{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T23:10:22Z","timestamp":1791414622978,"version":"4.3.3"},"reference-count":60,"publisher":"Springer Science and Business Media LLC","issue":"7","license":[{"start":{"date-parts":[[2012,6,17]],"date-time":"2012-06-17T00:00:00Z","timestamp":1339891200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/www.springer.com\/tdm"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Nat Struct Mol Biol"],"published-print":{"date-parts":[[2012,7]]},"DOI":"10.1038\/nsmb.2330","type":"journal-article","created":{"date-parts":[[2012,6,17]],"date-time":"2012-06-17T21:14:34Z","timestamp":1339967674000},"page":"707-715","source":"Crossref","is-referenced-by-count":179,"title":["Structural basis for heteromeric assembly and perinuclear organization of keratin filaments"],"prefix":"10.1038","volume":"19","author":[{"given":"Chang-Hun","family":"Lee","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Min-Sung","family":"Kim","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Byung Min","family":"Chung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel J","family":"Leahy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pierre A","family":"Coulombe","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2012,6,17]]},"reference":[{"key":"BFnsmb2330_CR1","doi-asserted-by":"publisher","first-page":"249","DOI":"10.1038\/283249a0","volume":"283","author":"E Lazarides","year":"1980","unstructured":"Lazarides, E. Intermediate filaments as mechanical integrators of cellular space. Nature 283, 249\u2013256 (1980).","journal-title":"Nature"},{"key":"BFnsmb2330_CR2","doi-asserted-by":"publisher","first-page":"514","DOI":"10.1126\/science.279.5350.514","volume":"279","author":"E Fuchs","year":"1998","unstructured":"Fuchs, E. & Cleveland, D.W. A structural scaffolding of intermediate filaments in health and disease. Science 279, 514\u2013519 (1998).","journal-title":"Science"},{"key":"BFnsmb2330_CR3","first-page":"372","volume":"48","author":"M Osborn","year":"1983","unstructured":"Osborn, M. & Weber, K. Tumor diagnosis by intermediate filament typing: a novel tool for surgical pathology. Lab. Invest. 48, 372\u2013394 (1983).","journal-title":"Lab. Invest."},{"key":"BFnsmb2330_CR4","doi-asserted-by":"publisher","first-page":"2087","DOI":"10.1056\/NEJMra040319","volume":"351","author":"MB Omary","year":"2004","unstructured":"Omary, M.B., Coulombe, P.A. & McLean, W.H.I. Intermediate filament proteins and their associated diseases. N. Engl. J. Med. 351, 2087\u20132100 (2004).","journal-title":"N. Engl. J. Med."},{"key":"BFnsmb2330_CR5","doi-asserted-by":"publisher","first-page":"351","DOI":"10.1002\/humu.20652","volume":"29","author":"I Szeverenyi","year":"2008","unstructured":"Szeverenyi, I. et al. The Human Intermediate Filament Database: comprehensive information on a gene family involved in many human diseases. Hum. Mutat. 29, 351\u2013360 (2008).","journal-title":"Hum. Mutat."},{"key":"BFnsmb2330_CR6","doi-asserted-by":"publisher","first-page":"1581","DOI":"10.1101\/gad.1552107","volume":"21","author":"S Kim","year":"2007","unstructured":"Kim, S. & Coulombe, P.A. Intermediate filament scaffolds fulfill mechanical, organizational, and signaling functions in the cytoplasm. Genes Dev. 21, 1581\u20131597 (2007).","journal-title":"Genes Dev."