Inna Sabirzhanova
Overview
Explore the profile of Inna Sabirzhanova including associated specialties, affiliations and a list of published articles.
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Articles
12
Citations
170
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Recent Articles
1.
Liu Q, Sabirzhanova I, Bergbower E, Yanda M, Guggino W, Cebotaru L
Cell Physiol Biochem
. 2019 Aug;
53(2):400-412.
PMID: 31403270
Background/aims: Mutations in ABCA4 cause Stargardt macular degeneration, which invariably ends in legal blindness. We studied two common mutants, A1038V (in NBD1) and G1961E (in NBD2), with the purpose of...
2.
Bergbower E, Sabirzhanova I, Boinot C, Guggino W, Cebotaru L
Cell Physiol Biochem
. 2019 Apr;
52(6):1267-1279.
PMID: 31026390
Background/aims: Because of the small size of adeno-associated virus, AAV, the cystic fibrosis conductance regulator, CFTR, cDNA is too large to fit within AAV and must be truncated. We report...
3.
Sabirzhanova I, Boinot C, Guggino W, Cebotaru L
Cell Physiol Biochem
. 2018 Nov;
51(3):1489-1499.
PMID: 30485852
Background/aims: Cystic fibrosis (CF) is a lethal recessive disorder caused by mutations in the CF transmembrane conductance regulator (CFTR). ΔF508, the most common mutation, is a misfolded protein that is...
4.
Liu Q, Sabirzhanova I, Yanda M, Bergbower E, Boinot C, Guggino W, et al.
J Cyst Fibros
. 2018 Jun;
17(5):582-594.
PMID: 29936070
The missing phenylalanine at position 508, located in nucleotide-binding domain (NBD1) of the cystic fibrosis transmembrane regulator (CFTR), is the most common cystic fibrosis mutation. Severe disease-causing mutations also occur...
5.
Bergbower E, Boinot C, Sabirzhanova I, Guggino W, Cebotaru L
Cell Physiol Biochem
. 2018 Feb;
45(2):639-655.
PMID: 29402832
Background/aims: The CFTR-Associated Ligand (CAL), a PDZ domain containing protein with two coiled-coil domains, reduces cell surface WT CFTR through degradation in the lysosome by a well-characterized mechanism. However, CAL's...
6.
Lopes-Pacheco M, Boinot C, Sabirzhanova I, Rapino D, Cebotaru L
Cell Physiol Biochem
. 2017 Apr;
41(6):2194-2210.
PMID: 28448979
Background/aims: Premature degradation of mutated cystic fibrosis transmembrane conductance regulator (CFTR) protein causes cystic fibrosis (CF), the commonest Mendelian disease in Caucasians. Despite recent advances in precision medicines for CF...
7.
Lopes-Pacheco M, Sabirzhanova I, Rapino D, Morales M, Guggino W, Cebotaru L
Chembiochem
. 2016 Feb;
17(6):493-505.
PMID: 26864378
We evaluated whether small molecule correctors could rescue four nucleotide-binding domain 1 (NBD1) mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) gene (A455E, S492F, ΔI507, and R560T). We first...
8.
Lopes-Pacheco M, Boinot C, Sabirzhanova I, Morales M, Guggino W, Cebotaru L
J Biol Chem
. 2015 Sep;
290(42):25636-45.
PMID: 26336106
Correcting the processing of ΔF508-CFTR, the most common mutation in cystic fibrosis, is the major goal in the development of new therapies for this disease. Here, we determined whether ΔF508...
9.
Sabirzhanova I, Lopes Pacheco M, Rapino D, Grover R, Handa J, Guggino W, et al.
J Biol Chem
. 2015 Jun;
290(32):19743-55.
PMID: 26092729
Stargardt disease is the most common form of early onset macular degeneration. Mutations in ABCA4, a member of the ATP-binding cassette (ABC) family, are associated with Stargardt disease. Here, we...
10.
Rapino D, Sabirzhanova I, Lopes-Pacheco M, Grover R, Guggino W, Cebotaru L
PLoS One
. 2015 Mar;
10(3):e0119796.
PMID: 25799511
Although, the most common Cystic Fibrosis mutation, ΔF508, in the cystic fibrosis transmembrane regulator. (CFTR), is located in nucleotide binding domain (NBD1), disease-causing mutations also occur in NBD2. To provide...