| DHHC7-mediated palmitoylation of the accessory protein barttin critically regulates the functions of ClC-K chloride channels. | DHHC7-mediated palmitoylation of the accessory protein barttin critically regulates the functions of ClC-K chloride channels.
Gorinski N, Wojciechowski D, Guseva D, Abdel Galil D, Mueller FE, Wirth A, Thiemann S, Zeug A, Schmidt S, Zareba-Kozioł M, Wlodarczyk J, Skryabin BV, Glage S, Fischer M, Al-Samir S, Kerkenberg N, Hohoff C, Zhang W, Endeward V, Ponimaskin E., Free PMC Article | 12/26/2020 |
| Increasing expression of barttin over that of ClC-K partially recovered this insufficiency, indicating that N-terminal modifications of barttin alter both binding affinities and gating properties | Activation of renal ClC-K chloride channels depends on an intact N terminus of their accessory subunit barttin.
Wojciechowski D, Thiemann S, Schaal C, Rahtz A, de la Roche J, Begemann B, Becher T, Fischer M., Free PMC Article | 01/19/2019 |
| These results suggest that BSND is expressed only in normal salivary glands and oncocytic salivary gland tumors such as Warthin's tumor and oncocytoma | BSND is a Novel Immunohistochemical Marker for Oncocytic Salivary Gland Tumors.
Shinmura K, Kato H, Kawanishi Y, Kamo T, Inoue Y, Yoshimura K, Sugiyama K, Misawa K, Hosokawa S, Mineta H, Sugimura H. | 09/1/2018 |
| results demonstrate that the carboxyl terminus of hClC-Kb is not part of the binding site for barttin, but functionally modifies the interplay with barttin. | Carboxyl-terminal Truncations of ClC-Kb Abolish Channel Activation by Barttin Via Modified Common Gating and Trafficking.
Stölting G, Bungert-Plümke S, Franzen A, Fahlke C., Free PMC Article | 04/23/2016 |
| These results demonstrate that mutations in a cluster of hydrophobic residues within transmembrane domain 1 affect barttin-CLC-K interaction and impair gating modification by the accessory subunit | Tryptophan Scanning Mutagenesis Identifies the Molecular Determinants of Distinct Barttin Functions.
Wojciechowski D, Fischer M, Fahlke C., Free PMC Article | 10/24/2015 |
| R8W and G47R, two naturally occurring barttin mutations identified in patients with Bartter syndrome type IV, reduce barttin palmitoylation and CLC-K/barttin channel activity. | Human CLC-K Channels Require Palmitoylation of Their Accessory Subunit Barttin to Be Functional.
Steinke KV, Gorinski N, Wojciechowski D, Todorov V, Guseva D, Ponimaskin E, Fahlke C, Fischer M., Free PMC Article | 10/3/2015 |
| BSND, was first modeled, and then, the identified mutation was further analyzed by using different bioinformatics tools. | Identification of missense mutation (I12T) in the BSND gene and bioinformatics analysis.
Iqbal H, Sarfaraz T, Anjum F, Anwar Z, Mir A., Free PMC Article | 08/27/2011 |
| Case Report: G47R mutation decreases barttin expression, resulting CIC-K location being changed from the basement membrane to the cytoplasm in the tubule and might have varying effects on renal function associated with factors other than this gene. | Renal dysfunction and barttin expression in Bartter syndrome Type IV associated with a G47R mutation in BSND in a family.
Park CW, Lim JH, Youn DY, Chung S, Lim MH, Kim YK, Chang YS, Lee JH. | 04/9/2011 |
| Observational study of gene-disease association, gene-environment interaction, and pharmacogenomic / toxicogenomic. (HuGE Navigator) | Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study.
