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A."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0365","doi-asserted-by":"crossref","first-page":"9056","DOI":"10.1073\/pnas.161280798","article-title":"The Calpha\u2013H\u22efO hydrogen bond: a determinant of stability and specificity in transmembrane helix interactions","volume":"98","author":"Senes","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0370","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1021\/bi901660t","article-title":"A single glutamate residue controls the oligomerization, function, and stability of the aquaglyceroporin GlpF","volume":"49","author":"Cymer","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0375","doi-asserted-by":"crossref","first-page":"10223","DOI":"10.1021\/bi201266m","article-title":"The tetrameric alpha-helical membrane protein GlpF unfolds via a dimeric folding intermediate","volume":"50","author":"Veerappan","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0380","doi-asserted-by":"crossref","first-page":"e14674","DOI":"10.1371\/journal.pone.0014674","article-title":"Structure and stability of the spinach aquaporin SoPIP2;1 in detergent micelles and lipid membranes","volume":"6","author":"Plasencia","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0385","doi-asserted-by":"crossref","first-page":"2600","DOI":"10.1016\/j.bbamem.2011.05.021","article-title":"Interaction between sodium dodecyl sulfate and membrane reconstituted aquaporins: a comparative study of spinach SoPIP2;1 and E. coli AqpZ","volume":"1808","author":"Hansen","year":"2011","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0390","doi-asserted-by":"crossref","first-page":"11896","DOI":"10.1073\/pnas.1105112108","article-title":"Mechanism of activation gating in the full-length KcsA K+ channel","volume":"108","author":"Uysal","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0395","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1126\/science.280.5360.69","article-title":"The structure of the potassium channel: molecular basis of K+ conduction and selectivity","volume":"280","author":"Doyle","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0400","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1038\/nature01748","article-title":"Structure and gating mechanism of the acetylcholine receptor pore","volume":"423","author":"Miyazawa","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0405","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/j.jmb.2004.12.031","article-title":"Refined structure of the nicotinic acetylcholine receptor at 4A resolution","volume":"346","author":"Unwin","year":"2005","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0410","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2014.07.017","article-title":"Folding energetics and oligomerization of polytopic alpha-helical transmembrane proteins","author":"Neumann","year":"2014","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0415","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1515\/hsz-2012-0231","article-title":"Oligomerization of polytopic alpha-helical membrane proteins: causes and consequences","volume":"393","author":"Cymer","year":"2012","journal-title":"Biol. Chem."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0420","doi-asserted-by":"crossref","first-page":"5013","DOI":"10.1016\/j.bmc.2005.05.037","article-title":"Protein oligomerization: how and why","volume":"13","author":"Ali","year":"2005","journal-title":"Bioorg. Med. 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Rev."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0435","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1038\/nature02027","article-title":"The tobacco aquaporin NtAQP1 is a membrane CO2 pore with physiological functions","volume":"425","author":"Uehlein","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0440","doi-asserted-by":"crossref","first-page":"5884","DOI":"10.1021\/bi963095j","article-title":"A method for assessing the stability of a membrane protein","volume":"36","author":"Lau","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0445","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1016\/S0022-2836(03)00624-7","article-title":"Folding of DsbB in mixed micelles: a kinetic analysis of the stability of a bacterial membrane protein","volume":"330","author":"Otzen","year":"2003","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0450","doi-asserted-by":"crossref","first-page":"18970","DOI":"10.1073\/pnas.0705067104","article-title":"Combined kinetic and thermodynamic analysis of alpha-helical membrane protein unfolding","volume":"104","author":"Curnow","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0455","doi-asserted-by":"crossref","first-page":"2123","DOI":"10.1021\/bi700778c","article-title":"Protein self-assembly and lipid binding in the folding of the potassium channel KcsA","volume":"47","author":"Barrera","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0460","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1038\/nrd4226","article-title":"Aquaporins: important but elusive drug targets","volume":"13","author":"Verkman","year":"2014","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0465","doi-asserted-by":"crossref","first-page":"330","DOI":"10.1016\/j.ajhg.2013.06.008","article-title":"Mutations in AQP5, encoding a water-channel protein, cause autosomal-dominant diffuse nonepidermolytic palmoplantar keratoderma","volume":"93","author":"Blaydon","year":"2013","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0470","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1146\/annurev.biophys.33.110502.140348","article-title":"Disease-related misassembly of membrane proteins","volume":"33","author":"Sanders","year":"2004","journal-title":"Annu. Rev. Biophys. Biomol. Struct."