ABCMdb

ABCA1 p.Ala1046Asp

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Publications

PMID: 19019193 [PubMed] Pisciotta L et al: "Severe HDL deficiency due to novel defects in the ABCA1 transporter."

No. Sentence Comment

13 Two patients were homozygous for mutations in the coding region of the ABCA1 gene, resulting in an amino acid substitution (p.A1046D) and a truncated protein (p.I74YFsX76). Login to comment
17 ABCA1-mediated cholesterol efflux was abolished in fibroblasts from patients with p.A1046D and del p.D1567_K1591 mutants and in fibroblasts homozygous for p.R587W. Login to comment
93 The proband was found to be homozygous for a C>A transversion in exon 22 (c.3137 C>A) of the ABCA1 gene, causing a nonconservative amino acid substitution (p.A1046D). Login to comment
97 He had a mild dysmorphism (coarse facial features), developmental and speech delay, abnormal gait, congenital cataracts (removed at 2 weeks of life), hypertrophied tonsils and adenoids (tonsillo-adenoidectomy at 2 years of age), yellowish pharyngeal deposits, no Table 1 ABCA1 alleles, demographics and plasma lipid, lipoprotein and apolipoprotein concentrations in members of the four families Subject ABCA1 gene alleles Age (years) Sex BMI (kg m)2 ) TC (mmol L)1 ) LDL-C (mmol L)1 ) HDL-C (mmol L)1 ) TG (mmol L)1 ) Apo A-I (mg dL)1 ) Apo B (mg dL)1 ) APOE genotype CAD Family 1 I.1 W / W 74 M 24.0 5.33 3.38 1.47 1.02 - - - I.2 M1 / M1 72 M 23.0 1.24 0.75 0.08 1.29 <5 59 33 + Family 2 I.2 M2 / W 34 F 34.0 2.51 1.40 0.70 0.91 - - - II.1 M2 / M2 7 M 14.6 1.89 0.90 0.10 1.93 <5 - 34 Family 3 I.1 M3 / W 33 M - 5.61 ND 0.77 ND 88 141 33 I.2 M3 / W 27 F - 3.26 ND 1.08 ND 126 60 33 II.1 M3 / M3 4 M - 1.47 0.95 0.02 1.07 <5 82 33 Family 4 I.1 M4 / W 70 M - 8.01 6.30 1.19 1.13 145 160 33 +++ I.2 M5 / W 68 F - 6.69 4.76 1.24 1.50 153 145 33 I.4 M5 / W 67 F - 5.48 3.82 1.24 0.90 151 89 33 II.2 M4 / W 47 F - 6.59 4.34 1.19 2.29 148 129 33 II.3 M4 / M5 42 M - 4.70 3.98 0.10 1.35 <5 114 33 II.4 M5 / W 48 F - 3.64 2.76 0.59 0.60 92 73 33 + II.5 W / W 47 F - 4.70 3.05 1.24 0.90 150 80 23 II.6 M5 / W 42 M - 4.83 3.64 0.54 1.40 78 85 23 + II.7 M5 / W 41 F - 3.89 2.02 1.08 0.60 138 65 23 III.1 M4 / W 24 F - 3.70 1.65 1.73 0.70 170 71 34 W, ABCA1 wild type allele; M, ABCA1 mutant allele: M1 (p.A1046D); M2 (del. Login to comment
155 Cholesterol efflux from cultured fibroblasts ABCA1-mediated cholesterol efflux was evaluated in fibroblasts from the probands of families 1 and 2, homozygous for the p.A1046D substitution and for the splice site mutation in intron 35 (c.4773 + 1g>a, del p.D1567_K1591) respectively. Login to comment
162 In the p.A1046D (family 1) and homozygous p.R587W cells this increase was significant, although much lower than that of control cells, whilst in c.4773 + 1g>a mutant cells (family 2) no increase in membrane cholesterol was observed. Login to comment
169 Ctrl, control cells; p.R587W, fibroblasts from a homozygous patient reported previously [24]; p.A1046D, fibroblasts from the proband of family 1; del p.D1567_K1591, fibroblasts of the proband of family 2. able, even though its content appears to be lower than that seen in control fibroblasts. Login to comment
181 Ctrl, control cells; p.R587W, fibroblasts from a homozygous patient reported previously [24]; p.A1046D, fibroblasts from the proband of family 1; del p.D1567_K1591, fibroblasts of the proband of family 2. Login to comment
184 Lanes 1 and 2: control fibroblasts before (lane 1) and after (lane 2) stimulation of ABCA1 gene expression with 22OH / cRA; lane 3: fibroblasts from a homozygous patient for p.R578W mutation reported previously [24]; lane 4: fibroblasts of a compound heterozygote for ABCA1 null alleles reported previously [21]; lane 5: p.A1046D fibroblasts from the proband of family 1; lane 6: del p.D1567_K1591 fibroblasts from the proband of family 2. Login to comment
210 The proband of family 1 was homozygous for a missense mutation (p.A1046D) previously reported by Wang et al. [31] in a kindred with HDL deficiency, which included three compound heterozygotes (whose second mutant allele was a nucleotide insertion in exon 34 - c.4630 ins A - causing a frameshift) and two heterozygotes for this mutation. Login to comment
211 Previous in vitro experiments have shown that the p.A1046D mutation, which occurs in the intracellular domain between the first Walker A and B motifs, severely impairs cholesterol efflux from transfected cells, even if it does not abolish the localization of ABCA1 in the plasma membrane, where it retains a residual capacity to bind Apo A-I [32]. Login to comment

