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@ARTICLE{Zafar:282327,
      author       = {Zafar, Saima and Noor, Aneeqa and Younas, Neelam and
                      Shafiq, Mohsin and Dittmar, Kathrin and Yagensky, Oleksandr
                      and Schmitz, Matthias and Ferrer, Isidre and Hermann, Peter
                      and Zerr, Inga},
      title        = {{P}roteomic {P}rofiling {R}eveals {M}itochondrial
                      {D}ysregulation in {R}apidly {P}rogressive {A}lzheimer's:
                      {R}ole of {DLDH} in {A}myloid {B}eta {A}ggregation.},
      journal      = {Molecular neurobiology},
      volume       = {63},
      number       = {1},
      issn         = {0893-7648},
      address      = {Totowa, NJ},
      publisher    = {Humana Press},
      reportid     = {DZNE-2025-01288},
      pages        = {73},
      year         = {2025},
      abstract     = {Alzheimer's disease (AD) is presented as multiple clinical
                      variants depending upon the rate of progression and familial
                      background; however, the exact molecular mechanisms
                      associated with these subtypes and their treatments are yet
                      to be understood. The current study is based on a global
                      proteome analysis of brain samples from patients (n = 38)
                      with rapidly progressive AD (rpAD-survival time < 3 years),
                      sporadic AD (spAD-survival time of 8-10 years), and healthy
                      controls. Proteome analysis revealed a differential
                      regulation of 79 proteins and highlighted the dysregulation
                      of mitochondrial machinery and glucose metabolism in rpAD.
                      Dihydrolipoamide dehydrogenase (DLDH), a mitochondrial
                      oxidoreductase, showed a significant reduction and
                      delocalization in rpAD. In vitro analysis revealed a
                      potential role of DLDH in the aggregation of amyloid beta.
                      Rapid progression in AD may be influenced by the energy
                      homeostasis and redox dysfunction linked with the DLDH.},
      keywords     = {Humans / Alzheimer Disease: metabolism / Alzheimer Disease:
                      pathology / Amyloid beta-Peptides: metabolism / Proteomics:
                      methods / Mitochondria: metabolism / Mitochondria: pathology
                      / Male / Female / Disease Progression / Aged / Protein
                      Aggregation, Pathological: metabolism / Brain: metabolism /
                      Brain: pathology / Protein Aggregates / Aged, 80 and over /
                      Alzheimer’s disease (AD) (Other) / DLDH (Other) /
                      Metabolic networks (Other) / Metabolism (Other) /
                      Post-translational modification (Other) / Proteomics (Other)
                      / Rapidly progressive Alzheimer’s disease (rpAD) (Other) /
                      Amyloid beta-Peptides (NLM Chemicals) / Protein Aggregates
                      (NLM Chemicals)},
      cin          = {AG Zerr},
      ddc          = {570},
      cid          = {I:(DE-2719)1440011-1},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41254340},
      doi          = {10.1007/s12035-025-05327-0},
      url          = {https://pub.dzne.de/record/282327},
}