Affinage

HSD17B10

3-hydroxyacyl-CoA dehydrogenase type-2 · UniProt Q99714

Length
261 aa
Mass
26.9 kDa
Annotated
2026-06-10
59 papers in source corpus 19 papers cited in narrative 19 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 7/7 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

HSD17B10 (ABAD/ERAB/SDR5C1/MRPP2) is a mitochondrial short-chain dehydrogenase/reductase that operates as a moonlighting enzyme bridging mitochondrial metabolism and tRNA maturation (PMID:9890977, PMID:22127393). As a metabolic enzyme it adopts a Rossmann-fold and catalyzes NAD(H)-dependent reactions including reduction of S-acetoacetyl-CoA, oxidation of 3-hydroxyacyl-CoA derivatives, oxidation of 17β-estradiol, and broad-spectrum alcohol dehydrogenase activity, with ketobutyrate binding triggering closure of an active-site specificity loop (PMID:9890977, PMID:11023795). In isoleucine catabolism it performs the 2-methyl-3-hydroxybutyryl-CoA dehydrogenation step and also inactivates GABAA-modulating neuroactive steroids such as allopregnanolone (PMID:17618155, PMID:19706438). Independently of its catalytic activity, HSD17B10 is an essential homotetrameric subunit of mitochondrial RNase P, where together with TRMT10C/MRPP1 it enables 5'-end processing of mitochondrial tRNA precursors and N1-methylation of purines at tRNA position 9 (PMID:22127393, PMID:25925575). Both functions are tuned post-translationally: SIRT3 deacetylates K79/K99/K105 (acetylated by CBP) and CPT1A succinylates K99 to regulate dehydrogenase activity and RNase P complex assembly (PMID:32703935, PMID:39038923). Pathogenic missense mutations causing X-linked HSD10 disease impair these activities through distinct mechanisms—loss of dehydrogenase/MHBD activity, disrupted homotetramerization, reduced stability, or impaired TRMT10C binding and tRNA maturation—establishing that either metabolic or RNase P dysfunction can drive the neurological phenotype (PMID:19706438, PMID:25925575, PMID:26950678, PMID:28888424). HSD17B10 also binds Aβ peptide via a hydrophobically-driven interaction (KD ~21 nM) that is mutually exclusive with NAD+, distorts the enzyme, and potentiates Aβ-induced mitochondrial oxidant stress, cytochrome c release, and selective complex IV deficiency (PMID:11023795, PMID:15665036, PMID:17253767); controlled in vitro work establishes that Aβ inhibition of RNase P is not SDR5C1-specific and therefore does not account for this toxicity (PMID:23755257).

Mechanistic history

Synthesis pass · year-by-year structured walk · 18 steps
  1. 1999 High

    Established that HSD17B10 is a catalytically active NAD(H)-dependent dehydrogenase and that this enzymatic activity is mechanistically required for Aβ-induced cytotoxicity, linking an enzyme to neurodegenerative cell death.

    Evidence In vitro enzyme kinetics with recombinant protein, active-site mutagenesis (Y168G/K172G), and cell transfection cytotoxicity assays

    PMID:9890977

    Open questions at the time
    • Did not resolve which physiological substrate mediates toxicity
    • Mechanism connecting catalysis to lipid peroxidation adducts left undefined
  2. 1999 High

    Defined the kinetic mode of Aβ inhibition of HSD17B10 and the Aβ region required, framing the enzyme as a direct intracellular Aβ target.

    Evidence In vitro enzyme inhibition kinetics with 3-hydroxybutyryl-CoA, Aβ peptide fragment analysis, and subcellular fractionation

    PMID:10371197

    Open questions at the time
    • ER vs mitochondrial localization not reconciled with later mitochondrial assignment
    • Structural basis of Aβ binding not yet defined
  3. 2000 High

    Solved the catalytic architecture, showing a Rossmann-fold dehydrogenase with a substrate-specificity loop and quantifying high-affinity Aβ binding, providing structural mechanism for cofactor and substrate handling.