PMID: 16873719 [PubMed] Singaraja RR et al: "Specific mutations in ABCA1 have discrete effects on ABCA1 function and lipid phenotypes both in vivo and in vitro."

No. Sentence Comment

46 Indeed, patients heterozygous for the mutations R587W, Q597R, ⌬L693, N935S, A1046D, C1477R, and R2081W had between 47% and 69% of HDL-C levels of controls (Table). Login to comment
50 Two mutants, A1046D and S1506L, showed an intermediate phenotype where plasma membrane localization was reduced (Figure 2A). Login to comment
60 Mutant A1046D showed an intermediate phenotype with some ABCA1 localized at the plasma membrane (Figure 2C). Login to comment
71 The A1046D and S1506L mutants displayed a partial ability to induce cell surface ApoA-I binding (56.3Ϯ16.4%, nϭ3, Pϭ0.02 and 61.0Ϯ12.7%, nϭ3, Pϭ0.004, respectively; Figure 3A), suggesting that in these mutants, some of the protein is localized at the plasma membrane. Login to comment
79 A1046D and S1506L showed reduced localization at the plasma membrane, and C1477R, D1289L, and P2150L showed localization at the plasma membrane and intracellularly. Login to comment
85 A1046D showed intermediate plasma membrane localization and the other missense mutations showed little plasma membrane localization. Login to comment
152 Both A1046D and S1506L were partially localized at the plasma membrane and showed significantly reduced ApoA-I binding. Login to comment
154 The mutation A1046D, however, occurs in the intracellular domain of ABCA1 and is localized between the first Walker A and B motifs. Login to comment

PMID: 16704350 [PubMed] Brunham LR et al: "Variations on a gene: rare and common variants in ABCA1 and their impact on HDL cholesterol levels and atherosclerosis."

No. Sentence Comment

555 Since a complete loss of function allele would be expected to result in a 50% reduction in HDL levels, a greater than 50% reduction in HDL is most likely explained by a dominant negative allele, in which TABLE 3 Patient phenotypes associated with heterozygous ABCA1 mutations Mutation HDL (mmol/L) HDL (% of control) Number of patients M1091T 0.48 ± 0.5 30 ± 30 4 G1216V 0.50 40 1 R2144X 0.56 ± 0.2 41 ± 18 12 R282X 0.52 41 1 R909X 0.59 ± 0.3 42 ± 19 5 K776N 0.55 ± 0.1 47 ± 5 2 R587W 0.61 ± 0.1 47 ± 8 7 S364C 0.60 48 1 P1065S 0.80 51 1 c-ter deletion 0.75 53 1 N1800H - 56.5 33 P85L 0.72 ± 0.4 57 ± 33 5 Del693L 0.79 ± 0.2 57 ± 15 8 D1289N 0.80 ± 0.1 59 ± 12 4 R2081W 0.80 ± 0.1 59 ± 12 4 2203X 0.80 ± 0.2 59 ± 20 4 DelED1893,4 0.77 ± 0.2 59 ± 18 8 2145X 0.82 ± 0.1 59 ± 9 4 A1046D 0.70 ± 0.1 60 ± 8 2 Q597R 0.82 ± 0.1 60 ± 5 5 C1477R 0.82 ± 0.2 61 ± 15 9 IVS25 + 1G > C 0.78 ± 0.1 62 ± 12 4 D1099Y 0.83 ± 0.3 63 ± 21 5 1552X 1.00 64 1 F2009S 0.82 ± 0.2 64 ± 19 6 R587W 0.86 ± 0.1 65 ± 17 2 R1068H 0.90 ± 0.3 67 ± 26 9 N935S 1.00 ± 0.3 74 ± 16 7 T929I 1.01 ± 0.2 76 ± 7 8 1284X 1.11 ± 0.2 83 ± 14 5 A937V 1.15 ± 0.6 85 ± 28 2 R1680W 1.22 ± 0.2 87 ± 17 3 635X 1.24 ± 0.5 90 ± 32 7 W590S 1.32 ± 0.6 103 ± 46 15 the mutant protein actually interferes with the activity of the remaining wild-type protein. Login to comment

