transthyretin","volume":"302","author":"H\u00f6rnberg","year":"2000","journal-title":"J. Mol. 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Lett."},{"key":"2023092819590688900_ref24","doi-asserted-by":"crossref","first-page":"49707","DOI":"10.1074\/jbc.M306748200","article-title":"In vitro and in vivo interactions of homocysteine with human plasma transthyretin","volume":"278","author":"Lim","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2023092819590688900_ref25","doi-asserted-by":"crossref","first-page":"11654","DOI":"10.1074\/jbc.M210798200","article-title":"X-ray absorption spectroscopy reveals a substantial increase of sulfur oxidation in transthyretin (TTR) upon fibrillization","volume":"278","author":"Gales","year":"2003","journal-title":"J. Biol. Chem."},{"key":"2023092819590688900_ref26","doi-asserted-by":"crossref","first-page":"8756","DOI":"10.1021\/bi030077a","article-title":"Cys10 mixed disulfides make transthyretin more amyloidogenic under mildly acidic conditions","volume":"42","author":"Zhang","year":"2003","journal-title":"Biochemistry"},{"key":"2023092819590688900_ref27","doi-asserted-by":"crossref","first-page":"9079","DOI":"10.1021\/bi050378f","article-title":"Cys-10 mixed disulfide modifications exacerbate transthyretin familial variant amyloidogenicity: a likely explanation for variable clinical expression of amyloidosis and the lack of pathology in C10S\/V30M transgenic mice?","volume":"44","author":"Zhang","year":"2005","journal-title":"Biochemistry"},{"key":"2023092819590688900_ref28","doi-asserted-by":"crossref","first-page":"1349","DOI":"10.1002\/(SICI)1522-2683(19990601)20:7<1349::AID-ELPS1349>3.0.CO;2-5","article-title":"Electrically neutral microheterogeneity of human plasma transthyretin (prealbumin) detected by isoelectric focusing in urea gradients","volume":"20","author":"Altland","year":"1999","journal-title":"Electrophoresis"},{"key":"2023092819590688900_ref29","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1007\/s10048-003-0160-1","article-title":"Sulfite and base for the treatment of familial amyloidotic polyneuropathy: two additive approaches to stabilize the conformation of human amyloidogenic transthyretin","volume":"5","author":"Altland","year":"2004","journal-title":"Neurogenetics"},{"key":"2023092819590688900_ref30","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/S0002-9440(10)63123-9","article-title":"Cysteine 10 is a key residue in amyloidogenesis of human transthyretin Val30Met","volume":"164","author":"Takaoka","year":"2004","journal-title":"Am. J. Pathol."},{"key":"2023092819590688900_ref31","doi-asserted-by":"crossref","first-page":"2501","DOI":"10.1038\/sj.emboj.7601685","article-title":"Endoplasmic reticulum quality control regulates the fate of transthyretin variants in the cell","volume":"26","author":"Sato","year":"2007","journal-title":"EMBO J."},{"key":"2023092819590688900_ref32","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1007\/s10858-008-9296-5","article-title":"Attachment of an NMR-invisible solubility enhancement tag using a sortase-mediated protein ligation method","volume":"43","author":"Kobashigawa","year":"2009","journal-title":"J. Biomol. NMR"},{"key":"2023092819590688900_ref33","doi-asserted-by":"crossref","first-page":"28.9.1","DOI":"10.1002\/0471140864.ps2809s79","article-title":"Current protocols in protein science: analysis of protein stability and ligand interactions by thermal shift assay","volume":"79","author":"Huynh","year":"2015","journal-title":"Curr. Protoc. Protein Sci."},{"key":"2023092819590688900_ref34","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/BF00197809","article-title":"NMRPipe: A multidimensional spectral processing system based on UNIX pipes","volume":"6","author":"Delaglio","year":"1995","journal-title":"J. Biomol. NMR"},{"key":"2023092819590688900_ref35","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1038\/nsmb.3380","article-title":"Mechanistic basis for the recognition of a misfolded protein by the molecular chaperone Hsp90","volume":"24","author":"Oroz","year":"2017","journal-title":"Nat. Struct. Mol. Biol."},{"key":"2023092819590688900_ref36","doi-asserted-by":"crossref","first-page":"2416","DOI":"10.1016\/S0021-9258(18)53792-3","article-title":"The x-ray crystal structure refinements of normal human transthyretin and the amyloidogenic Val-30\u2013&gt;Met variant to 1.7-A resolution","volume":"268","author":"Hamilton","year":"1993","journal-title":"J. Biol. Chem."