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Molecular Mechanisms and Drug Treatment in Alzheimer’s Disease

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Neurobiology".

Deadline for manuscript submissions: 20 March 2026 | Viewed by 1053

Special Issue Editors


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Guest Editor
Department of Biochemistry, Desio Hospital, ASST-Brianza, 20832 Desio, Italy
Interests: intracerebroventricular; mtor; mTOR-I; rapalog; neurological disorders; neurodegeneration; Alzheimer’s disease; DSPE-PEG2000 micelles; micellar liquid formulation; drug stabilization

E-Mail Website
Guest Editor
Neuroscience Institute of Rosà, 36027 Rosà, Italy
Interests: Alzheimer's disease; cognitive function; neurobehavioral disorders

Special Issue Information

Dear Colleagues,

The understanding of the pathogenic mechanisms of Alzheimer's disease in the last decade is evolving much more rapidly than in the entire century from the discovery to the first decade of the new millennium. New hypotheses are emerging. Moreover, the role of the Immune System is growing, and according to some, it will soon prove to be prevalent and will modify the entire concept of “neurodegenerative diseases”.

The dynamics of Beta-Amyloid and NeuroFibrillary Tangle accumulation, their toxicity for the neuron, the interaction between neuron and glia, and between neurons and the Immune System: these remain the main chapters. It is difficult to predict which of these will offer therapies capable of effectively reaching the patient.

The journal does not deal with clinical trials, but in this Special Issue, all studies preceding this phase, on the understanding of dementia and possible molecular targets in the search for a pharmacological treatment, are welcome.

Dr. Roberto Dominici
Dr. Diego Dolcetta
Guest Editors

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Keywords

  • Alzheimer’s disease (AD)
  • glia
  • immune system
  • neurotoxicity
  • inflammation
  • beta-Amyloid (bA)
  • neurofibrillary tangles (NFTs)

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Published Papers (1 paper)

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24 pages, 5024 KB  
Article
Deubiquitinating Enzymes Ubiquitin-Specific Proteases 7 and 10 Regulate TAU Aggregation
by Christiane Volbracht and Karina Fog
Int. J. Mol. Sci. 2025, 26(22), 11062; https://doi.org/10.3390/ijms262211062 - 15 Nov 2025
Viewed by 621
Abstract
Accumulation of the microtubule-associated protein TAU into inclusions is a hallmark of tauopathies including Alzheimer’s disease (AD), potentially driven by impaired protein degradation and dysregulated ubiquitination. To explore the role of deubiquitinating enzymes (DUBs), we performed siRNA knockdown screens targeting 93 murine DUBs [...] Read more.
Accumulation of the microtubule-associated protein TAU into inclusions is a hallmark of tauopathies including Alzheimer’s disease (AD), potentially driven by impaired protein degradation and dysregulated ubiquitination. To explore the role of deubiquitinating enzymes (DUBs), we performed siRNA knockdown screens targeting 93 murine DUBs in rTg4510 cortical cultures. Knockdown and pharmacological inhibition of the ubiquitin-specific proteases 7 (Usp7) and 10 (Usp10) significantly reduced seeded TAU aggregation without affecting soluble TAU levels. These effects were observed in both cortical and organotypic hippocampal slice cultures from rTg4510 mice, as well as in wildtype neurons seeded with AD-derived pathological TAU. Inhibition of Usp7 and Usp10 was associated with increased polyubiquitination of residual TAU inclusions in rTg4510 cortical cultures. These findings suggest that Usp7 and Usp10 contribute to pathological TAU accumulation by modulating ubiquitin-dependent degradation pathways. Targeting USP7 and USP10 may offer a novel therapeutic strategy for AD and related tauopathies. Full article
(This article belongs to the Special Issue Molecular Mechanisms and Drug Treatment in Alzheimer’s Disease)
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