    Evidence X-ray crystallography of binary and ternary complexes (NADH, NAD+/3-ketobutyrate, NADH/17β-estradiol) plus in vitro Aβ binding

    PMID:11023795

    Open questions at the time
    • Aβ binding site not mapped on the structure
    • Human enzyme structure not yet determined here (rat ortholog)
  4. 2000 Medium

    Ruled out quinone redox cycling as the source of Aβ-ABAD-induced lipid peroxidation, narrowing candidate toxicity mechanisms.

    Evidence In vitro orthoquinone reductase assays with recombinant human ERAB +/- Aβ

    PMID:10781884

    Open questions at the time
    • Negative result does not identify the actual oxidant-generating mechanism
    • Single lab in vitro assay
  5. 2004 High

    Demonstrated a druggable active site by capturing an inhibitor forming a covalent adduct with the NAD+ cofactor in the human enzyme, establishing a structural strategy to block activity.

    Evidence X-ray crystallography of human ABAD with NAD+ and a small-molecule inhibitor

    PMID:15342248

    Open questions at the time
    • Cellular efficacy of inhibitor not addressed in this structural study
    • Selectivity over other SDRs not established
  6. 2005 High

    Provided in vivo genetic proof that ABAD acts as a cofactor converting Aβ into mitochondrial dysfunction, including selective complex IV loss.

    Evidence Double vs single transgenic mouse epistasis (mAPP/ABAD), ROS, COX activity, ATP, cytochrome c release, caspase-3 assays

    PMID:15665036

    Open questions at the time
    • Molecular cause of selective complex IV vulnerability not defined
    • Did not distinguish loss of enzyme function from gain of toxic complex
  7. 2007 High

    Resolved the thermodynamics and exclusivity of Aβ binding, showing hydrophobically-driven Aβ association is mutually exclusive with NAD+, defining a competitive inactivation mechanism.

    Evidence Surface plasmon resonance thermodynamics and saturation transfer difference NMR

    PMID:17253767

    Open questions at the time
    • Atomic-resolution Aβ-bound structure still lacking
    • Quantitative contribution of conformational distortion to toxicity unquantified
  8. 2007 Medium

    Connected HSD17B10 metabolic functions—isoleucine catabolism and neurosteroid inactivation—to X-linked mental retardation/HSD10 deficiency, broadening its physiological remit beyond Alzheimer biology.

    Evidence Enzyme activity assays on patient-derived samples and molecular genetic analysis

    PMID:17618155

    Open questions at the time
    • Relative contribution of each metabolic function to disease unresolved
    • Compilation-style evidence rather than single reconstitution
  9. 2009 High

    Showed a disease mutation can disrupt subunit interactions and confer allosteric kinetics, implicating neurosteroid metabolic failure rather than isoleucine catabolism alone in pathology.

    Evidence Recombinant E249Q mutant kinetics (Hill coefficient ~1.3) versus wild-type

    PMID:19706438

    Open questions at the time
    • In vivo neurosteroid levels in patients not measured here
    • Generalizability to other mutations not tested
  10. 2011 Medium

    Established a wholly distinct, non-metabolic role for HSD17B10 as an essential subunit of mitochondrial RNase P, coupling it to tRNA 5'-processing and position-9 methylation.

    Evidence Biochemical characterization of the mitochondrial RNase P complex and tRNA processing assays

    PMID:22127393

    Open questions at the time
    • Catalytic vs structural contribution of HSD17B10 to RNase P not separated
    • Stoichiometry within the complex not defined here
  11. 2011 Medium

    Provided loss-of-function evidence that ABAD upregulation is required for stress-induced mitochondrial dysfunction under Aβ pathology, linking glucocorticoid stress to the ABAD-Aβ axis.

    Evidence siRNA knockdown in SH-SY5Y cells, ROS and mitochondrial dysfunction assays, plus Tg-APPswe/PS1dE9 mouse model

    PMID:21382475

    Open questions at the time
    • Transcriptional mechanism of stress-induced ABAD upregulation unknown
    • Single cell line for knockdown
  12. 2011 Medium

    Showed a small-molecule disruptor of the Aβ-ABAD interaction rescues mitochondrial respiration and estradiol homeostasis, supporting enzymatic activity as a therapeutic node in Aβ toxicity.