},{"key":"BFnsmb2330_CR7","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1016\/0092-8674(83)90034-X","volume":"33","author":"I Hanukoglu","year":"1983","unstructured":"Hanukoglu, I. & Fuchs, E. The cDNA sequence of a Type II cytoskeletal keratin reveals constant and variable structural domains among keratins. Cell 33, 915\u2013924 (1983).","journal-title":"Cell"},{"key":"BFnsmb2330_CR8","doi-asserted-by":"publisher","first-page":"362","DOI":"10.1038\/nature04659","volume":"441","author":"S Kim","year":"2006","unstructured":"Kim, S., Wong, P. & Coulombe, P.A. A keratin cytoskeletal protein regulates protein synthesis and epithelial cell growth. Nature 441, 362\u2013365 (2006).","journal-title":"Nature"},{"key":"BFnsmb2330_CR9","doi-asserted-by":"publisher","first-page":"1199","DOI":"10.1083\/jcb.110.4.1199","volume":"110","author":"M Hatzfeld","year":"1990","unstructured":"Hatzfeld, M. & Weber, K. The coiled coil of in vitro assembled keratin filaments is a heterodimer of type I and II keratins: use of site-specific mutagenesis and recombinant protein expression. J. Cell Biol. 110, 1199\u20131210 (1990).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2330_CR10","doi-asserted-by":"publisher","first-page":"1255","DOI":"10.1093\/emboj\/21.6.1255","volume":"21","author":"SV Strelkov","year":"2002","unstructured":"Strelkov, S.V. et al. Conserved segments 1A and 2B of the intermediate filament dimer: their atomic structures and role in filament assembly. EMBO J. 21, 1255\u20131266 (2002).","journal-title":"EMBO J."},{"key":"BFnsmb2330_CR11","doi-asserted-by":"publisher","first-page":"436","DOI":"10.1006\/jmbi.1993.1161","volume":"230","author":"PM Steinert","year":"1993","unstructured":"Steinert, P.M., Marekov, L.N., Fraser, R.D. & Parry, D.A. Keratin intermediate filament structure. Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly. J. Mol. Biol. 230, 436\u2013452 (1993).","journal-title":"J. Mol. Biol."},{"key":"BFnsmb2330_CR12","doi-asserted-by":"publisher","first-page":"965","DOI":"10.1083\/jcb.200408116","volume":"168","author":"KM Bernot","year":"2005","unstructured":"Bernot, K.M., Lee, C.H. & Coulombe, P.A. A small surface hydrophobic stripe in the coiled-coil domain of type I keratins mediates tetramer stability. J. Cell Biol. 168, 965\u2013974 (2005).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2330_CR13","doi-asserted-by":"publisher","first-page":"17","DOI":"10.1016\/0014-4827(87)90328-4","volume":"173","author":"WW Franke","year":"1987","unstructured":"Franke, W.W. et al. Monoclonal cytokeratin antibody recognizing a heterotypic complex: immunological probing of conformational states of cytoskeletal proteins in filaments and in solution. Exp. Cell Res. 173, 17\u201337 (1987).","journal-title":"Exp. Cell Res."},{"key":"BFnsmb2330_CR14","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1007\/BF01349341","volume":"145","author":"U Aebi","year":"1988","unstructured":"Aebi, U., Haner, M., Troncoso, J., Eichner, R. & Engel, A. Unifying principles in intermediate filament assembly. Protoplasma 145, 73\u201381 (1988).","journal-title":"Protoplasma"},{"key":"BFnsmb2330_CR15","doi-asserted-by":"publisher","first-page":"16206","DOI":"10.1073\/pnas.0603629103","volume":"103","author":"AV Sokolova","year":"2006","unstructured":"Sokolova, A.V. et al. Monitoring intermediate filament assembly by small-angle x-ray scattering reveals the molecular architecture of assembly intermediates. Proc. Natl. Acad. Sci. USA 103, 16206\u201316211 (2006).