{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,29]],"date-time":"2026-04-29T01:38:38Z","timestamp":1777426718358,"version":"3.51.4"},"reference-count":43,"publisher":"Elsevier BV","issue":"10","license":[{"start":{"date-parts":[[2006,11,1]],"date-time":"2006-11-01T00:00:00Z","timestamp":1162339200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2006,11,1]],"date-time":"2006-11-01T00:00:00Z","timestamp":1162339200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2013,7,16]],"date-time":"2013-07-16T00:00:00Z","timestamp":1373932800000},"content-version":"vor","delay-in-days":2449,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/100000190","name":"U.S. Department of Commerce","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000190","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000161","name":"National Institute of Standards and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000161","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["cell.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biophysical Journal"],"published-print":{"date-parts":[[2006,11]]},"DOI":"10.1529\/biophysj.106.092247","type":"journal-article","created":{"date-parts":[[2006,9,1]],"date-time":"2006-09-01T20:38:08Z","timestamp":1157143088000},"page":"3736-3747","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":31,"title":["Neutron Diffraction Studies of Fluid Bilayers with Transmembrane Proteins: Structural Consequences of the Achondroplasia Mutation"],"prefix":"10.1016","volume":"91","author":[{"given":"Xue","family":"Han","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mihaela","family":"Mihailescu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kalina","family":"Hristova","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1529\/biophysj.106.092247_bib1","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1146\/annurev.biophys.28.1.319","article-title":"Membrane protein folding and stability: physical principles","volume":"28","author":"White","year":"1999","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1529\/biophysj.106.092247_bib2","first-page":"91","article-title":"Protein folding in membranes: pondering the nature of the bilayer milieu","volume":"49","author":"White","year":"1998","journal-title":"Biol. Skr. Dan. Selsk."},{"key":"10.1529\/biophysj.106.092247_bib3","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1006\/jmbi.2001.5008","article-title":"Energetics, stability, and prediction of transmembrane helices","volume":"312","author":"Jayasinghe","year":"2001","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.106.092247_bib4","doi-asserted-by":"crossref","first-page":"1427","DOI":"10.1126\/science.1109176","article-title":"Membrane insertion of a potassium-channel voltage sensor","volume":"307","author":"Hessa","year":"2005","journal-title":"Science"},{"key":"10.1529\/biophysj.106.092247_bib5","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1038\/nature03216","article-title":"Recognition of transmembrane helices by the endoplasmic reticulum translocon","volume":"433","author":"Hessa","year":"2005","journal-title":"Nature"},{"key":"10.1529\/biophysj.106.092247_bib6","doi-asserted-by":"crossref","first-page":"10826","DOI":"10.1021\/bi00091a038","article-title":"Extension of the parallax analysis of membrane penetration depth to the polar region of model membranes: use of fluorescence quenching by a spin-label attached to the phospholipid polar headgroup","volume":"32","author":"Abrams","year":"1993","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.106.092247_bib7","doi-asserted-by":"crossref","first-page":"15475","DOI":"10.1021\/bi00047a012","article-title":"Anchoring of tryptophan and tyrosine analogs at the hydrocarbon-polar boundary in model membrane vesicles: parallax analysis of fluorescence quenching induced by nitroxide-labeled phospholipids","volume":"34","author":"Kachel","year":"1995","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.106.092247_bib8","series-title":"Peptide-Lipid Interactions","article-title":"Measuring the depth of membrane penetration by amino acid residues in peptides using fluorescence quenching","author":"London","year":"2001"},{"key":"10.1529\/biophysj.106.092247_bib9","doi-asserted-by":"crossref","first-page":"1139","DOI":"10.1006\/jmbi.1997.0931","article-title":"The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR","volume":"267","author":"Macosko","year":"1997","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.106.092247_bib10","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1016\/S0959-440X(94)90219-4","article-title":"Investigation of structure and dynamics in membrane proteins using site-directed spin labeling","volume":"4","author":"Hubbell","year":"1994","journal-title":"Curr. Opinion Struct. Biol."