Bailey SD, Xie C, Do R, Montpetit A, Diaz R, Mohan V, Keavney B, Yusuf S, Gerstein HC, Engert JC, Anand S, DREAM investigators., Free PMC Article | 09/15/2010 |
| Observational study of gene-disease association. (HuGE Navigator) | Gene-centric association signals for lipids and apolipoproteins identified via the HumanCVD BeadChip.
Talmud PJ, Drenos F, Shah S, Shah T, Palmen J, Verzilli C, Gaunt TR, Pallas J, Lovering R, Li K, Casas JP, Sofat R, Kumari M, Rodriguez S, Johnson T, Newhouse SJ, Dominiczak A, Samani NJ, Caulfield M, Sever P, Stanton A, Shields DC, Padmanabhan S, Melander O, Hastie C, Delles C, Ebrahim S, Marmot MG, Smith GD, Lawlor DA, Munroe PB, Day IN, Kivimaki M, Whittaker J, Humphries SE, Hingorani AD, ASCOT investigators, NORDIL investigators, BRIGHT Consortium., Free PMC Article | 09/15/2010 |
| The molecular basis of DFNB73 autosomal recessive deafness is reported. | Molecular basis of DFNB73: mutations of BSND can cause nonsyndromic deafness or Bartter syndrome.
Riazuddin S, Anwar S, Fischer M, Ahmed ZM, Khan SY, Janssen AG, Zafar AU, Scholl U, Husnain T, Belyantseva IA, Friedman PL, Riazuddin S, Friedman TB, Fahlke C, Riazuddin S, Anwar S, Fischer M, Ahmed ZM, Khan SY, Janssen AG, Zafar AU, Scholl U, Husnain T, Belyantseva IA, Friedman PL, Riazuddin S, Friedman TB, Fahlke C., Free PMC Articles: PMC2725234, PMC2725234 | 01/21/2010 |
| Mutations of BSND can cause nonsyndromic deafness or Bartter syndrome. | Molecular basis of DFNB73: mutations of BSND can cause nonsyndromic deafness or Bartter syndrome.
Riazuddin S, Anwar S, Fischer M, Ahmed ZM, Khan SY, Janssen AG, Zafar AU, Scholl U, Husnain T, Belyantseva IA, Friedman PL, Riazuddin S, Friedman TB, Fahlke C, Riazuddin S, Anwar S, Fischer M, Ahmed ZM, Khan SY, Janssen AG, Zafar AU, Scholl U, Husnain T, Belyantseva IA, Friedman PL, Riazuddin S, Friedman TB, Fahlke C., Free PMC Articles: PMC2725234, PMC2725234 | 01/21/2010 |
| In a large cohort of ante/neonatal Bartter syndrome, deafness, transient hyperkalaemia and severe hypokalaemic hypochloraemic alkalosis orientate molecular investigations to BSND, KCNJ1 and CLCNKB genes, respectively. | Phenotype-genotype correlation in antenatal and neonatal variants of Bartter syndrome.
Brochard K, Boyer O, Blanchard A, Loirat C, Niaudet P, Macher MA, Deschenes G, Bensman A, Decramer S, Cochat P, Morin D, Broux F, Caillez M, Guyot C, Novo R, Jeunemaître X, Vargas-Poussou R. | 01/21/2010 |
| Deletion of exons 2-4 in the BSND gene causes severe antenatal Bartter syndrome. | Deletion of exons 2-4 in the BSND gene causes severe antenatal Bartter syndrome.
Bircan Z, Harputluoglu F, Jeck N. | 01/21/2010 |
| Bartter syndrome type IV can be caused by various derangements in the function of barttin, likely contributing to the diversity of observed phenotypes. | Disease-causing dysfunctions of barttin in Bartter syndrome type IV.
Janssen AG, Scholl U, Domeyer C, Nothmann D, Leinenweber A, Fahlke C., Free PMC Article | 01/21/2010 |
| Observational study of genotype prevalence and gene-disease association. (HuGE Navigator) | Functional BSND variants in essential hypertension.