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2330_CR16","doi-asserted-by":"publisher","first-page":"378","DOI":"10.1016\/j.jsb.2006.12.007","volume":"158","author":"KN Goldie","year":"2007","unstructured":"Goldie, K.N. et al. Dissecting the 3-D structure of vimentin intermediate filaments by cryo-electron tomography. J. Struct. Biol. 158, 378\u2013385 (2007).","journal-title":"J. Struct. Biol."},{"key":"BFnsmb2330_CR17","doi-asserted-by":"publisher","first-page":"773","DOI":"10.1006\/jmbi.2001.4442","volume":"306","author":"SV Strelkov","year":"2001","unstructured":"Strelkov, S.V. et al. Divide-and-conquer crystallographic approach towards an atomic structure of intermediate filaments. J. Mol. Biol. 306, 773\u2013781 (2001).","journal-title":"J. Mol. Biol."},{"key":"BFnsmb2330_CR18","doi-asserted-by":"publisher","first-page":"1067","DOI":"10.1016\/j.jmb.2004.08.093","volume":"343","author":"SV Strelkov","year":"2004","unstructured":"Strelkov, S.V., Schumacher, J., Burkhard, P., Aebi, U. & Herrmann, H. Crystal structure of the human lamin A coil 2B dimer: implications for the head-to-tail association of nuclear lamins. J. Mol. Biol. 343, 1067\u20131080 (2004).","journal-title":"J. Mol. Biol."},{"key":"BFnsmb2330_CR19","doi-asserted-by":"publisher","first-page":"811","DOI":"10.1016\/S0969-2126(02)00777-3","volume":"10","author":"I Krimm","year":"2002","unstructured":"Krimm, I. et al. The Ig-like structure of the C-terminal domain of lamin A\/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy. Structure 10, 811\u2013823 (2002).","journal-title":"Structure"},{"key":"BFnsmb2330_CR20","doi-asserted-by":"publisher","first-page":"17381","DOI":"10.1074\/jbc.C200038200","volume":"277","author":"S Dhe-Paganon","year":"2002","unstructured":"Dhe-Paganon, S., Werner, E.D., Chi, Y.I. & Shoelson, S.E. Structure of the globular tail of nuclear lamin. J. Biol. Chem. 277, 17381\u201317384 (2002).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2330_CR21","doi-asserted-by":"publisher","first-page":"245","DOI":"10.1016\/j.jmb.2009.04.067","volume":"390","author":"M Meier","year":"2009","unstructured":"Meier, M. et al. Vimentin coil 1A-A molecular switch involved in the initiation of filament elongation. J. Mol. Biol. 390, 245\u2013261 (2009).","journal-title":"J. Mol. Biol."},{"key":"BFnsmb2330_CR22","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1016\/j.jsb.2010.02.012","volume":"170","author":"S Nicolet","year":"2010","unstructured":"Nicolet, S., Herrmann, H., Aebi, U. & Strelkov, S.V. Atomic structure of vimentin coil 2. J. Struct. Biol. 170, 369\u2013376 (2010).","journal-title":"J. Struct. Biol."},{"key":"BFnsmb2330_CR23","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1146\/annurev.cb.11.110195.001011","volume":"11","author":"E Fuchs","year":"1995","unstructured":"Fuchs, E. Keratins and the skin. Annu. Rev. Cell Dev. Biol. 11, 123\u2013153 (1995).","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"BFnsmb2330_CR24","doi-asserted-by":"publisher","first-page":"11","DOI":"10.1016\/0092-8674(82)90400-7","volume":"31","author":"R Moll","year":"1982","unstructured":"Moll, R., Franke, W.W., Schiller, D.L., Geiger, B. & Krepler, R. The catalog of human cytokeratins: patterns of expression in normal epithelia, tumors and cultured cells. Cell 31, 11\u201324 (1982).","journal-title":"Cell"},{"key":"BFnsmb2330_CR25","doi-asserted-by":"publisher","first-page":"153","DOI":"10.1083\/jcb.111.1.153","volume":"111","author":"PA Coulombe","year":"1990","unstructured":"Coulombe, P.A. & Fuchs, E. Elucidating the early stages of keratin filament assembly. J. Cell Biol. 111, 153\u2013169 (1990).