    Evidence Pull-down, estradiol-based enzyme activity readout, mitochondrial respiration, ROS, and viability assays with AG18051

    PMID:22174920

    Open questions at the time
    • Only partial blockade of interaction achieved
    • In vivo efficacy not tested; single lab
  13. 2013 High

    Demonstrated that Aβ inhibition of the SDR5C1-containing RNase P is non-specific, excluding RNase P inhibition as the mechanism of Aβ mitochondrial toxicity.

    Evidence In vitro RNase P and methyltransferase assays comparing SDR5C1-containing and non-SDR5C1 complexes with Aβ titration

    PMID:23755257

    Open questions at the time
    • Does not identify the bona fide Aβ target for mitochondrial dysfunction
    • Confined to in vitro reconstituted activities
  14. 2015 High

    Unified the disease mechanism by showing pathogenic mutations simultaneously impair dehydrogenase activity, RNase P tRNA processing, methylation, homotetramerization, and TRMT10C interaction.

    Evidence Recombinant mutant proteins with dehydrogenase, tRNA processing, methyltransferase, and protein interaction assays

    PMID:25925575

    Open questions at the time
    • Which deficit dominates clinically per mutation not resolved
    • Structural basis of disrupted tetramerization not shown
  15. 2016 High

    Dissociated the two functions in vivo by identifying a mutation (K212E) that impairs RNase P activities while sparing dehydrogenase/MHBD function, proving tRNA maturation defects alone can be pathogenic.

    Evidence In vitro tRNA processing and methylation assays with recombinant K212E and patient exome sequencing

    PMID:26950678

    Open questions at the time
    • How a single residue selectively affects RNase P but not catalysis structurally unexplained
    • Single patient
  16. 2017 High

    Defined two distinct molecular routes to pathogenicity—protein destabilization versus impaired kinetics and complex formation—for additional patient mutations.

    Evidence Recombinant V12L and V176M mutant kinetics, tRNA processing/methylation, stability, and MRPP1 complex formation assays

    PMID:28888424

    Open questions at the time
    • In vivo consequences of each mechanism not measured
    • Limited to two mutations
  17. 2020 Medium

    Revealed post-translational acetylation control of HSD17B10, with CBP and SIRT3 setting K79/K99/K105 acetylation to regulate both dehydrogenase activity and RNase P assembly and stress resistance.

    Evidence Co-IP, mass spectrometry site mapping, site-directed mutagenesis, in vitro activity, and cell-based stress assays

    PMID:32703935

    Open questions at the time
    • Physiological stimuli driving acetylation changes not defined
    • Single lab; in vivo relevance untested
  18. 2024 Medium

    Added a second PTM layer by showing CPT1A-mediated K99 succinylation maintains RNase P (MRPP1) stability and protects against oxidative stress in tubular epithelial cells.

    Evidence Succinyl-proteomics, docking, thermal shift, MD simulation, K99R mutagenesis, Co-IP, RNase P activity, and mouse model

    PMID:39038923

    Open questions at the time
    • Interplay between K99 acetylation and succinylation unresolved
    • Single lab; mechanism of CPT1A targeting to HSD17B10 unclear

Open questions

Synthesis pass · forward-looking unresolved questions
  • The bona fide intracellular substrate and molecular event by which Aβ binding to HSD17B10 selectively impairs complex IV and drives oxidant stress remains unidentified.
  • RNase P inhibition excluded as the toxic mechanism
  • No atomic-resolution Aβ-bound HSD17B10 structure
  • Causal substrate linking catalysis to mitochondrial damage undefined

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0016491 oxidoreductase activity 4 GO:0003723 RNA binding 2 GO:0140098 catalytic activity, acting on RNA 2
Localization
GO:0005739 mitochondrion 3
Pathway
R-HSA-1430728 Metabolism 3 R-HSA-1643685 Disease 2 R-HSA-8953854 Metabolism of RNA 2
Partners
CBPCPT1ASIRT3TRMT10C
Complex memberships
mitochondrial RNase P