},{"key":"10.1529\/biophysj.106.092247_bib11","doi-asserted-by":"crossref","first-page":"8626","DOI":"10.1073\/pnas.88.19.8626","article-title":"Locations of Arg-82, Asp-85, and Asp-96 in helix C of bacteriorhodopsin relative to the aqueous boundaries","volume":"88","author":"Greenhalgh","year":"1991","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1529\/biophysj.106.092247_bib12","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1016\/S0006-3495(89)82765-1","article-title":"Conformation of spin-labeled melittin at membrane surfaces investigated by pulse saturation recovery and continuous wave power saturation electron paramagnetic resonance","volume":"56","author":"Altenbach","year":"1989","journal-title":"Biophys. J"},{"key":"10.1529\/biophysj.106.092247_bib13","doi-asserted-by":"crossref","first-page":"6581","DOI":"10.1021\/bi000224u","article-title":"Oblique membrane insertion of viral fusion peptide probed by neutron diffraction","volume":"39","author":"Bradshaw","year":"2000","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.106.092247_bib14","doi-asserted-by":"crossref","first-page":"2610","DOI":"10.1016\/S0006-3495(02)75271-5","article-title":"\u03b2-amyloid 25 to 35 is intercalated in anionic and zwitterionic lipid membranes to different extents","volume":"83","author":"Dante","year":"2002","journal-title":"Biophys. J"},{"key":"10.1529\/biophysj.106.092247_bib15","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.bbabio.2005.08.007","article-title":"Localization of coenzyme Q(10) in the center of a deuterated lipid membrane by neutron diffraction","volume":"1710","author":"Hauss","year":"2005","journal-title":"Biochim. Biophys. Acta Bioenerg."},{"key":"10.1529\/biophysj.106.092247_bib16","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1016\/S0921-4526(99)01821-9","article-title":"Neutron diffraction studies of viral fusion peptides","volume":"276","author":"Bradshaw","year":"2000","journal-title":"Physica B (Amsterdam)"},{"key":"10.1529\/biophysj.106.092247_bib17","doi-asserted-by":"crossref","first-page":"6997","DOI":"10.1021\/bi00242a027","article-title":"Transbilayer distribution of bromine in fluid bilayers containing a specifically brominated analog of dioleoylphosphatidylcholine","volume":"30","author":"Wiener","year":"1991","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.106.092247_bib18","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1021\/bi048480k","article-title":"SDS-PAGE and FRET suggest weak interactions between FGFR3 TM domains in the absence of extracellular domains and ligands","volume":"44","author":"Li","year":"2005","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.106.092247_bib19","doi-asserted-by":"crossref","first-page":"520","DOI":"10.1002\/j.1460-2075.1996.tb00384.x","article-title":"Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia","volume":"15","author":"Webster","year":"1996","journal-title":"EMBO J"},{"key":"10.1529\/biophysj.106.092247_bib20","doi-asserted-by":"crossref","first-page":"600","DOI":"10.1016\/j.jmb.2005.11.077","article-title":"FGFR3 dimer stabilization due to a single amino acid pathogenic mutation","volume":"356","author":"Li","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.106.092247_bib21","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jmb.2006.01.086","article-title":"Transmembrane helix heterodimerization in lipids bilayers: probing the energetics behind autosomal dominant growth disorders","volume":"358","author":"Merzlyakov","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.106.092247_bib22","doi-asserted-by":"crossref","first-page":"5551","DOI":"10.1021\/bi060113g","article-title":"The achondroplasia mutation does not alter the dimerization energetics of FGFR3 transmembrane domain","volume":"45","author":"You","year":"2006","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.106.092247_bib23","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1038\/sj.ejhg.5200883","article-title":"Novel fibroblast growth factor receptor 3 (FGFR3) mutations in bladder cancer previously identified in non-lethal skeletal disorders","volume":"10","author":"van Rhijin","year":"2002","journal-title":"Eur. J. Hum. Genet."