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2330_CR26","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1083\/jcb.200810196","volume":"186","author":"CH Lee","year":"2009","unstructured":"Lee, C.H. & Coulombe, P.A. Self-organization of keratin intermediate filaments into cross-linked networks. J. Cell Biol. 186, 409\u2013421 (2009).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2330_CR27","doi-asserted-by":"publisher","first-page":"1301","DOI":"10.1016\/0092-8674(91)90051-Y","volume":"66","author":"PA Coulombe","year":"1991","unstructured":"Coulombe, P.A. et al. Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: genetic and functional analyses. Cell 66, 1301\u20131311 (1991).","journal-title":"Cell"},{"key":"BFnsmb2330_CR28","doi-asserted-by":"publisher","first-page":"1784","DOI":"10.1172\/JCI38177","volume":"119","author":"PA Coulombe","year":"2009","unstructured":"Coulombe, P.A., Kerns, M.L. & Fuchs, E. Epidermolysis bullosa simplex: a paradigm for disorders of tissue fragility. J. Clin. Invest. 119, 1784\u20131793 (2009).","journal-title":"J. Clin. Invest."},{"key":"BFnsmb2330_CR29","doi-asserted-by":"publisher","first-page":"749","DOI":"10.1146\/annurev.biochem.73.011303.073823","volume":"73","author":"H Herrmann","year":"2004","unstructured":"Herrmann, H. & Aebi, U. Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular Scaffolds. Annu. Rev. Biochem. 73, 749\u2013789 (2004).","journal-title":"Annu. Rev. Biochem."},{"key":"BFnsmb2330_CR30","doi-asserted-by":"publisher","first-page":"258","DOI":"10.1016\/j.jsb.2008.01.016","volume":"163","author":"DA Parry","year":"2008","unstructured":"Parry, D.A., Fraser, R.D. & Squire, J.M. Fifty years of coiled-coils and alpha-helical bundles: a close relationship between sequence and structure. J. Struct. Biol. 163, 258\u2013269 (2008).","journal-title":"J. Struct. Biol."},{"key":"BFnsmb2330_CR31","doi-asserted-by":"publisher","first-page":"4","DOI":"10.1016\/j.bbaexp.2005.12.005","volume":"1759","author":"C Vinson","year":"2006","unstructured":"Vinson, C., Acharya, A. & Taparowsky, E.J. Deciphering B-ZIP transcription factor interactions in vitro and in vivo. Biochim. Biophys. Acta 1759, 4\u201312 (2006).","journal-title":"Biochim. Biophys. Acta"},{"key":"BFnsmb2330_CR32","doi-asserted-by":"publisher","first-page":"3539","DOI":"10.1091\/mbc.11.10.3539","volume":"11","author":"KC Wu","year":"2000","unstructured":"Wu, K.C. et al. Coiled-coil trigger motifs in the 1B and 2B rod domain segments are required for the stability of keratin intermediate filaments. Mol. Biol. Cell 11, 3539\u20133558 (2000).","journal-title":"Mol. Biol. Cell"},{"key":"BFnsmb2330_CR33","doi-asserted-by":"publisher","first-page":"23670","DOI":"10.1074\/jbc.M200974200","volume":"277","author":"K Yasukawa","year":"2002","unstructured":"Yasukawa, K., Sawamura, D., McMillan, J.R., Nakamura, H. & Shimizu, H. Dominant and recessive compound heterozygous mutations in epidermolysis bullosa simplex demonstrate the role of the stutter region in keratin intermediate filament assembly. J. Biol. Chem. 277, 23670\u201323674 (2002).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2330_CR34","doi-asserted-by":"publisher","first-page":"401","DOI":"10.1083\/jcb.119.2.401","volume":"119","author":"AK Wilson","year":"1992","unstructured":"Wilson, A.K., Coulombe, P.A. & Fuchs, E. The roles of K5 and K14 head, tail, and R\/K L L E G E domains in keratin filament assembly in vitro. J. Cell Biol. 119, 401\u2013414 (1992).