PMID: 16429166 [PubMed] Brunham LR et al: "Accurate prediction of the functional significance of single nucleotide polymorphisms and mutations in the ABCA1 gene."

No. Sentence Comment

48 This SNP has been reported to be associated with decreased HDL cholesterol and increased severity of atherosclerosis in Table 1. subPSEC Scores and Probability of Functional Impairment (Pdeleterious) for ABCA1 Mutations and SNPs Mutations SNPs Variant SubPSEC Pdeleterious Variant subPSEC Pdeleterious P85L À4.62 0.83 R219K À0.57 0.08 H160F À2.79 0.45 V399A À2.26 0.32 R230C À4.27 0.78 V771M À2.86 0.46 A255T À1.81 0.23 T774P À1.99 0.27 E284K À2.34 0.34 K776N À3.53 0.63 Y482C À4.21 0.77 V825I À1.06 0.13 R587W À6.04 0.95 I883M À1.38 0.17 W590S À5.19 0.9 E1172D À1.96 0.26 W590L À4.48 0.82 R1587K À0.58 0.08 Q597R À7.15 0.98 S1731C À4.21 0.77 T929I À4.29 0.78 N935H À8.54 1 N935S À7.53 0.99 A937V À6.6 0.97 A1046D À7.52 0.99 M1091T À3.56 0.64 D1099Y À6.09 0.96 D1289N À2.48 0.37 L1379F À3.81 0.69 C1477R À5.44 0.92 S1506L À5.17 0.9 N1611D À5.69 0.94 R1680W À6.02 0.95 V1704D À3.21 0.55 N1800H À4.23 0.77 R1901S À5.06 0.89 F2009S À2.73 0.43 R2081W À8.08 0.99 P2150L À2.88 0.47 Q2196H À2.74 0.43 DOI: 10.1371/journal.pgen.0010083.t001 PLoS Genetics | www.plosgenetics.org December 2005 | Volume 1 | Issue 6 | e83 0740 Accurate Prediction of ABCA1 Variants Synopsis A major goal of human genetics research is to understand how genetic variation leads to differences in the function of genes. Login to comment
75 Cholesterol Efflux Values for 293 Cells Transfected with ABCA1 Variants and subPSEC and PolyPhen Predictions of the Functional Impact of these Variants Variant Variant Type subPSEC Cholesterol Efflux PolyPhen R2081W Mutation À8.08 21.1 6 21%* Probably damaging N935S Mutation À7.53 29.3 6 13%* Benign A1046D Mutation À7.52 16.8 6 7%* Possibly damaging Q597R Mutation À7.15 17.7 6 14%* Probably damaging R587W Mutation À6.04 31.7 6 33%* Probably damaging C1477R Mutation À5.44 20.5 6 10%* Probably damaging W590S Mutation À5.19 47.1 6 13%* Probably damaging S1506L Mutation À5.17 17.8 6 15%* Probably damaging T929I Mutation À4.29 69.9 6 11%* Possibly damaging N1800H Mutation À4.23 31.3 6 16%* Possibly damaging S1731C SNP À4.21 12.3 6 10%* Possibly damaging M1091T Mutation À3.56 6.9 6 20%* Probably damaging P2150L Mutation À2.88 88.4 6 21% Probably damaging V771M SNP À2.86 145.4 6 33% Benign D1289N Mutation À2.48 137.7 6 86% Benign I883M SNP À1.38 69.1 6 16%* Benign R219K SNP À0.57 103.7 6 21.05 Benign Wild-type - 0.0 100% - *p , 0.01 compared to wild-type ABCA1. Login to comment

PMID: 15066991 [PubMed] Kockx M et al: "Apolipoprotein A-I-stimulated apolipoprotein E secretion from human macrophages is independent of cholesterol efflux."