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0475","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1016\/j.bbamem.2011.07.046","article-title":"Membrane protein misassembly in disease","volume":"1818","author":"Ng","year":"2012","journal-title":"Biochim. Biophys. 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Pathol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0520","doi-asserted-by":"crossref","first-page":"990","DOI":"10.1681\/ASN.2008060648","article-title":"LIP5 interacts with aquaporin 2 and facilitates its lysosomal degradation","volume":"20","author":"van Balkom","year":"2009","journal-title":"J. Am. Soc. Nephrol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0525","doi-asserted-by":"crossref","first-page":"G1106","DOI":"10.1152\/ajpgi.00194.2010","article-title":"Roles of lysosomal proteolytic systems in AQP5 degradation in the submandibular gland of rats following chorda tympani parasympathetic denervation","volume":"299","author":"Azlina","year":"2010","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0530","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.neulet.2014.02.054","article-title":"Upregulation and lysosomal degradation of AQP4 in rat brains with bacterial meningitis","volume":"566","author":"Huang","year":"2014","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0535","doi-asserted-by":"crossref","first-page":"e45976","DOI":"10.1371\/journal.pone.0045976","article-title":"Aquaporin-1 translocation and degradation mediates the water transportation mechanism of acetazolamide","volume":"7","author":"Zhang","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0540","doi-asserted-by":"crossref","first-page":"1","DOI":"10.5049\/EBP.2009.7.1.1","article-title":"Ubiquitination of aquaporin-2 in the kidney","volume":"7","author":"Lee","year":"2009","journal-title":"Electrolyte Blood Press."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0545","first-page":"1770","article-title":"Changes in ocular aquaporin-4 (AQP4) expression following retinal injury","volume":"14","author":"Dibas","year":"2008","journal-title":"Mol. Vis."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0550","doi-asserted-by":"crossref","first-page":"18344","DOI":"10.1073\/pnas.0604073103","article-title":"Short-chain ubiquitination mediates the regulated endocytosis of the aquaporin-2 water channel","volume":"103","author":"Kamsteeg","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0555","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/978-3-540-79885-9_6","article-title":"Regulation of aquaporin-2 trafficking","author":"Nedvetsky","year":"2009","journal-title":"Handb. Exp. Pharmacol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0560","doi-asserted-by":"crossref","first-page":"963","DOI":"10.1016\/j.bbamem.2011.07.035","article-title":"Transmembrane helix\u2013helix interactions are modulated by the sequence context and by lipid bilayer properties","volume":"1818","author":"Cymer","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0565","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1016\/j.bbamem.2011.08.031","article-title":"Transmembrane helix dimerization: beyond the search for sequence motifs","volume":"1818","author":"Li","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0570","doi-asserted-by":"crossref","first-page":"14045","DOI":"10.1073\/pnas.0405274101","article-title":"The channel architecture of aquaporin 0 at a 2.2-A resolution","volume":"101","author":"Harries","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0575","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/0014-4835(76)90135-4","article-title":"Lens membranes II. Isolation and characterization of the main intrinsic polypeptide (MIP) of bovine lens fiber membranes","volume":"23","author":"Broekhuyse","year":"1976","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0580","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1083\/jcb.92.1.213","article-title":"Immunocytochemical localization of the lens main intrinsic polypeptide (MIP26) in communicating junctions","volume":"92","author":"Bok","year":"1982","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0585","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1083\/jcb.93.1.175","article-title":"On the structural organization of isolated bovine lens fiber junctions","volume":"93","author":"Zampighi","year":"1982","journal-title":"J. Cell Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0590","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1038\/nature02503","article-title":"Aquaporin-0 membrane junctions reveal the structure of a closed water pore","volume":"429","author":"Gonen","year":"2004","journal-title":"Nature"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0595","doi-asserted-by":"crossref","first-page":"1026","DOI":"10.1038\/nature06387","article-title":"Molecular code for transmembrane-helix recognition by the Sec61 translocon","volume":"450","author":"Hessa","year":"2007","journal-title":"Nature"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0600","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/S0959-440X(03)00102-7","article-title":"Sequence motifs, polar interactions and conformational changes in helical membrane proteins","volume":"13","author":"Curran","year":"2003","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0605","doi-asserted-by":"crossref","first-page":"1221","DOI":"10.1016\/j.jmb.2006.02.065","article-title":"The stability of transmembrane helix interactions measured in a