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2330_CR35","doi-asserted-by":"publisher","first-page":"483","DOI":"10.1080\/10255842.2011.560147","volume":"14","author":"M Arslan","year":"2011","unstructured":"Arslan, M., Qin, Z. & Buehler, M.J. Coiled-coil intermediate filament stutter instability and molecular unfolding. Comput. Methods Biomech. Biomed. Engin. 14, 483\u2013489 (2011).","journal-title":"Comput. Methods Biomech. Biomed. Engin."},{"key":"BFnsmb2330_CR36","doi-asserted-by":"crossref","first-page":"2053","DOI":"10.1016\/S0021-9258(19)62353-7","volume":"253","author":"TT Sun","year":"1978","unstructured":"Sun, T.T. & Green, H. Keratin filaments of cultured human epidermal cells. Formation of intermolecular disulfide bonds during terminal differentiation. J. Biol. Chem. 253, 2053\u20132060 (1978).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2330_CR37","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1016\/0014-4827(83)90115-5","volume":"143","author":"H Hennings","year":"1983","unstructured":"Hennings, H. & Holbrook, K.A. Calcium regulation of cell-cell contact and differentiation of epidermal cells in culture. Exp. Cell Res. 143, 127\u2013142 (1983).","journal-title":"Exp. Cell Res."},{"key":"BFnsmb2330_CR38","doi-asserted-by":"publisher","first-page":"167","DOI":"10.1016\/j.ceb.2010.10.012","volume":"23","author":"MJ Feige","year":"2011","unstructured":"Feige, M.J. & Hendershot, L.M. Disulfide bonds in ER protein folding and homeostasis. Curr. Opin. Cell Biol. 23, 167\u2013175 (2011).","journal-title":"Curr. Opin. Cell Biol."},{"key":"BFnsmb2330_CR39","doi-asserted-by":"publisher","first-page":"7573","DOI":"10.1074\/jbc.M111.301549","volume":"287","author":"BM Chung","year":"2012","unstructured":"Chung, B.M., Murray, C.I., Van Eyk, J.E. & Coulombe, P.A. Identification of a novel interaction between Annexin A2 and Keratin 17: Evidence for reciprocal regulation. J. Biol. Chem. 287, 7573\u20137581 (2012).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2330_CR40","doi-asserted-by":"publisher","first-page":"882","DOI":"10.1038\/170882b0","volume":"170","author":"FH Crick","year":"1952","unstructured":"Crick, F.H. Is alpha-keratin a coiled coil? Nature 170, 882\u2013883 (1952).","journal-title":"Nature"},{"key":"BFnsmb2330_CR41","doi-asserted-by":"publisher","first-page":"539","DOI":"10.1126\/science.1948029","volume":"254","author":"EK O'Shea","year":"1991","unstructured":"O'Shea, E.K., Klemm, J.D., Kim, P.S. & Alber, T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254, 539\u2013544 (1991).","journal-title":"Science"},{"key":"BFnsmb2330_CR42","doi-asserted-by":"publisher","first-page":"1403","DOI":"10.1006\/jmbi.1999.2528","volume":"286","author":"H Herrmann","year":"1999","unstructured":"Herrmann, H., H\u00e4ner, M., Brettel, M., Ku, N.O. & Aebi, U. Characterization of distinct early assembly units of different intermediate filament proteins. J. Mol. Biol. 286, 1403\u20131420 (1999).","journal-title":"J. Mol. Biol."},{"key":"BFnsmb2330_CR43","doi-asserted-by":"publisher","first-page":"715","DOI":"10.1111\/j.0022-202X.2004.23213.x","volume":"123","author":"L Norlen","year":"2004","unstructured":"Norlen, L. & Al-Amoudi, A. Stratum corneum keratin structure, function, and formation: the cubic rod-packing and membrane templating model. J. Invest. Dermatol. 