Cysteine Modification 47
Dodier Y, Banderali U, Klein H, Topalak O, Dafi O, Simoes M, Bernatchez G, Sauve R, Parent L
(2004) Outer pore topology of the ECaC-TRPV5 channel by cysteine scan mutagenesis. J Biol
Chem 279(8):6853–6862. doi:10.1074/jbc.M310534200
Falke JJ, Koshland DE Jr (1987) Global flexibility in a sensory receptor: a site-directed cross-
linking approach. Science 237(4822):1596–1600
Falke JJ, Dernburg AF, Sternberg DA, Zalkin N, Milligan DL, Koshland DE Jr (1988) Structure
of a bacterial sensory receptor. A site-directed sulfhydryl study. J Biol Chem 263(29):14850–
14858
Fass D (2012) Disulfide bonding in protein biophysics. Annu Rev Biophys 41:63–79. doi:10.1146/
annurev-biophys-050511-102321
Feige MJ, Hendershot LM (2011) Disulfide bonds in ER protein folding and homeostasis. Curr
Opin Cell Biol 23(2):167–175. doi:10.1016/j.ceb.2010.10.012
ffrench-Constant RH, Rocheleau TA, Steichen JC, Chalmers AE (1993a) A point mutation in
a Drosophila GABA receptor confers insecticide resistance. Nature 363(6428):449–451.
doi:10.1038/363449a0
ffrench-Constant RH, Steichen JC, Rocheleau TA, Aronstein K, Roush RT (1993b) A single-
amino acid substitution in a gamma-aminobutyric acid subtype A receptor locus is associated
with cyclodiene insecticide resistance in Drosophila populations. Proc Natl Acad Sci U S A
90(5):1957–1961
Filippova N, Wotring VE, Weiss DS (2004) Evidence that the TM1-TM2 loop contributes to the
rho1 GABA receptor pore. J Biol Chem 279(20):20906–20914. doi:10.1074/jbc.M401012200
M401012200 [pii]
Finkelstein A (1994) The channel formed in planar lipid bilayers by the protective antigen compo-
nent of anthrax toxin. Toxicology 87(1–3):29–41
Finkelstein A (2009) Proton-coupled protein transport through the anthrax toxin channel. Philos
Trans R Soc Lond B Biol Sci 364(1514):209–215. doi:10.1098/rstb.2008.0126
Finkelstein A, Oh KJ, Senzel L, Gordon M, Blaustein RO, Collier RJ (2000) The diphtheria toxin
channel-forming T-domain translocates its own NH2-terminal region and the catalytic domain
across planar phospholipid bilayers. Int J Med Microbiol 290(4–5):435–440. doi:10.1016/
s1438-4221(00)80059-4
Fraser JS, van den Bedem H, Samelson AJ, Lang PT, Holton JM, Echols N, Alber T (2011) Access-
ing protein conformational ensembles using room-temperature X-ray crystallography. Proc
Natl Acad Sci U S A 108(39):16247–16252. doi:10.1073/pnas.1111325108
Furukawa H, Singh SK, Mancusso R, Gouaux E (2005) Subunit arrangement and function in
NMDA receptors. Nature 438(7065):185–192. doi:10.1038/nature04089
Gajewski C, Dagcan A, Roux B, Deutsch C (2011) Biogenesis of the pore architecture of a volt-
age-gated potassium channel. Proc Natl Acad Sci U S A 108(8):3240–3245. doi:10.1073/
pnas.1017097108
Galzi JL, Revah F, Black D, Goeldner M, Hirth C, Changeux JP (1990) Identification of a novel
amino acid alpha-tyrosine 93 within the cholinergic ligands-binding sites of the acetylcholine
receptor by photoaffinity labeling. Additional evidence for a three-loop model of the choliner-
gic ligands-binding sites. J Biol Chem 265(18):10430–10437
Galzi JL, Devillers-Thiery A, Hussy N, Bertrand S, Changeux JP, Bertrand D (1992) Mutations
in the channel domain of a neuronal nicotinic receptor convert ion selectivity from cationic to
anionic. Nature 359(6395):500–505. doi:10.1038/359500a0
Getz EB, Xiao M, Chakrabarty T, Cooke R, Selvin PR (1999) A comparison between the sulfhy-
dryl reductants tris(2-carboxyethyl)phosphine and dithiothreitol for use in protein biochem-
istry. Anal Biochem 273(1):73–80. doi:10.1006/abio.1999.4203S0003-2697(99)94203-3 [pii]
Giraudat J, Dennis M, Heidmann T, Chang JY, Changeux JP (1986) Structure of the high-affinity
binding site for noncompetitive blockers of the acetylcholine receptor: serine-262 of the delta
subunit is labeled by [^3 H]chlorpromazine. Proc Natl Acad Sci U S A 83(8):2719–2723
Giraudat J, Dennis M, Heidmann T, Haumont PY, Lederer F, Changeux JP (1987) Structure of the
high-affinity binding site for noncompetitive blockers of the acetylcholine receptor: [^3 H]chlor-
promazine labels homologous residues in the beta and delta chains. Biochemistry 26(9):2410–2418