biological membrane","volume":"358","author":"Finger","year":"2006","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0610","doi-asserted-by":"crossref","first-page":"911","DOI":"10.1006\/jmbi.1999.3489","article-title":"The GxxxG motif: a framework for transmembrane helix\u2013helix association","volume":"296","author":"Russ","year":"2000","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0615","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/j.sbi.2004.07.007","article-title":"Folding of helical membrane proteins: the role of polar, GxxxG-like and proline motifs","volume":"14","author":"Senes","year":"2004","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0620","doi-asserted-by":"crossref","first-page":"2250","DOI":"10.1073\/pnas.041593698","article-title":"Polar residues drive association of polyleucine transmembrane helices","volume":"98","author":"Zhou","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0625","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1073\/pnas.98.3.880","article-title":"Polar side chains drive the association of model transmembrane peptides","volume":"98","author":"Gratkowski","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0630","doi-asserted-by":"crossref","first-page":"1814","DOI":"10.1046\/j.1432-1033.2002.02821.x","article-title":"Human aquaporin adipose (AQPap) gene, genomic structure, promoter analysis and functional mutation","volume":"269","author":"Kondo","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0635","doi-asserted-by":"crossref","first-page":"227","DOI":"10.1016\/S0378-1119(96)00730-5","article-title":"Analysis of an expression profile of genes in the human adipose tissue","volume":"190","author":"Maeda","year":"1997","journal-title":"Gene"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0640","doi-asserted-by":"crossref","first-page":"20782","DOI":"10.1074\/jbc.272.33.20782","article-title":"Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea","volume":"272","author":"Ishibashi","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0645","doi-asserted-by":"crossref","first-page":"1004","DOI":"10.1016\/j.bbamem.2006.01.008","article-title":"Aquaporins and glycerol metabolism","volume":"1758","author":"Hibuse","year":"2006","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0650","doi-asserted-by":"crossref","first-page":"1945","DOI":"10.1529\/biophysj.107.110395","article-title":"Hydrogen-bonding and packing features of membrane proteins: functional implications","volume":"94","author":"Hildebrand","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0655","doi-asserted-by":"crossref","first-page":"1607","DOI":"10.1021\/bi048065s","article-title":"The contribution of C alpha-H\u22efO hydrogen bonds to membrane protein stability depends on the position of the amide","volume":"44","author":"Mottamal","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0660","doi-asserted-by":"crossref","first-page":"e82154","DOI":"10.1371\/journal.pone.0082154","article-title":"A novel null homozygous mutation confirms CACNA2D2 as a gene mutated in epileptic encephalopathy","volume":"8","author":"Pippucci","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0665","doi-asserted-by":"crossref","first-page":"1108","DOI":"10.1002\/humu.20762","article-title":"Genetic variation in human aquaporins and effects on phenotypes of water homeostasis","volume":"29","author":"Sorani","year":"2008","journal-title":"Hum. Mutat."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0670","doi-asserted-by":"crossref","first-page":"5990","DOI":"10.1021\/bi0200763","article-title":"GXXXG and AXXXA: common alpha-helical interaction motifs in proteins, particularly in extremophiles","volume":"41","author":"Kleiger","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0675","doi-asserted-by":"crossref","first-page":"4075","DOI":"10.1529\/biophysj.104.049288","article-title":"Helical packing patterns in membrane and soluble proteins","volume":"87","author":"Gimpelev","year":"2004","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0680","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1186\/1472-6807-7-27","article-title":"Homology modeling of major intrinsic proteins in rice, maize and Arabidopsis: comparative analysis of transmembrane helix association and aromatic\/arginine selectivity filters","volume":"7","author":"Bansal","year":"2007","journal-title":"BMC Struct. Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0685","doi-asserted-by":"crossref","first-page":"799","DOI":"10.1006\/jmbi.2001.5353","article-title":"Motifs of serine and threonine can drive association of transmembrane helices","volume":"316","author":"Dawson","year":"2002","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0690","doi-asserted-by":"crossref","first-page":"2103","DOI":"10.1016\/j.bbamem.2012.04.003","article-title":"A Ser residue influences the structure and stability of a Pro-kinked transmembrane helix dimer","volume":"1818","author":"Weber","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.bbamem.2014.11.015_bb0695","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/S0006-3495(04)74088-6","article-title":"Ser and Thr residues modulate the conformation of pro-kinked transmembrane alpha-helices","volume":"86","author":"Deupi","year":"2004","journal-title":"Biophys. J."},{"key":"10.1016\/j.bbamem.2014.11.015_bb0700","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1074\/jbc.M603761200","article-title":"Specific aquaporins facilitate the diffusion of hydrogen peroxide across membranes","volume":"282","author":"Bienert","year":"2007","journal-title":"J. Biol. 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