},{"key":"2023092819590688900_ref37","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014a visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"2023092819590688900_ref38","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1016\/j.softx.2015.06.001","article-title":"GROMACS: High performance molecular simulations through multi-level parallelism from laptops to supercomputers","volume":"1-2","author":"Abraham","year":"2015","journal-title":"Softwarex."},{"key":"2023092819590688900_ref39","doi-asserted-by":"crossref","first-page":"71","DOI":"10.1038\/nmeth.4067","article-title":"CHARMM36m: an improved force field for folded and intrinsically disordered proteins","volume":"14","author":"Huang","year":"2017","journal-title":"Nat. Methods"},{"key":"2023092819590688900_ref40","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1021\/ja036959e","article-title":"Improved treatment of the protein backbone in empirical force fields","volume":"126","author":"MacKerell","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"2023092819590688900_ref41","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: an N \u00b7log(N) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J. Chem. Phys."},{"key":"2023092819590688900_ref42","doi-asserted-by":"crossref","first-page":"1463","DOI":"10.1002\/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.0.CO;2-H","article-title":"LINCS: A linear constraint solver for molecular simulations","volume":"18","author":"Hess","year":"1997","journal-title":"J. Comput. Chem."},{"key":"2023092819590688900_ref43","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/0263-7855(96)00018-5","article-title":"VMD: Visual molecular dynamics","volume":"14","author":"Humphrey","year":"1996","journal-title":"J. Mol. Graph."},{"key":"2023092819590688900_ref44","doi-asserted-by":"crossref","first-page":"1995","DOI":"10.1016\/j.bpj.2020.08.043","article-title":"Edge strand dissociation and conformational changes in transthyretin under amyloidogenic conditions","volume":"119","author":"Childers","year":"2020","journal-title":"Biophys. J."},{"key":"2023092819590688900_ref45","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.bbapap.2006.10.015","article-title":"Structural basis for the protective role of sulfite against transthyretin amyloid formation","volume":"1774","author":"Gales","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"2023092819590688900_ref46","doi-asserted-by":"crossref","first-page":"4421","DOI":"10.1021\/acs.biochem.8b00642","article-title":"NMR measurements reveal the structural basis of transthyretin destabilization by pathogenic mutations","volume":"57","author":"Leach","year":"2018","journal-title":"Biochemistry"},{"key":"2023092819590688900_ref47","doi-asserted-by":"crossref","first-page":"2997","DOI":"10.1021\/ct300284c","article-title":"Routine access to millisecond time scale events with accelerated molecular synamics","volume":"8","author":"Pierce","year":"2012","journal-title":"J. Chem. Theory Comput."},{"key":"2023092819590688900_ref48","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/S0009-2614(99)01123-9","article-title":"Replica-exchange molecular dynamics method for protein folding","volume":"314","author":"Sugita","year":"1999","journal-title":"Chem. Phys. Lett."},{"key":"2023092819590688900_ref49","doi-asserted-by":"crossref","first-page":"12562","DOI":"10.1073\/pnas.202427399","article-title":"Escaping free-energy minima","volume":"99","author":"Laio","year":"2002","journal-title":"Proc. Natl. Acad. Sci. U. S. A."}],"container-title":["The Journal of Biochemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/academic.oup.com\/jb\/advance-article-pdf\/doi\/10.1093\/jb\/mvad049\/50850989\/mvad049.pdf","content-type":"application\/pdf","content-version":"am","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/jb\/article-pdf\/174\/4\/355\/51790822\/mvad049.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/academic.oup.com\/jb\/article-pdf\/174\/4\/355\/51790822\/mvad049.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,28]],"date-time":"2023-09-28T20:02:28Z","timestamp":1695931348000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jb\/article\/174\/4\/355\/7218525"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,7,3]]},"references-count":49,"journal-issue":{"issue":"4","published-online":{"date-parts":[[2023,7,3]]},"published-print":{"date-parts":[[2023,9,29]]}},"URL":"https:\/\/doi.org\/10.1093\/jb\/mvad049","relation":{},"ISSN":["0021-924X","1756-2651"],"issn-type":[{"value":"0021-924X","type":"print"},{"value":"1756-2651","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2023,10]]},"published":{"date-parts":[[2023,7,3]]}}}