},{"key":"10.1529\/biophysj.106.092247_bib24","first-page":"23","article-title":"The molecular and genetic basis of fibroblast growth factor receptor 3 disorders: the achondroplasia family of skeletal dysplasias, Muenke craniosynostosis, and Crouzon syndrome with","volume":"21","author":"Vajo","year":"2000","journal-title":"Acanthosis nigricans. Endocr. Rev."},{"key":"10.1529\/biophysj.106.092247_bib25","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1016\/0092-8674(94)90302-6","article-title":"Mutations in the transmembrane domain of FGFR3 cause the most common genetic form of dwarfism, achondroplasia","volume":"78","author":"Shiang","year":"1994","journal-title":"Cell"},{"key":"10.1529\/biophysj.106.092247_bib26","doi-asserted-by":"crossref","first-page":"230","DOI":"10.1038\/339230a0","article-title":"A point mutation in the Neu oncogene mimics ligand induction of receptor aggregation","volume":"339","author":"Weiner","year":"1989","journal-title":"Nature"},{"key":"10.1529\/biophysj.106.092247_bib27","doi-asserted-by":"crossref","first-page":"6241","DOI":"10.1021\/bi060609y","article-title":"Role of receptor tyrosine kinase transmembrane domains in cell signaling and human pathologies","volume":"45","author":"Li","year":"2006","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.106.092247_bib28","doi-asserted-by":"crossref","first-page":"609","DOI":"10.1073\/pnas.2237184100","article-title":"Defective lysosomal targeting of activated fibroblast growth factor receptor 3 in achondroplasia","volume":"101","author":"Cho","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1529\/biophysj.106.092247_bib29","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1128\/MCB.20.2.516-522.2000","article-title":"The transmembrane mutation G380R in fibroblast growth factor receptor 3 uncouples ligand-mediated receptor activation from down-regulation","volume":"20","author":"Monsonego-Ornan","year":"2000","journal-title":"Mol. Cell. Biol."},{"key":"10.1529\/biophysj.106.092247_bib30","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1016\/S0014-5793(02)03255-6","article-title":"FGF receptors ubiquitylation: dependence on tyrosine kinase activity and role in downregulation","volume":"528","author":"Monsonego-Ornan","year":"2002","journal-title":"FEBS Lett."},{"key":"10.1529\/biophysj.106.092247_bib31","doi-asserted-by":"crossref","first-page":"568","DOI":"10.1016\/S0006-3495(91)82086-0","article-title":"Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. I. Scaling of neutron data and the distribution of double-bonds and water","volume":"60","author":"Wiener","year":"1991","journal-title":"Biophys. J"},{"key":"10.1529\/biophysj.106.092247_bib32","doi-asserted-by":"crossref","first-page":"2419","DOI":"10.1016\/S0006-3495(98)77950-0","article-title":"Determination of the hydrocarbon core structure of fluid dioleoylphosphatidylcholine (DOPC) bilayers by x-ray diffraction using specific bromination of the double-bonds: effect of hydration","volume":"74","author":"Hristova","year":"1998","journal-title":"Biophys. J"},{"key":"10.1529\/biophysj.106.092247_bib33","doi-asserted-by":"crossref","first-page":"3421","DOI":"10.1021\/bi00434a042","article-title":"The nature of the hydrophobic binding of small peptides at the bilayer interface: implications for the insertion of transbilayer helices","volume":"28","author":"Jacobs","year":"1989","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.106.092247_bib34","doi-asserted-by":"crossref","first-page":"434","DOI":"10.1016\/S0006-3495(92)81849-0","article-title":"Structure of a fluid dioleoylphosphatidylcholine bilayer determined by joint