Evidence

Reading pass · 19 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1999 ERAB/HSD17B10 (HADH II) catalyzes NADH-dependent reduction of S-acetoacetyl-CoA (Km ~68 µM, Vmax ~430 µmol/min/mg), oxidation of 17β-estradiol, and oxidation of a variety of simple alcohols (C2–C10) in the presence of NAD+. Active-site mutagenesis (Y168G/K172G) abolished both enzymatic activity and Aβ-mediated cytotoxicity and prevented generation of malondialdehyde-protein and 4-hydroxynonenal adducts, establishing that the generalized alcohol dehydrogenase activity is required for Aβ-induced cell death. In vitro enzyme kinetics with purified recombinant protein; site-directed mutagenesis of catalytic domain; cell transfection assay The Journal of biological chemistry High 9890977
1999 Aβ peptide inhibits ERAB/HSD17B10 hydroxyacyl-CoA dehydrogenase activity in a mixed-type fashion (Ki ~1.2 µM using 3-hydroxybutyryl-CoA as substrate; KiES ~0.3 µM). The region of Aβ comprising residues 12–24 is required for inhibition. ERAB is localized to endoplasmic reticulum and mitochondria. In vitro enzyme inhibition kinetics with recombinant ERAB; peptide fragment analysis; subcellular fractionation/localization FEBS letters High 10371197
2000 Crystal structures of rat HADH II/ABAD were determined as: (1) binary complex with NADH at 2.0 Å, (2) ternary complex with NAD+ and 3-ketobutyrate at 1.4 Å, and (3) ternary complex with NADH and 17β-estradiol at 1.7 Å. The enzyme is a short-chain hydroxysteroid dehydrogenase with a Rossman fold. Ketobutyrate binding triggers closure of the active-site specificity loop; steroid substrate does not require loop closure. Rat HADH II/ABAD binds Aβ(1-40) with KD ~21 nM. X-ray crystallography; in vitro binding assay Journal of molecular biology High 11023795
2004 Crystal structure of human ABAD/HSD10 complexed with NAD+ and a small-molecule inhibitor revealed that the inhibitor occupies the substrate-binding site and forms a covalent adduct with the NAD+ cofactor, thereby blocking enzymatic activity. X-ray crystallography Journal of molecular biology High 15342248
2005 In neurons from transgenic mice overexpressing both mutant APP and ABAD (Tg mAPP/ABAD), ABAD potentiates Aβ-induced mitochondrial dysfunction: spontaneous generation of H2O2 and superoxide, decreased ATP, cytochrome c release, caspase-3 activation, DNA fragmentation, and selective reduction of mitochondrial complex IV (cytochrome c oxidase, COX) activity. These changes were not present in Tg ABAD or Tg mAPP single-transgenic mice, establishing ABAD as a cofactor linking Aβ to mitochondrial oxidant stress. Transgenic mouse model (double vs single transgenic genetic epistasis); ROS assays; COX activity measurement; ATP quantification; cytochrome c release assay; caspase activity assay FASEB journal High 15665036
2007 Surface plasmon resonance thermodynamic analysis showed that ABAD–Aβ association is driven by a favorable entropic change (ΔS = 300 ± 30 J mol−1 K−1) overcoming an unfavorable enthalpy (ΔH = 49 ± 7 kJ/mol), indicating hydrophobic interactions dominate. Saturation transfer difference NMR directly demonstrated that Aβ binding inhibits ABAD–NAD interaction, and conversely NAD inhibits Aβ binding, establishing that Aβ and NAD binding to ABAD are mutually exclusive. Aβ binding induces conformational changes in ABAD. Surface plasmon resonance (SPR) thermodynamic analysis; saturation transfer difference (STD) NMR Biochemistry High 17253767
2007 HSD17B10 encodes a mitochondrial multifunctional enzyme (HSD10) that catalyzes the 2-methyl-3-hydroxybutyryl-CoA dehydrogenation step in isoleucine catabolism and inactivates positive modulators of GABAA receptors (neuroactive steroids such as allopregnanolone). Missense mutations causing X-linked mental retardation and HSD10 deficiency impair these enzymatic functions. Enzyme activity assays on patient-derived samples; molecular genetic analysis Molecular genetics and metabolism Medium 17618155
2009 The HSD10 E249Q mutation impairs subunit interactions, yielding allosteric enzyme kinetics (Hill coefficient ~1.3 for allopregnanolone oxidation). HSD10(E249Q) fails to catalyze dehydrogenation of 2-methyl-3-hydroxybutyryl-CoA and oxidation of allopregnanolone at low substrate concentrations, linking neurosteroid metabolic dysfunction—not isoleucine catabolism alone—to the neurological phenotype. Recombinant mutant protein expression; enzyme kinetics; comparison with wild-type activity Proceedings of the National Academy of Sciences of the United States of America High 19706438
2011 HSD17B10 is an essential component of the mitochondrial RNase P complex, which removes 5'-extensions from mitochondrial tRNA precursors (tRNA processing). It also participates in the RNase P subcomplex that catalyzes N1-methylation of purines at position 9 of mitochondrial tRNAs. Biochemical characterization of the mitochondrial RNase P complex; tRNA processing assays Journal of inherited metabolic disease Medium 22127393