123, 715\u2013732 (2004).","journal-title":"J. Invest. Dermatol."},{"key":"BFnsmb2330_CR44","doi-asserted-by":"publisher","first-page":"570","DOI":"10.1007\/s004030000171","volume":"292","author":"Y Hashimoto","year":"2000","unstructured":"Hashimoto, Y. et al. Immunohistochemical localization of sulfhydryl oxidase correlates with disulfide crosslinking in the upper epidermis of rat skin. Arch. Dermatol. Res. 292, 570\u2013572 (2000).","journal-title":"Arch. Dermatol. Res."},{"key":"BFnsmb2330_CR45","doi-asserted-by":"crossref","first-page":"3179","DOI":"10.1242\/jcs.111.21.3179","volume":"111","author":"S Lyle","year":"1998","unstructured":"Lyle, S. et al. The C8\/144B monoclonal antibody recognizes cytokeratin 15 and defines the location of human hair follicle stem cells. J. Cell Sci. 111, 3179\u20133188 (1998).","journal-title":"J. Cell Sci."},{"key":"BFnsmb2330_CR46","doi-asserted-by":"publisher","first-page":"409","DOI":"10.1002\/(SICI)1097-4652(199909)180:3<409::AID-JCP12>3.0.CO;2-V","volume":"180","author":"TC Troy","year":"1999","unstructured":"Troy, T.C. & Turksen, K. In vitro characteristics of early epidermal progenitors isolated from keratin 14 (K14)-deficient mice: insights into the role of keratin 17 in mouse keratinocytes. J. Cell. Physiol. 180, 409\u2013421 (1999).","journal-title":"J. Cell. Physiol."},{"key":"BFnsmb2330_CR47","doi-asserted-by":"publisher","first-page":"865","DOI":"10.1242\/jcs.076356","volume":"124","author":"I Dupin","year":"2011","unstructured":"Dupin, I., Sakamoto, Y. & Etienne-Manneville, S. Cytoplasmic intermediate filaments mediate actin-driven positioning of the nucleus. J. Cell Sci. 124, 865\u2013872 (2011).","journal-title":"J. Cell Sci."},{"key":"BFnsmb2330_CR48","doi-asserted-by":"publisher","first-page":"47998","DOI":"10.1074\/jbc.M406021200","volume":"279","author":"F Arnesano","year":"2004","unstructured":"Arnesano, F. et al. The unusually stable quaternary structure of human Cu,Zn-superoxide dismutase 1 is controlled by both metal occupancy and disulfide status. J. Biol. Chem. 279, 47998\u201348003 (2004).","journal-title":"J. Biol. Chem."},{"key":"BFnsmb2330_CR49","doi-asserted-by":"publisher","first-page":"711","DOI":"10.1146\/annurev.bi.52.070183.003431","volume":"52","author":"A Meister","year":"1983","unstructured":"Meister, A. & Anderson, M.E. Glutathione. Annu. Rev. Biochem. 52, 711\u2013760 (1983).","journal-title":"Annu. Rev. Biochem."},{"key":"BFnsmb2330_CR50","doi-asserted-by":"publisher","first-page":"337","DOI":"10.1083\/jcb.200402120","volume":"166","author":"H Ostergaard","year":"2004","unstructured":"Ostergaard, H., Tachibana, C. & Winther, J.R. Monitoring disulfide bond formation in the eukaryotic cytosol. J. Cell Biol. 166, 337\u2013345 (2004).","journal-title":"J. Cell Biol."},{"key":"BFnsmb2330_CR51","doi-asserted-by":"crossref","unstructured":"Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. in Methods in Enzymology, Macromolecular Crystallography Part A Vol. 276 (eds., Carter, C.W. Jr. & Sweet, R.M.) 307\u2013326 (Academic Press, New York, 1997).","DOI":"10.1016\/S0076-6879(97)76066-X"},{"key":"BFnsmb2330_CR52","doi-asserted-by":"publisher","first-page":"22","DOI":"10.1016\/S0076-6879(03)74002-6","volume":"374","author":"TC Terwilliger","year":"2003","unstructured":"Terwilliger, T.C. SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374, 22\u201337 (2003).","journal-title":"Methods Enzymol."