ABCMdb

ABCC7 p.Lys95Asp

None has been submitted yet.

Publications

PMID: 16442101 [PubMed] Frelet A et al: "Insight in eukaryotic ABC transporter function by mutation analysis."

No. Sentence Comment

366 K95D altered the whole cell anion permeability sequence by converting CFTR from a low to a high iodide permeability pore [18]. Login to comment

PMID: 11341822 [PubMed] Zou X et al: "ATP hydrolysis-coupled gating of CFTR chloride channels: structure and function."

No. Sentence Comment

56 For instance, replacing two positively charged residues with negatively charged residues in the M1 and M2 R-helices of MSD (K95D and K335E) alters the anion selectivity sequence of CFTR (17). Login to comment

PMID: 9922375 [PubMed] Sheppard DN et al: "Structure and function of the CFTR chloride channel."

No. Sentence Comment

102 This would suggest that like acidic residues (K95D and K335E) altered the whole cell other Cl0 channels, including ligand-gated Cl0 channels in anion permeability sequence by converting CFTR from a neurons (20) and outwardly rectifying Cl0 channels in low I0 permeability pore (Br0 ' Cl0 ú I0 ) to a high I0 epithelia (55), the CFTR pore has a ''weak field strength`` permeability pore (I0 ú Br0 ú Cl0 ) (4). Login to comment

PMID: 9922376 [PubMed] Dawson DC et al: "CFTR: mechanism of anion conduction."

No. Sentence Comment

431 The substitutions examined were K95D 101) or 1.0-2.0 (59, 145, 146). Login to comment
434 Finkelstein and Cass (55) called attention to the factthe order of 1:10, but two of the substitutions (K95D and K335E) altered the sequence of relative anion permeabilit- that the electrical behavior of planar lipid membranes bathed by iodide-containing solutions may be strongly in-ies by increasing the ratio for iodide, PI/PCl . Login to comment
584 This substitu- K95, to aspartic acid (K95D) increased PI/PCl (6). Login to comment

PMID: 1381146 [PubMed] Fuller CM et al: "CFTR!"

No. Sentence Comment

222 Overexpression of CFTR bearing either a K95D mutation in TM1 or a K335D mutation in TM6 in HeLa cells resulted in a shift in ion selectivity of the CAMP- l Amino acid changes corresponding to mutations in the CF gene are given in single letter code, with the changed residue followed by residue position and the substituted amino acid. Login to comment

PMID: 9804160 [PubMed] Vankeerberghen A et al: "Characterization of mutations located in exon 18 of the CFTR gene."

No. Sentence Comment

15 The anion selectivity 'lter itself seems to be formed by the transmembrane helices [11], since mutagenesis of lysine 95 to aspartate and of lysine 335 to glutamate changed the anion selectivity of the channel. Login to comment

PMID: 9879057 [PubMed] Gallet X et al: "Topological model of membrane domain of the cystic fibrosis transmembrane conductance regulator."

No. Sentence Comment

232 Mutations associated with mild forms of cystic fibrosis (R117H, R334W, and R347P) implicate three of our inner pore residues in the chloride conductance.50 In other studies, basic amino acids of membrane helices were replaced by acidic residues (K95D, K335E, R347E, and R1030E). Login to comment
236 Mutations associated with mild forms of cystic fibrosis (R117H, R334W, and R347P) implicate three of our inner pore residues in the chloride conductance.50 In other studies, basic amino acids of membrane helices were replaced by acidic residues (K95D, K335E, R347E, and R1030E). Login to comment

PMID: 9512029 [PubMed] Mansoura MK et al: "Cystic fibrosis transmembrane conductance regulator (CFTR) anion binding as a probe of the pore."

No. Sentence Comment

11 Substitution of an aspartic acid for K95 (K95D) in TM1 altered anion selectivity (Anderson et al., 1991), and three cysteine-substituted residues in this TM (G91, K95, and Q98) were identified as being accessible to water-soluble, charged, sulfhydryl-specific reagents (Akabas et al., 1994), but a CFTR construct in which the first 118 amino acids, including those that constitute TM1, were deleted produced channels with conduction properties similar to wild type (Carroll et al., 1995). Login to comment

PMID: 9511930 [PubMed] Akabas MH et al: "Probing the structural and functional domains of the CFTR chloride channel."

No. Sentence Comment

140 The mutations K95D and K335E altered the halide permeability sequence, leading to the suggestion that these residues might be involved in anion binding (Anderson et al., 1991b). Login to comment

PMID: 9379167 [PubMed] Tabcharani JA et al: "Halide permeation in wild-type and mutant cystic fibrosis transmembrane conductance regulator chloride channels."