2011 The AG18051 small-molecule inhibitor partially blocks the Aβ–ABAD interaction (pull-down assay), prevents Aβ42-induced downregulation of ABAD's estradiol-producing activity (used as a functional readout), reduces Aβ42-induced mitochondrial respiration impairment, and reduces ROS, establishing that ABAD enzymatic activity contributes to Aβ toxicity through disruption of estradiol homeostasis in neurons. Pull-down assay; ABAD enzyme activity assay (estradiol measurement); mitochondrial respiration assay; ROS measurement; cell viability assays PloS one Medium 22174920
2013 Negative finding: Micromolar concentrations of monomeric or oligomerized Aβ inhibit mitochondrial tRNA 5'-end processing and position-9 methylation by the SDR5C1 (HSD17B10)-containing RNase P complex, but the same concentrations also inhibit related RNase P and methyltransferase activities that do NOT contain an SDR5C1 homolog. Therefore, the deleterious effect of Aβ on mitochondrial function cannot be explained by specific inhibition of the mitochondrial RNase P or its tRNA:m1R9 methyltransferase subcomplex via SDR5C1. In vitro RNase P and methyltransferase activity assays with recombinant components and Aβ titration PloS one High 23755257
2015 Pathogenic missense mutations in SDR5C1/HSD17B10 (HSD10 disease mutations) impair: (1) SDR5C1-dependent dehydrogenase activity, (2) mitochondrial tRNA 5'-end processing by the RNase P complex, and (3) N1-methylation of purines at tRNA position 9. Some mutations disrupt SDR5C1 homotetramerization and/or impair its interaction with TRMT10C (the methyltransferase subunit of mitochondrial RNase P). Recombinant mutant protein expression and biochemical characterization; tRNA processing assays; methyltransferase assays; protein–protein interaction assays Nucleic acids research High 25925575
2016 A novel p.K212E mutation in HSD17B10 impairs SDR5C1-dependent mitochondrial RNase P activities (tRNA 5'-processing and position-9 methylation), but does not abolish dehydrogenase activity or MHBD function, indicating that pathogenicity in this case is due to impaired mitochondrial tRNA maturation rather than metabolic enzyme deficiency. In vitro tRNA processing and methylation assays with recombinant mutant protein; patient exome sequencing RNA biology High 26950678
2017 Two novel patient mutations (p.V12L and p.V176M) in HSD17B10 reduce dehydrogenase activity, mitochondrial tRNA methyltransferase activity, and tRNA 5'-processing activity in vitro. p.V12L reduces protein stability; p.V176M impairs kinetics and TRMT10C/MRPP1 complex formation, revealing two distinct molecular mechanisms for pathogenic mutations. Recombinant mutant protein expression; enzyme kinetics; tRNA processing and methylation assays; protein stability and complex formation assays Biochimica et biophysica acta. Molecular basis of disease High 28888424
2020 HSD17B10 is acetylated at K79, K99, and K105 by the acetyltransferase CBP, and deacetylated by SIRT3. Acetylation of HSD17B10 regulates its dehydrogenase enzymatic activity and the formation of the mitochondrial RNase P complex. HSD17B10 acetylation state also affects cell growth and cell resistance under oxidative and starvation stress conditions. Co-IP; mass spectrometry identification of acetylation sites; site-directed mutagenesis; in vitro enzyme activity assay; cell-based functional assays Cell death & disease Medium 32703935
2024 HSD17B10 is succinylated at K99 by CPT1A. K99 succinylation maintains mitochondrial RNase P (MRPP1 complex) stability, and the K99R mutation disrupts HSD17B10 binding to CPT1A and MRPP1, impairs RNase P activity, and induces oxidative stress. ASIV restores CPT1A activity and K99 succinylation of HSD17B10, thereby preserving RNase P function in tubular epithelial cells. Succinylated proteomics; molecular docking; cell thermal shift assay; molecular dynamics simulation; site-directed mutagenesis (K99R); Co-IP; in vitro RNase P activity assay; in vivo mouse model Phytotherapy research : PTR Medium 39038923
2000 Negative finding: Recombinant human ERAB/HSD17B10 showed no quinone reductase activity against several orthoquinones, with or without Aβ, indicating that Aβ-ERAB-induced lipid peroxidation observed in vivo is not mediated by quinone redox cycling. In vitro enzyme assay with recombinant human ERAB and orthoquinone substrates Toxicology Medium 10781884
1998 ERAB/HSD17B10 contains a putative signal peptide sequence (identified by computational and comparative analysis across human, rodent, and bovine sequences) suggesting it is a type II integral membrane protein in vertebrates, potentially explaining its localization in secretory organelles and ability to bind Aβ. Computational sequence analysis; comparative vertebrate analysis Biochemical and biophysical research communications Low 9712734
2011 Behavioral stress (restraint) upregulates ABAD expression in mitochondria of the brain of Tg-APPswe/PS1dE9 mice. Knockdown of ABAD by siRNA in SH-SY5Y cells suppresses glucocorticoid-enhanced mitochondrial dysfunction and ROS accumulation, establishing that ABAD upregulation is required for stress-induced mitochondrial dysfunction in the context of Aβ pathology. siRNA knockdown; mitochondrial dysfunction assays; ROS measurement; transgenic mouse model Free radical biology & medicine Medium 21382475