Sile S, Gillani NB, Velez DR, Vanoye CG, Yu C, Byrne LM, Gainer JV, Brown NJ, Williams SM, George AL Jr, Sile S, Gillani NB, Velez DR, Vanoye CG, Yu C, Byrne LM, Gainer JV, Brown NJ, Williams SM, George AL Jr. | 03/13/2008 |
| Observational study of genotype prevalence. (HuGE Navigator) | Haplotype diversity in four genes (CLCNKA, CLCNKB, BSND, NEDD4L) involved in renal salt reabsorption.
Sile S, Velez DR, Gillani NB, Alexander CA, George AL Jr, Williams SM., Free PMC Article | 03/13/2008 |
| Observational study of gene-disease association and gene-environment interaction. (HuGE Navigator) | Common genetic variants and haplotypes in renal CLCNKA gene are associated to salt-sensitive hypertension.
Barlassina C, Dal Fiume C, Lanzani C, Manunta P, Guffanti G, Ruello A, Bianchi G, Del Vecchio L, Macciardi F, Cusi D. | 03/13/2008 |
| Disruption of the gene encoding Barttin, BSND, results in a 'double knockout' of the functions of both ClCKA and ClCKB, manifesting as Bartter syndrome type IV with sensorineural deafness and an especially severe salt-losing phenotype. | Mechanisms of Disease: the kidney-specific chloride channels ClCKA and ClCKB, the Barttin subunit, and their clinical relevance.
Krämer BK, Bergler T, Stoelcker B, Waldegger S. | 01/21/2010 |
| BSND-V43I, a common variant conferring partial loss of function, exhibits significant deviation from equilibrium in the Ghanaian normotensive control population | Functional BSND variants in essential hypertension.
Sile S, Gillani NB, Velez DR, Vanoye CG, Yu C, Byrne LM, Gainer JV, Brown NJ, Williams SM, George AL Jr, Sile S, Gillani NB, Velez DR, Vanoye CG, Yu C, Byrne LM, Gainer JV, Brown NJ, Williams SM, George AL Jr. | 01/21/2010 |
| Barttin mutations is associated with antenatal Bartter syndrome with sensorineural deafness | Barttin mutations in antenatal Bartter syndrome with sensorineural deafness.
Ozlu F, Yapicioğlu H, Satar M, Narli N, Ozcan K, Buyukcelik M, Konrad M, Demirhan O. | 01/21/2010 |
| The mislocalization of CLC-K2 was identified as the molecular pathogenesis of Bartter syndrome by mutant barttins. | Molecular mechanisms of Bartter syndrome caused by mutations in the BSND gene.
Hayama A, Rai T, Sasaki S, Uchida S. | 01/21/2010 |
| ClC-Ka/barttin channels are regulated by SGK1 and SGK3, which may thus participate in the regulation of transport in kidney and inner ear. | Regulation of CLC-Ka/barttin by the ubiquitin ligase Nedd4-2 and the serum- and glucocorticoid-dependent kinases.
Embark HM, Böhmer C, Palmada M, Rajamanickam J, Wyatt AW, Wallisch S, Capasso G, Waldegger P, Seyberth HW, Waldegger S, Lang F. | 01/21/2010 |
| Barttin modulates trafficking and function of ClC-K1 and ClC-Kb channels | Barttin modulates trafficking and function of ClC-K channels.
Scholl U, Hebeisen S, Janssen AG, Müller-Newen G, Alekov A, Fahlke C., Free PMC Article | 01/21/2010 |
| A missense, point mutation on gene BSND exon 1, affects the function of the CLC-K/barttin chloride channel and caused Bartter syndrome with sensorineural deafness in two families from Spain. | Mutation G47R in the BSND gene causes Bartter syndrome with deafness in two Spanish families.
García-Nieto V, Flores C, Luis-Yanes MI, Gallego E, Villar J, Claverie-Martín F. | 01/21/2010 |