No. Sentence Comment

277 Halide selectivity in CFTR cannot be attributed exclusively to the region around arg347; however, because high PI/PCl ratios have been reported previously for other pore mutants (K95D and K335E; Anderson et al., 1991), and because R347D retains some preference for Br- over Cl- and selects strongly against F- (our unpublished observations). Login to comment
305 Halide selectivity in CFTR cannot be attributed exclusively to the region around arg347; however, because high PI/PCl ratios have been reported previously for other pore mutants (K95D and K335E; Anderson et al., 1991), and because R347D retains some preference for Br2 over Cl2 and selects strongly against F2 (our unpublished observations). Login to comment

PMID: 9089437 [PubMed] Cheung M et al: "Locating the anion-selectivity filter of the cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel."

No. Sentence Comment

204 Based on the effects of the mutations K95D and K335E on halide selectivity sequences, Anderson et al. (1991b) concluded that Lys95 and Lys335 were determinants of halide selectivity. Login to comment

PMID: 7589561 [PubMed] Hipper A et al: "Mutations in the putative pore-forming domain of CFTR do not change anion selectivity of the cAMP activated Cl- conductance."

No. Sentence Comment

105 In fact, in a previous study lysine and arginine were replaced by negatively charged amino acids in the first and sixth transmembrane domain (K95D, K335E, R347E), respectively [1]. Login to comment

PMID: 7539989 [PubMed] Gadsby DC et al: "The CFTR chloride channel of mammalian heart."

No. Sentence Comment

18 For example, expression in 3T3 cells of two CFTR mutants, K95D and K335E, in which negatively charged amino acids replaced positively charged lysines in the first (Ml) and sixth (M6) putative transmembrane a-helices (Figure I) yielded Cl- channels with altered anion permeability sequences, 1- > B..- > Cl- instead of the normal Br > CI- > 1- (3). Login to comment

PMID: 7515047 [PubMed] Akabas MH et al: "Amino acid residues lining the chloride channel of the cystic fibrosis transmembrane conductance regulator."

No. Sentence Comment

15 Mutation of Lys-95 to Asp, in M1, and Lys-335 and Arg-347 to Glu, in M6, altered the permeability andlor conductance ratios for halides (6). Login to comment
123 Effects on single-channel properties have been observed with other missense mutations associated with mild disease (11).Mutation of Lys-95 to Asp altered the relative anionper- meability sequence of the channel, although no evidence was presented that Lys-95 actually faced the channel lumen (6). Login to comment

PMID: 1322048 [PubMed] Anderson MP et al: "Chloride channels in the apical membrane of normal and cystic fibrosis airway and intestinal epithelia."

No. Sentence Comment

69 Relative anion permeability of CAMP-regulated channels in apical membrane and in cells expressing wild-type and mutant CFTR PXlPCl- Gx/Gcl- Br- ClI- Br ClI- CAMP 3T3 fibroblasts CFTR 1.11 1.00 0.59 1.26 1.00 0.29 HeLa cells CFTR 1.24 1.00 0.57 1.02 1.00 0.39 K95D 1.25 1.00 1.43 1.39 1.00 0.75 K335E 1.06 1.00 1.37 1.71 1.00 1.43 R347E 1.24 1.00 0.90 1.46 1.00 0.47 Rl030E 1.46 1.00 0.81 1.50 1.00 0.28 Human airway epithelia Apical ND 1.00 0.41 ND 1.00 0.35 T84 epithelia Apical 1.21 1.00 0.56 0.92 1.00 0.47 over cations. Login to comment

PMID: 1375960 [PubMed] Cuthbert AW et al: "The biochemical defect in cystic fibrosis."

No. Sentence Comment

70 Changing lysine 95 to aspartic acid and lysine 335 to glutamic acid alters the selectivity of the chloride conductance fiom chloride>iodide to iodide>chloride When the R-domain was deleted the CFTR chloride conductance was increased in the unstimulated state (ie absence ofcAMP) suggesting that the R-domain is involved in thegatingofthe ion channeL A similar mechanism has beenproposedfor the gating ofpotassium channels. Login to comment

PMID: 1375035 [PubMed] Welsh MJ et al: "Cystic fibrosis transmembrane conductance regulator: a chloride channel with novel regulation."

No. Sentence Comment

87 Yet two mutations, K95D and K335E, each altered anion selectivity. Login to comment
89 Thus K95D means that lysine residue 95 was changed to aspartate.) Login to comment