| CLPB disaggregase dysfunction impacts the functional integrity of the proteolytic SPY complex. | CLPB disaggregase dysfunction impacts the functional integrity of the proteolytic SPY complex.
Baker MJ, Blau KU, Anderson AJ, Palmer CS, Fielden LF, Crameri JJ, Milenkovic D, Thorburn DR, Frazier AE, Langer T, Stojanovski D., Free PMC Article | 01/30/2024 |
| Comprehensive structural characterization of the human AAA+ disaggregase CLPB in the apo- and substrate-bound states reveals a unique mode of action driven by oligomerization. | Comprehensive structural characterization of the human AAA+ disaggregase CLPB in the apo- and substrate-bound states reveals a unique mode of action driven by oligomerization.
Wu D, Liu Y, Dai Y, Wang G, Lu G, Chen Y, Li N, Lin J, Gao N., Free PMC Article | 02/24/2023 |
| Premature Ovarian Insufficiency in CLPB Deficiency: Transcriptomic, Proteomic and Phenotypic Insights. | Premature Ovarian Insufficiency in CLPB Deficiency: Transcriptomic, Proteomic and Phenotypic Insights.
Tucker EJ, Baker MJ, Hock DH, Warren JT, Jaillard S, Bell KM, Sreenivasan R, Bakhshalizadeh S, Hanna CA, Caruana NJ, Wortmann SB, Rahman S, Pitceathly RDS, Donadieu J, Alimi A, Launay V, Coppo P, Christin-Maitre S, Robevska G, van den Bergen J, Kline BL, Ayers KL, Stewart PN, Stroud DA, Stojanovski D, Sinclair AH., Free PMC Article | 12/3/2022 |
| Heterozygous variants of CLPB are a cause of severe congenital neutropenia. | Heterozygous variants of CLPB are a cause of severe congenital neutropenia.
Warren JT, Cupo RR, Wattanasirakul P, Spencer DH, Locke AE, Makaryan V, Bolyard AA, Kelley ML, Kingston NL, Shorter J, Bellanné-Chantelot C, Donadieu J, Dale DC, Link DC., Free PMC Article | 03/12/2022 |
| Neutropenia and intellectual disability are hallmarks of biallelic and de novo CLPB deficiency. | Neutropenia and intellectual disability are hallmarks of biallelic and de novo CLPB deficiency.
Wortmann SB, Ziętkiewicz S, Guerrero-Castillo S, Feichtinger RG, Wagner M, Russell J, Ellaway C, Mróz D, Wyszkowski H, Weis D, Hannibal I, von Stülpnagel C, Cabrera-Orefice A, Lichter-Konecki U, Gaesser J, Windreich R, Myers KC, Lorsbach R, Dale RC, Gersting S, Prada CE, Christodoulou J, Wolf NI, Venselaar H, Mayr JA, Wevers RA. | 10/23/2021 |
| Human CLPB forms ATP-dependent complexes in the mitochondrial intermembrane space. | Human CLPB forms ATP-dependent complexes in the mitochondrial intermembrane space.
Thevarajan I, Zolkiewski M, Zolkiewska A. | 07/3/2021 |
| Skd3 (human ClpB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations. | Skd3 (human ClpB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations.
Cupo RR, Shorter J., Free PMC Article | 02/20/2021 |
| It present for the first time the biochemical characteristics of the human CLPB protein with the aim of shedding light on its physiological function and the pathogenesis of MEGCANN syndrome. | CLPB (caseinolytic peptidase B homolog), the first mitochondrial protein refoldase associated with human disease.
Mróz D, Wyszkowski H, Szablewski T, Zawieracz K, Dutkiewicz R, Bury K, Wortmann SB, Wevers RA, Ziętkiewicz S. | 09/19/2020 |
| The neonatal presentation of CLPB deficiency predicts the course of disease in later life, which is extremely important for counselling. | A scoring system predicting the clinical course of CLPB defect based on the foetal and neonatal presentation of 31 patients.