},{"key":"BFnsmb2330_CR53","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1107\/S0907444904019158","volume":"60","author":"P Emsley","year":"2004","unstructured":"Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126\u20132132 (2004).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"BFnsmb2330_CR54","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"PD Adams","year":"2010","unstructured":"Adams, P.D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213\u2013221 (2010).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"BFnsmb2330_CR55","doi-asserted-by":"publisher","first-page":"W375","DOI":"10.1093\/nar\/gkm216","volume":"35","author":"IW Davis","year":"2007","unstructured":"Davis, I.W. et al. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375\u2013W383 (2007).","journal-title":"Nucleic Acids Res."},{"key":"BFnsmb2330_CR56","doi-asserted-by":"publisher","first-page":"127","DOI":"10.1093\/protein\/8.2.127","volume":"8","author":"AC Wallace","year":"1995","unstructured":"Wallace, A.C., Laskowski, R.A. & Thornton, J.M. LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions. Protein Eng. 8, 127\u2013134 (1995).","journal-title":"Protein Eng."},{"key":"BFnsmb2330_CR57","doi-asserted-by":"crossref","unstructured":"Eswar, N. et al. Comparative Protein Structure Modeling with MODELLER. in Current Protocols in Bioinformatics (suppl. 15) 5.6.1\u20135.6.30 (John Wiley & Sons, Inc., 2006).","DOI":"10.1002\/0471250953.bi0506s15"},{"key":"BFnsmb2330_CR58","doi-asserted-by":"publisher","first-page":"10037","DOI":"10.1073\/pnas.181342398","volume":"98","author":"NA Baker","year":"2001","unstructured":"Baker, N.A., Sept, D., Joseph, S., Holst, M.J. & McCammon, J.A. Electrostatics of nanosystems: application to microtubules and the ribosome. Proc. Natl. Acad. Sci. USA 98, 10037\u201310041 (2001).","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"BFnsmb2330_CR59","doi-asserted-by":"crossref","first-page":"727","DOI":"10.1242\/jcs.104.3.727","volume":"104","author":"YY Pang","year":"1993","unstructured":"Pang, Y.Y., Schermer, A., Yu, J. & Sun, T.T. Suprabasal change and subsequent formation of disulfide-stabilized homo- and hetero-dimers of keratins during esophageal epithelial differentiation. J. Cell Sci. 104, 727\u2013740 (1993).","journal-title":"J. Cell Sci."},{"key":"BFnsmb2330_CR60","doi-asserted-by":"publisher","first-page":"1329","DOI":"10.1083\/jcb.129.5.1329","volume":"129","author":"C Lloyd","year":"1995","unstructured":"Lloyd, C. et al. The basal keratin network of stratified squamous epithelia: defining K15 function in the absence of K14. J. Cell Biol. 129, 1329\u20131344 (1995).","journal-title":"J. Cell Biol."}],"container-title":["Nature Structural &amp; Molecular Biology"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2330.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2330","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/nsmb.2330.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,5,19]],"date-time":"2023-05-19T04:32:01Z","timestamp":1684470721000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/nsmb.2330"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2012,6,17]]},"references-count":60,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2012,7]]}},"alternative-id":["BFnsmb2330"],"URL":"https:\/\/doi.org\/10.1038\/nsmb.2330","relation":{},"ISSN":["1545-9993","1545-9985"],"issn-type":[{"value":"1545-9993","type":"print"},{"value":"1545-9985","type":"electronic"}],"subject":[],"published":{"date-parts":[[2012,6,17]]}}}