ABCC7 p.Lys335His
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PMID: 9512029
[PubMed]
Mansoura MK et al: "Cystic fibrosis transmembrane conductance regulator (CFTR) anion binding as a probe of the pore."
No.
Sentence
Comment
229
Hipper et al. (1995) reported that the mutations R334E, R334H, K335E, K335H, R347E, and R347H did not alter CFTR conduction properties, but careful inspection of the data presented revealed that the level of CFTR expression was very low so that altered properties of mutant CFTRs might have been easily obscured.
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ABCC7 p.Lys335His 9512029:229:70
status: NEW
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
6
The following mutations were examined: K335E, R347E, R334E, K335H, R347H, R334H.
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ABCC7 p.Lys335His 7589561:6:60
status: NEW9 Various mutants for which positively charged amino acids were replaced by histidines (K335H, R347H, R334H) did not show pH sensitivity of the IBMX activated wc conductance.
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ABCC7 p.Lys335His 7589561:9:86
status: NEW32 Synthesis of mutated CFTR-cDNA was induced by annealing of ampicillin repair oligonucleotide and oligonucleotide primers carrying the respective mutation changing positively charged to negatively charged amino acids (R334E, R347E, K335E) or replacing R and K at these positions by histidines (R334H, R347H, K335H).
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ABCC7 p.Lys335His 7589561:32:307
status: NEW76 I R334EIIR334HI K335E...... I K335H I R347EII R347H l (n=16) n=10) (n=10) (n=24) (n=9) "° ,11 ml I'lnt;"i' ii Illll 111 0.8 X T °., I ~ 0.4 0.2 I o.o ~ ~ ~ 6!~ 6 ~ 8 ~ ,I I ~ ...... ] J I I L ...... ,j I I t 1 I * *J t........ ~,_J L * * I * *I _ J I .......... I I , * * * , (n=18) (n=lO) (n=22) (n=7) 1.o - T T (n=8) (n=14) T / T T T o.eT T T o 1 "~ 0.4-O 0.2- oo_ L__J , i I i t - - I 1 I I I ~ t J L ' t * J I__~ * I [ * * I l * * j l.
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ABCC7 p.Lys335His 7589561:76:30
status: NEW80 Next, positively charged amino acids R334, R347, K335 located in the putative 6th pore forming transmembrane a-helical domain of CFTR, were exchanged by histidines (R334H, R347H, K335H) or by the negatively charged glutamate (R334E, R347E, K335E).
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ABCC7 p.Lys335His 7589561:80:179
status: NEW81 Wc conductances were activated significantly by IBMX in all 6 mutants but to variable degrees (AG in/.tS): 3.2 + 0.6 (R334E, n = 20), 2.7 + 0.6 (R334H, n = 13), 7.1 + 0.9 (K335E, n-- 20), 2.8 + 0.7 (K335H, n = 10), 3.2 + 0.04 (R347E, n = 32) and 1.8 + 0.3 (R347H, n = 10).
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ABCC7 p.Lys335His 7589561:81:199
status: NEW91 Following previous experiments [7] wc C1- conductances were examined in mutants bearing a histidine mutation (K335H, R347H, R334H) at different extracellular pH values.
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ABCC7 p.Lys335His 7589561:91:110
status: NEW94 aL IFEBS Letters 374 (1995) 312-316 - ~ - K335H (n=7) .... ~ .... R347H (n=8) 8 - • R334H (n=5) ...6- I~ ...L 25.5/6 7.5 8/8.5 opH Fig. 5. Summary of the conductances obtained from IBMX stimulated oocytes at different extracellular pH values.
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ABCC7 p.Lys335His 7589561:94:43
status: NEW95 Experiments were performed with oocytes overexpressing three different CFTR mutants: K335H, R347H, R334H.
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ABCC7 p.Lys335His 7589561:95:85
status: NEW108 In the present study we repeated some of the published (K335E, R347E, R347H) and performed additional mutations (R334E, R334H, K335H) which are all located in the putative sixth transmembrane domain and overexpressed the respective CFTRs in oocytes.
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ABCC7 p.Lys335His 7589561:108:127
status: NEW117 Additional mutations were constructed in which positively charged lysine and two arginines in the sixth transmembrane domain were replaced by pH-sensitive histidines (R334H, K335H, R347H).
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ABCC7 p.Lys335His 7589561:117:174
status: NEW