Source papers

Stage 0 corpus · 59 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2005 ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 227 15665036
2008 Submicroscopic duplications of the hydroxysteroid dehydrogenase HSD17B10 and the E3 ubiquitin ligase HUWE1 are associated with mental retardation. American journal of human genetics 178 18252223
2005 Mitochondrial dysfunction and Alzheimer's disease: role of amyloid-beta peptide alcohol dehydrogenase (ABAD). International journal of experimental pathology 111 15910550
1999 Role of ERAB/L-3-hydroxyacyl-coenzyme A dehydrogenase type II activity in Abeta-induced cytotoxicity. The Journal of biological chemistry 100 9890977
2000 Recognition of structurally diverse substrates by type II 3-hydroxyacyl-CoA dehydrogenase (HADH II)/amyloid-beta binding alcohol dehydrogenase (ABAD). Journal of molecular biology 87 11023795
2004 Crystal structure of human ABAD/HSD10 with a bound inhibitor: implications for design of Alzheimer's disease therapeutics. Journal of molecular biology 86 15342248
1999 Binding of amyloid beta-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease. FEBS letters 83 10371197
2011 HSD10 disease: clinical consequences of mutations in the HSD17B10 gene. Journal of inherited metabolic disease 68 22127393
2012 Structure-based design and synthesis of benzothiazole phosphonate analogues with inhibitors of human ABAD-Aβ for treatment of Alzheimer's disease. Chemical biology & drug design 61 23039767
2007 Surface plasmon resonance and nuclear magnetic resonance studies of ABAD-Abeta interaction. Biochemistry 59 17253767
2007 HSD17B10: a gene involved in cognitive function through metabolism of isoleucine and neuroactive steroids. Molecular genetics and metabolism 58 17618155
2015 Molecular insights into HSD10 disease: impact of SDR5C1 mutations on the human mitochondrial RNase P complex. Nucleic acids research 54 25925575
2018 Amyloid-Binding Alcohol Dehydrogenase (ABAD) Inhibitors for the Treatment of Alzheimer's Disease. Journal of medicinal chemistry 49 30444369
2011 Inhibition of the mitochondrial enzyme ABAD restores the amyloid-β-mediated deregulation of estradiol. PloS one 49 22174920
2005 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) deficiency: an X-linked inborn error of isoleucine metabolism that may mimic a mitochondrial disease. Pediatric research 43 16148061
2014 Identification of human ABAD inhibitors for rescuing Aβ-mediated mitochondrial dysfunction. Current Alzheimer research 42 24479630
2009 Mental retardation linked to mutations in the HSD17B10 gene interfering with neurosteroid and isoleucine metabolism. Proceedings of the National Academy of Sciences of the United States of America 42 19706438
2016 A novel HSD17B10 mutation impairing the activities of the mitochondrial RNase P complex causes X-linked intractable epilepsy and neurodevelopmental regression. RNA biology 40 26950678
2017 Novel patient missense mutations in the HSD17B10 gene affect dehydrogenase and mitochondrial tRNA modification functions of the encoded protein. Biochimica et biophysica acta. Molecular basis of disease 38 28888424
2015 Methylene Blue Improves Brain Mitochondrial ABAD Functions and Decreases Aβ in a Neuroinflammatory Alzheimer's Disease Mouse Model. Molecular neurobiology 38 25601181
2009 Molecular characterization of the response to chemotherapy in conventional osteosarcomas: predictive value of HSD17B10 and IFITM2. International journal of cancer 38 19449377