No. Sentence Comment

7 Finally, apoA-I stimulates apoE secretion normally from macrophages of two unrelated subjects with genetically confirmed Tangier Disease (mutations C733R and c.5220-5222delTCT; and mutations A1046D and c.4629-4630insA), despite severely inhibited cholesterol efflux. Login to comment
134 Using current nomenclature, these are respectively equivalent to a missense mutation in exon 22 (c.3137CϾA; A1046D) and a frameshift mutation in exon 34 (c.4629-4630insA; A1544 fs X1552). Login to comment
135 HC2 has neither ABCA1 mutation, and HZ2A and HZ2B contain the 4629insA and the A1046D mutations, respectively. Login to comment
321 Cells from TD2, who is compound heterozygote for mutations A1046D and c.4629-4630insA, were compared with those of his healthy brother known to be free of ABCA1 mutations (HC2-HMDM), and his heterozygous parents with mutations 4629insA (HZ2A-HMDM) and A1046D (HZ2B-HMDM) (44, 45) (Table III, B). Login to comment
348 Subject Mutation HDL-C Basal apoE secretion ApoA-I-specific cholesterol efflux ApoA-I-stimulated apoE secretion mg/dL ␮g/mg cell protein ␮g/mg cell protein Aa HC1 44.0b 2.2 Ϯ 0.49b 3.1 Ϯ 0.5b 6.3 Ϯ 0.9 TD1 C733R;C.5220-5222delTCT 3.1 0.5 Ϯ 0.21 0.5 Ϯ 0.5 5.6 Ϯ 1.2 Bc HC2 43.0d 1.1 Ϯ 1.6 2.2 Ϯ 0.4d 4.2 Ϯ 1.0 TD2d A1046D;4629insA 2.7 NDe 0.2 Ϯ 0.2 3.8 Ϯ 0.7 HZ2A 4629insA 25.8d ND 1.9 Ϯ 0.3d 2.6 Ϯ 0.6 HZ2B A1046D 38.6d 1.4 Ϯ 0.2 2.8 Ϯ 0.1d 4.5 Ϯ 0.9 a Part A: macrophages from newly characterized TD1 and unrelated control subject HC1 were compared for cholesterol efflux and apoE secretion in the presence and absence of 25 ␮g/ml apoA-I. Cholesterol efflux and apoE secretion were determined at 8 h, and apoA-I-specific efflux derived by subtracting efflux to control medium (without A-I) from that to apoA-I. b Conditions are significantly different between HC1 and TD1, p Ͻ 0.01. c Part B: TD2 has previously been described (44). Login to comment
136 HC2 has neither ABCA1 mutation, and HZ2A and HZ2B contain the 4629insA and the A1046D mutations, respectively. Login to comment
320 Cells from TD2, who is compound heterozygote for mutations A1046D and c.4629-4630insA, were compared with those of his healthy brother known to be free of ABCA1 mutations (HC2-HMDM), and his heterozygous parents with mutations 4629insA (HZ2A-HMDM) and A1046D (HZ2B-HMDM) (44, 45) (Table III, B). Login to comment
346 Subject Mutation HDL-C Basal apoE secretion ApoA-I-specific cholesterol efflux ApoA-I-stimulated apoE secretion mg/dL òe;g/mg cell protein òe;g/mg cell protein Aa HC1 44.0b 2.2 afe; 0.49b 3.1 afe; 0.5b 6.3 afe; 0.9 TD1 C733R;C.5220-5222delTCT 3.1 0.5 afe; 0.21 0.5 afe; 0.5 5.6 afe; 1.2 Bc HC2 43.0d 1.1 afe; 1.6 2.2 afe; 0.4d 4.2 afe; 1.0 TD2d A1046D;4629insA 2.7 NDe 0.2 afe; 0.2 3.8 afe; 0.7 HZ2A 4629insA 25.8d ND 1.9 afe; 0.3d 2.6 afe; 0.6 HZ2B A1046D 38.6d 1.4 afe; 0.2 2.8 afe; 0.1d 4.5 afe; 0.9 a Part A: macrophages from newly characterized TD1 and unrelated control subject HC1 were compared for cholesterol efflux and apoE secretion in the presence and absence of 25 òe;g/ml apoA-I. Cholesterol efflux and apoE secretion were determined at 8 h, and apoA-I-specific efflux derived by subtracting efflux to control medium (without A-I) from that to apoA-I. b Conditions are significantly different between HC1 and TD1, p b0d; 0.01. c Part B: TD2 has previously been described (44). Login to comment

PMID: 12763760 [PubMed] Singaraja RR et al: "Efflux and atherosclerosis: the clinical and biochemical impact of variations in the ABCA1 gene."