refinement of x-ray and neutron diffraction data. III. Complete structure","volume":"61","author":"Wiener","year":"1992","journal-title":"Biophys. J"},{"key":"10.1529\/biophysj.106.092247_bib35","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1006\/jmbi.1999.2840","article-title":"An amphipathic \u03b1-helix at a membrane interface: a structural study using a novel x-ray diffraction method","volume":"290","author":"Hristova","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1529\/biophysj.106.092247_bib36","doi-asserted-by":"crossref","first-page":"801","DOI":"10.1016\/S0006-3495(01)76059-6","article-title":"Structure, location, and lipid perturbations of melittin at the membrane interface","volume":"80","author":"Hristova","year":"2001","journal-title":"Biophys. J"},{"key":"10.1529\/biophysj.106.092247_bib37","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.bbamem.2004.12.012","article-title":"Synthesis and initial characterization of FGFR3 transmembrane domain: consequences of sequence modifications","volume":"1668","author":"Iwamoto","year":"2005","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1529\/biophysj.106.092247_bib38","doi-asserted-by":"crossref","first-page":"9053","DOI":"10.1021\/la048676l","article-title":"Imaging FRET measurements of transmembrane helix interactions in lipid bilayers on a solid support","volume":"20","author":"Li","year":"2004","journal-title":"Langmuir"},{"key":"10.1529\/biophysj.106.092247_bib39","doi-asserted-by":"crossref","first-page":"154","DOI":"10.1016\/j.ab.2005.01.035","article-title":"FRET in liposomes: measurements of TM helix dimerization in the native bilayer environment","volume":"340","author":"You","year":"2005","journal-title":"Anal. Biochem."},{"key":"10.1529\/biophysj.106.092247_bib40","doi-asserted-by":"crossref","first-page":"4562","DOI":"10.1021\/bi00388a060","article-title":"Comparison of the conformation and orientation of alamethicin and melittin in lipid membranes","volume":"26","author":"Vogel","year":"1987","journal-title":"Biochemistry"},{"key":"10.1529\/biophysj.106.092247_bib41","doi-asserted-by":"crossref","first-page":"2531","DOI":"10.1063\/1.455047","article-title":"Circular dichroism of oriented \u03b1-helices. I. Proof of the exciton theory","volume":"89","author":"Olah","year":"1988","journal-title":"J. Chem. Phys."},{"key":"10.1529\/biophysj.106.092247_bib42","doi-asserted-by":"crossref","first-page":"6956","DOI":"10.1063\/1.455321","article-title":"Circular dichroism of oriented \u03b1-helices. II. Electric field oriented polypeptides","volume":"89","author":"Olah","year":"1988","journal-title":"J. Chem. Phys."},{"key":"10.1529\/biophysj.106.092247_bib43","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1016\/S0022-2836(76)80068-X","article-title":"Structural analysis of hydrated egg lecithin and cholesterol bilayers. II. Neutron diffraction","volume":"100","author":"Worcester","year":"1976","journal-title":"J. Mol. Biol."}],"container-title":["Biophysical Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349506720859?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0006349506720859?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,7,29]],"date-time":"2025-07-29T12:15:55Z","timestamp":1753791355000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0006349506720859"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,11]]},"references-count":43,"journal-issue":{"issue":"10","published-print":{"date-parts":[[2006,11]]}},"alternative-id":["S0006349506720859"],"URL":"https:\/\/doi.org\/10.1529\/biophysj.106.092247","relation":{},"ISSN":["0006-3495"],"issn-type":[{"value":"0006-3495","type":"print"}],"subject":[],"published":{"date-parts":[[2006,11]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Neutron Diffraction Studies of Fluid Bilayers with Transmembrane Proteins: Structural Consequences of the Achondroplasia Mutation","name":"articletitle","label":"Article Title"},{"value":"Biophysical Journal","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1529\/biophysj.106.092247","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2006 The Biophysical Society. Published by Elsevier Inc. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}]}}