Pronicka E, Ropacka-Lesiak M, Trubicka J, Pajdowska M, Linke M, Ostergaard E, Saunders C, Horsch S, van Karnebeek C, Yaplito-Lee J, Distelmaier F, Õunap K, Rahman S, Castelle M, Kelleher J, Baris S, Iwanicka-Pronicka K, Steward CG, Ciara E, Wortmann SB, Additional individual contributors. | 06/9/2018 |
| Case Reports: bi-allelic CLPB mutations cause cataract, renal cysts, nephrocalcinosis and 3-methylglutaconic aciduria, a novel disorder of mitochondrial protein disaggregation. | Bi-allelic CLPB mutations cause cataract, renal cysts, nephrocalcinosis and 3-methylglutaconic aciduria, a novel disorder of mitochondrial protein disaggregation.
Kanabus M, Shahni R, Saldanha JW, Murphy E, Plagnol V, Hoff WV, Heales S, Rahman S. | 03/5/2016 |
| Disruption of CLPB is associated with congenital microcephaly, severe encephalopathy and 3-methylglutaconic aciduria | Disruption of CLPB is associated with congenital microcephaly, severe encephalopathy and 3-methylglutaconic aciduria.
Capo-Chichi JM, Boissel S, Brustein E, Pickles S, Fallet-Bianco C, Nassif C, Patry L, Dobrzeniecka S, Liao M, Labuda D, Samuels ME, Hamdan FF, Vande Velde C, Rouleau GA, Drapeau P, Michaud JL. | 01/16/2016 |
| ClpB can passively thread soluble denatured proteins. | ClpB chaperone passively threads soluble denatured proteins through its central pore.
Nakazaki Y, Watanabe YH. | 05/30/2015 |
| CLPB is proposed to function as a mitochondrial chaperone involved in disaggregation of misfolded proteins, resulting from stress such as heat denaturation. | CLPB variants associated with autosomal-recessive mitochondrial disorder with cataract, neutropenia, epilepsy, and methylglutaconic aciduria.
Saunders C, Smith L, Wibrand F, Ravn K, Bross P, Thiffault I, Christensen M, Atherton A, Farrow E, Miller N, Kingsmore SF, Ostergaard E., Free PMC Article | 04/11/2015 |
| Mutations in CLPB define a syndrome with intellectual disability, congenital neutropenia, progressive brain atrophy, movement disorder, cataracts, and 3-methylglutaconic aciduria. | CLPB mutations cause 3-methylglutaconic aciduria, progressive brain atrophy, intellectual disability, congenital neutropenia, cataracts, movement disorder.
Wortmann SB, Ziętkiewicz S, Kousi M, Szklarczyk R, Haack TB, Gersting SW, Muntau AC, Rakovic A, Renkema GH, Rodenburg RJ, Strom TM, Meitinger T, Rubio-Gozalbo ME, Chrusciel E, Distelmaier F, Golzio C, Jansen JH, van Karnebeek C, Lillquist Y, Lücke T, Õunap K, Zordania R, Yaplito-Lee J, van Bokhoven H, Spelbrink JN, Vaz FM, Pras-Raves M, Ploski R, Pronicka E, Klein C, Willemsen MA, de Brouwer AP, Prokisch H, Katsanis N, Wevers RA., Free PMC Article | 04/11/2015 |
| Observational study of gene-disease association. (HuGE Navigator) | Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression.
Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O'Brien SJ., Free PMC Article | 12/5/2010 |
| formation of the DnaK-ClpB bichaperone network is a three step process | DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface.
Acebrón SP, Martín I, del Castillo U, Moro F, Muga A. | 01/21/2010 |
| ClpB-DnaK reactivated all aggregated fusion proteins with similar efficiency, without unfolding native domains, demonstrating that partial threading of the misfolded moiety is sufficient to solubilize aggregates. | Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments.
Haslberger T, Zdanowicz A, Brand I, Kirstein J, Turgay K, Mogk A, Bukau B. | 01/21/2010 |