No. Sentence Comment

83 TABLE 2. Conservation of Amino Acid Residues Mutated in Humans Mutation H. sapiens M. musculus G. gallus D. melanogaster C. elegans P85L P P P ⅐ ⅐ ⅐ P R230C R R R P G A255T A A S ⅐ ⅐ ⅐ ⅐ ⅐ ⅐ R587W R R R ⅐ ⅐ ⅐ ⅐ ⅐ ⅐ W590S W W W R Q Q597R Q Q Q Q Q ⌬L693 L L L L L T929I T T T T T N935S/H N N N N N A937V A A A A A A1046D A A A A A M1091T M M M M M D1099Y D D D D D D1289L/N D D D D D C1477R C C C ⅐ ⅐ ⅐ ⅐ ⅐ ⅐ S1506L S S S ⅐ ⅐ ⅐ ⅐ ⅐ ⅐ N1611D N N N N S R1680W R R R R R N1800H N N N A W F2009S F F F I M R2081W R R R R R P2150L P P P R N ⌬E1893 E E E D S ⌬D1894 D D D D D Twenty-three of 24 (95.83%) amino acids affected by mutations are conserved with G. gallus, reflecting the functional importance of these residues. Login to comment
75 TABLE 2. Conservation of Amino Acid Residues Mutated in Humans Mutation H. sapiens M. musculus G. gallus D. melanogaster C. elegans P85L P P P ዼ ዼ ዼ P R230C R R R P G A255T A A S ዼ ዼ ዼ ዼ ዼ ዼ R587W R R R ዼ ዼ ዼ ዼ ዼ ዼ W590S W W W R Q Q597R Q Q Q Q Q èc;L693 L L L L L T929I T T T T T N935S/H N N N N N A937V A A A A A A1046D A A A A A M1091T M M M M M D1099Y D D D D D D1289L/N D D D D D C1477R C C C ዼ ዼ ዼ ዼ ዼ ዼ S1506L S S S ዼ ዼ ዼ ዼ ዼ ዼ N1611D N N N N S R1680W R R R R R N1800H N N N A W F2009S F F F I M R2081W R R R R R P2150L P P P R N èc;E1893 E E E D S èc;D1894 D D D D D Twenty-three of 24 (95.83%) amino acids affected by mutations are conserved with G. gallus, reflecting the functional importance of these residues. Login to comment

PMID: 12840658 [PubMed] Miller M et al: "Genetics of HDL regulation in humans."

No. Sentence Comment

66 TD 1591 T/C 11 V399A extracellular [68] TD 1979 (110bpAlu Ins) 12 truncated truncation [60] TD/FHA 2154 C/T 14 R587W extracellular [67,69] TD 2164 G/C 14 W590S extracellular [61] TD 2185 A/G 14 Q597R extracellular [59,67] TD 2219 G/del 14 truncated, 635X truncated [60,61] FHA 2472-2474 3bp del 15 Del L693 TM domain #3 [59] phosphorylation 2706 G/A 16 V771M extracellular [68] 2715 A/C 16 T774P extracellular [68] 2723 G/C 16 K776N extracellular [68] 2868 G/A 17 V825I TM domain #6 [67,68] TD/FHA 3044 A/G 18 I883M cytoplasmic [68] phosphorylat site FHA 3120 C/T 19 R909X truncation [63,71] TD 3181 C/T 19 T929I cytoplasmic [62] TD 3199 A/G 19 N935S Walker A [61] TD 3205 C/T 19 A937V Walker A [61] TD 3532 C/A 22 A1046D cytoplasmic, Walker A/B [70] FHA 3667 T/C 23 M1091T cytoplasmic [63] 3690 G/T 23 D1099Y cytoplasmic [9] TD 3738 2bp del 23 1145X truncation [66] FHA 3911 G/C 24 E1172D linker/cytoplasmic [68] FHA 4242 4bp del 27 1297X truncated [64] TD 4260 G/A 27 D1289N linker cytoplasm [64,65] TD 4824 T/C 31 C1477R extracellular [59] TD 4912 C/T 32 S1506L extracellular loop #2 [71] TD 5025 ins A 34 A1544S?1552X truncation [70] 5059 T/C 34 I1555T extracellular loop #2 [67] 5155 G/A 35 R1587K extracellular loop #2 [68] FHA 5226 A/G 36 N1611D extracellular loop #2 [75..] 5338 T/C 36 L1648P extracellular loop #2 [67] TD 5443 C/T 37 R1680W cytoplasmic [74.] Login to comment