2016 Synthesis and evaluation of frentizole-based indolyl thiourea analogues as MAO/ABAD inhibitors for Alzheimer's disease treatment. Bioorganic & medicinal chemistry 36 28082069
2011 Behavioral stress causes mitochondrial dysfunction via ABAD up-regulation and aggravates plaque pathology in the brain of a mouse model of Alzheimer disease. Free radical biology & medicine 36 21382475
2001 Deposition of Alzheimer's vascular amyloid-beta is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB). Brain research 34 11430884
2008 Study of patients and carriers with 2-methyl-3-hydroxybutyryl-CoA dehydrogenase (MHBD) deficiency: difficulties in the diagnosis. Clinical biochemistry 31 18996107
2014 Molecular docking of fisetin with AD associated AChE, ABAD and BACE1 proteins. Bioinformation 29 25352723
2019 ABAD/17β-HSD10 reduction contributes to the protective mechanism of huperzine a on the cerebral mitochondrial function in APP/PS1 mice. Neurobiology of aging 27 31252207
2016 Design, synthesis and in vitro evaluation of benzothiazole-based ureas as potential ABAD/17β-HSD10 modulators for Alzheimer's disease treatment. Bioorganic & medicinal chemistry letters 26 27287370
2013 The serological study of cystic echinococcosis and assessment of surgical cases during 5 years (2007-2011) in Khorram Abad, Iran. Nigerian journal of clinical practice 25 23563466
2018 1-(Benzo[d]thiazol-2-yl)-3-phenylureas as dual inhibitors of casein kinase 1 and ABAD enzymes for treatment of neurodegenerative disorders. Journal of enzyme inhibition and medicinal chemistry 24 29536773
2011 A novel mutation in the HSD17B10 gene of a 10-year-old boy with refractory epilepsy, choreoathetosis and learning disability. PloS one 22 22132097
2006 Comparative evolutionary genomics of the HADH2 gene encoding Abeta-binding alcohol dehydrogenase/17beta-hydroxysteroid dehydrogenase type 10 (ABAD/HSD10). BMC genomics 21 16899120
2017 In Vitro Assay Development and HTS of Small-Molecule Human ABAD/17β-HSD10 Inhibitors as Therapeutics in Alzheimer's Disease. SLAS discovery : advancing life sciences R & D 18 28314118
2020 Deacetylation of HSD17B10 by SIRT3 regulates cell growth and cell resistance under oxidative and starvation stresses. Cell death & disease 17 32703935
2017 6-benzothiazolyl ureas, thioureas and guanidines are potent inhibitors of ABAD/17β-HSD10 and potential drugs for Alzheimer's disease treatment: Design, synthesis and in vitro evaluation. Medicinal chemistry (Shariqah (United Arab Emirates)) 17 28067167
2024 Astragaloside IV protects renal tubular epithelial cells against oxidative stress-induced injury by upregulating CPT1A-mediated HSD17B10 lysine succinylation in diabetic kidney disease. Phytotherapy research : PTR 14 39038923
2017 Clinical and molecular analysis of 6 Chinese patients with isoleucine metabolism defects: identification of 3 novel mutations in the HSD17B10 and ACAT1 gene. Metabolic brain disease 12 28875337
1998 The gene for the Alzheimer-associated beta-amyloid-binding protein (ERAB) is differentially expressed in the testicular Leydig cells of the azoospermic by w/w(v) mouse. European journal of biochemistry 12 9851691
2012 A 5-methylcytosine hotspot responsible for the prevalent HSD17B10 mutation. Gene 10 23266819
2010 X-inactivation of HSD17B10 revealed by cDNA analysis in two female patients with 17β-hydroxysteroid dehydrogenase 10 deficiency. European journal of human genetics : EJHG 10 20664630
