Structural basis of impaired disaggregase function in the oxidation-sensitive SKD3 mutant causing 3-methylglutaconic aciduria

[1]  Yan Liu,et al.  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 , 2023, PLoS biology.

[2]  Sukyeong Lee,et al.  Deciphering the mechanism and function of Hsp100 unfoldases from protein structure. , 2022, Biochemical Society transactions.

[3]  A. Sinclair,et al.  Premature Ovarian Insufficiency in CLPB Deficiency: Transcriptomic, Proteomic and Phenotypic Insights , 2022, The Journal of clinical endocrinology and metabolism.

[4]  C. Klein,et al.  HAX1-dependent control of mitochondrial proteostasis governs neutrophil granulocyte differentiation , 2022, The Journal of clinical investigation.

[5]  J. Shorter,et al.  Unique structural features govern the activity of a human mitochondrial AAA+ disaggregase, Skd3 , 2022, bioRxiv.

[6]  M. Zółkiewski,et al.  Human mitochondrial AAA+ ATPase SKD3/CLPB assembles into nucleotide-stabilized dodecamers. , 2022, Biochemical and biophysical research communications.

[7]  D. Spencer,et al.  Heterozygous Variants of CLPB are a Cause of Severe Congenital Neutropenia. , 2021, Blood.

[8]  I. Lindberg,et al.  A protease protection assay for the detection of internalized alpha-synuclein pre-formed fibrils , 2020, bioRxiv.

[9]  M. Zółkiewski,et al.  Human CLPB forms ATP-dependent complexes in the mitochondrial intermembrane space. , 2020, The international journal of biochemistry & cell biology.

[10]  Haiguang Liu,et al.  Prediction of disulfide bond engineering sites using a machine learning method , 2020, Scientific Reports.

[11]  J. Shorter,et al.  Skd3 (human ClpB) is a potent mitochondrial protein disaggregase that is inactivated by 3-methylglutaconic aciduria-linked mutations , 2020, bioRxiv.

[12]  R. Wevers,et al.  CLPB (caseinolytic peptidase B homolog), the first mitochondrial protein refoldase associated with human disease. , 2020, Biochimica et biophysica acta. General subjects.

[13]  A. Wlodawer,et al.  Cryo-EM structure of substrate-free E. coli Lon protease provides insights into the dynamics of Lon machinery , 2019, Current research in structural biology.

[14]  Zev A. Ripstein,et al.  A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery , 2019, bioRxiv.

[15]  H. Kosako,et al.  Structural Basis of Mitochondrial Scaffolds by Prohibitin Complexes: Insight into a Role of the Coiled-Coil Region , 2019, iScience.

[16]  T. Sakellaropoulos,et al.  Targeting Mitochondrial Structure Sensitizes Acute Myeloid Leukemia to Venetoclax Treatment. , 2019, Cancer discovery.

[17]  S. Sieber,et al.  Cryo-EM structure of the ClpXP protein degradation machinery , 2019, Nature Structural & Molecular Biology.

[18]  Jun Liu,et al.  Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation , 2019, Cell reports.

[19]  Gwyndaf Evans,et al.  DIALS: implementation and evaluation of a new integration package , 2018, Acta crystallographica. Section D, Structural biology.

[20]  Zhiyi Wei,et al.  Structural insights into ankyrin repeat–mediated recognition of the kinesin motor protein KIF21A by KANK1, a scaffold protein in focal adhesion , 2017, The Journal of Biological Chemistry.

[21]  C. Hryc,et al.  Overlapping and Specific Functions of the Hsp104 N Domain Define Its Role in Protein Disaggregation , 2017, Scientific Reports.

[22]  Kamila B. Franke,et al.  Regulatory coiled-coil domains promote head-to-head assemblies of AAA+ chaperones essential for tunable activity control , 2017, bioRxiv.

[23]  C. Saunders,et al.  A scoring system predicting the clinical course of CLPB defect based on the foetal and neonatal presentation of 31 patients , 2017, Journal of Inherited Metabolic Disease.

[24]  T. Langer,et al.  PARL mediates Smac proteolytic maturation in mitochondria to promote apoptosis , 2017, Nature Cell Biology.

[25]  E. Kıykım,et al.  Novel CLPB mutation in a patient with 3-methylglutaconic aciduria causing severe neurological involvement and congenital neutropenia. , 2016, Clinical immunology.

[26]  Laurie D. Smith,et al.  CLPB variants associated with autosomal-recessive mitochondrial disorder with cataract, neutropenia, epilepsy, and methylglutaconic aciduria. , 2015, American journal of human genetics.

[27]  T. Meitinger,et al.  CLPB mutations cause 3-methylglutaconic aciduria, progressive brain atrophy, intellectual disability, congenital neutropenia, cataracts, movement disorder. , 2015, American journal of human genetics.

[28]  C. Fallet-Bianco,et al.  Disruption of CLPB is associated with congenital microcephaly, severe encephalopathy and 3-methylglutaconic aciduria , 2015, Journal of Medical Genetics.

[29]  V. Plagnol,et al.  Bi-allelic CLPB mutations cause cataract, renal cysts, nephrocalcinosis and 3-methylglutaconic aciduria, a novel disorder of mitochondrial protein disaggregation , 2015, Journal of Inherited Metabolic Disease.

[30]  S. Carr,et al.  Proteomic mapping of the human mitochondrial intermembrane space in live cells via ratiometric APEX tagging. , 2014, Molecular cell.

[31]  Xavier Robert,et al.  Deciphering key features in protein structures with the new ENDscript server , 2014, Nucleic Acids Res..

[32]  T. Baker,et al.  Distinct quaternary structures of the AAA+ Lon protease control substrate degradation , 2013, Proceedings of the National Academy of Sciences.

[33]  Ji-Hyun Kim,et al.  Heat shock protein (Hsp) 70 is an activator of the Hsp104 motor , 2013, Proceedings of the National Academy of Sciences.

[34]  P. Emsley,et al.  Features and development of Coot , 2010, Acta crystallographica. Section D, Biological crystallography.

[35]  Randy J. Read,et al.  Acta Crystallographica Section D Biological , 2003 .

[36]  Lixue Dong,et al.  The Redox Environment in the Mitochondrial Intermembrane Space Is Maintained Separately from the Cytosol and Matrix* , 2008, Journal of Biological Chemistry.

[37]  R. Gaudet A primer on ankyrin repeat function in TRP channels and beyond. , 2008, Molecular bioSystems.

[38]  Bengt Fadeel,et al.  HAX1 deficiency causes autosomal recessive severe congenital neutropenia (Kostmann disease) , 2007, Nature Genetics.

[39]  Wladek Minor,et al.  HKL-3000: the integration of data reduction and structure solution--from diffraction images to an initial model in minutes. , 2006, Acta crystallographica. Section D, Biological crystallography.

[40]  Zbyszek Otwinowski,et al.  The integration of data reduction and structure solution - from diffraction images to an initial model in minutes , 2005 .