PMID: 12196520 [PubMed] See RH et al: "Protein kinase A site-specific phosphorylation regulates ATP-binding cassette A1 (ABCA1)-mediated phospholipid efflux."

No. Sentence Comment

243 The phosphorylated Ser-1042 and Ser-2054 residues are near the ABCA1 mutations A1046D and R2081W, both of which have resulted in a clinical phenotype in humans with low high density lipoprotein cholesterol, low plasma ApoA-I, and low total cholesterol values (47- 49). Login to comment

PMID: 12111381 [PubMed] Guo Z et al: "Double deletions and missense mutations in the first nucleotide-binding fold of the ATP-binding cassette transporter A1 ( ABCA1) gene in Japanese patients with Tangier disease."

No. Sentence Comment

86 The Ala937Val mutation in Walker A motif (Bodzioch et al. 1999) and Ala1046Asp near Walker B motif (Wang et al. 2000) of the first NBF have been reported. Login to comment

PMID: 20799350 [PubMed] Kelly L et al: "Functional hot spots in human ATP-binding cassette transporter nucleotide binding domains."

No. Sentence Comment

50 Disease-associated nsSNPs at Three Structural Hotspots in Human ABC Transporter NBDs Gene Disease Position ARA motif ABCB11 BRIC2 A570T ABCD1 X-ALD A616V CFTR CF A559T ABCC6 PXE R765Q ABCC8 HHF1 R841G ABCC8 HHF1 R1493Q ABCC8 HHF1 R1493W ABCD1 X-ALD R617C ABCD1 X-ALD R617G ABCD1 X-ALD R617H CFTR CF R560K CFTR CF R560S CFTR CF R560T ABCA1 HDLD1 A1046D ABCB4 ICP A546D C-loop 1 motif ABCC8 HHF1 D1471H ABCC8 HHF1 D1471N CFTR CBAVD G544V ABCC8 HHF1 G1478R C-loop2 motif ABCA4 STGD1 H2128R ABCC8 HHF1 K889T ABCD1 X-ALD R660P ABCD1 X-ALD R660W ABCA1 HDLD2 M1091T ABCA4 STGD1 E2131K ABCA12 LI2 E1539K ABCA4 STGD1 and CORD3 E1122K CFTR CF L610S ABCC8 HHF1 L1543P ABCA1 Colorectal cancer sample; somatic mutation A2109T ABCC9 CMD1O A1513T ABCD1 X-ALD H667D CFTR CF A613T ABCA1 HDLD2 D1099Y ABCD1 X-ALD T668I CFTR CF D614G ABCA4 STGD1 R2139W ABCA4 STGD1 R1129C ABCA4 ARMD2, STGD1, and FFM R1129L Disease abbreviations are as follows: BRIC2, benign recurrent intrahepatic cholestasis type 2; X-ALD, X-linked adrenoleukodystrophy; CF, cystic fibrosis; PXE, Pseudoxanthoma elasticum; HHF1, familial hyperinsulinemic hypoglycemia-1; HDLD1, high density lipoprotein deficiency type 1; ICP, intrahepatic cholestasis of pregnancy; CBAVD, congenital bilateral absence of the vas deferens; STGD1, Stargardt disease type 1; HDLD2, high density lipoprotein deficiency type 2; LI2, ichthyosis lamellar type 2; CORD3, cone-rod dystrophy type 3; CMD1O, cardiomyopathy dilated type 1O; ARMD2, age-related macular degeneration type 2; FFM, fundus flavimaculatus. Login to comment

PMID: 26546829 [PubMed] Ramasamy I et al: "Update on the molecular biology of dyslipidemias."

No. Sentence Comment

1064 All three mutations p.A1046D, p. Y1532C and p. W1699C were reported to be deleterious in functional studies (473). Login to comment