2009 ABAD: a potential therapeutic target for Abeta-induced mitochondrial dysfunction in Alzheimer's disease. Mini reviews in medicinal chemistry 10 19601895
2008 Molecular dynamics simulations of the amyloid-beta binding alcohol dehydrogenase (ABAD) enzyme. Bioorganic & medicinal chemistry 10 18835182
1998 ERAB contains a putative noncleavable signal peptide. Biochemical and biophysical research communications 10 9712734
2007 Stable expression of a novel fusion peptide of thioredoxin-1 and ABAD-inhibiting peptide protects PC12 cells from intracellular amyloid-beta. Journal of molecular neuroscience : MN 9 17917077
2017 In silico-designed novel non-peptidic ABAD LD hot spot mimetics reverse Aβ-induced mitochondrial impairments in vitro. Chemical biology & drug design 8 28660722
2013 The amyloid-β-SDR5C1(ABAD) interaction does not mediate a specific inhibition of mitochondrial RNase P. PloS one 8 23755257
2013 Transcription start sites and epigenetic analysis of the HSD17B10 proximal promoter. BMC biochemistry 8 23834306
2020 Xp11.22 duplications in four unrelated Chinese families: delineating the genotype-phenotype relationship for HSD17B10 and FGD1. BMC medical genomics 7 32381089
2025 Peptide-loaded chitosan nanoparticles improve mitochondrial and cognitive functions via inhibition of Aβ-ABAD interaction in Alzheimer's disease. European journal of pharmaceutics and biopharmaceutics : official journal of Arbeitsgemeinschaft fur Pharmazeutische Verfahrenstechnik e.V 5 40484144
2024 Novel Mutation in the HSD17B10 Gene Accompanied by Dysmorphic Findings in Female Patients. Molecular syndromology 4 38841322
2000 Lack of quinone reductase activity suggests that amyloid-beta peptide/ERAB induced lipid peroxidation is not directly related to production of reactive oxygen species by redoxcycling. Toxicology 4 10781884
2025 A novel c.59 C > T variant of the HSD17B10 gene as a possible cause of the neonatal form of HSD10 mitochondrial disease with hepatic dysfunction: a case report and review of the literature. Orphanet journal of rare diseases 3 40055822
2014 rAAV/ABAD-DP-6His attenuates oxidative stress-induced injury of PC12 cells. Neural regeneration research 3 25206842
2009 Comments on 'Significance of developmental expression of amphioxus Branchiostoma belcheri and zebrafish Danio rerio Hsd17b10 in biological and medical research'. Journal of fish biology 3 20735667
2012 [Cloning and expression of fusion gene of amyloid beta binding alcohol dehydrogenase decoy peptide aptamer (TRX1-ABAD-DP-TRX2)]. Zhonghua yi xue za zhi 1 22490659
2012 [Mitochondrial enzyme ABAD and its role in the development and treatment of Alzheimer's disease]. Ceska a Slovenska farmacie : casopis Ceske farmaceuticke spolecnosti a Slovenske farmaceuticke spolecnosti 1 23251955
2026 Adult case of 17β-hydroxysteroid dehydrogenase type 10 (HSD10) deficiency due to the p. Arg130Cys mutation of the HSD17B10 gene: case report. AME case reports 0 41971928
2024 [Clinical analysis and genetic diagnosis of three children with Isoleucine metabolic disorders due to variants of HSD17B10 and ACAT1 genes]. Zhonghua yi xue yi chuan xue za zhi = Zhonghua yixue yichuanxue zazhi = Chinese journal of medical genetics 0 38684297
2001 [Analysis of the polymorphisms of the AACT, ERAB and NACP genes in 15 patients with Alzheimer's disease]. Zhonghua yi xue za zhi 0 11798857

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