Correction to: Molecular Psychiatry, published online 5 September 2023

In this article, an incorrect table was inadvertently displayed as Table 2. Correct Table 2 is shown below:

Table 2. Targeting synaptic function for Alzheimer’s drug development*

Molecular target

Drugs

Clinical trials

References

Fyn kinase

Saracatinib

Phase 2

[197–199]; NCT02167256

Tyrosine kinase

Masitinib

Phase 3

[199, 200]; NCT01872598

Rho kinase

Fasudil

Preclinical

[201, 202]

Rho kinase

FSD-C10

Preclinical

[203, 204]

NMDA receptor

Memantine

Approved

[205, 206]

Glutamatergic pathway

NitroSynapsin

Preclinical

[207, 208]

Glutamate generation

Riluzole

Phase 2

[98, 209]; NCT01703117

Cholinesterase

Donepezil

Approved

[210–212]

Cholinesterase

Galantamine

Approved

[213–215]

Cholinesterase

Rivastigmine

Approved

[213, 216, 217]

Serotonin reuptake

Sertraline

Phase 4

[126, 218–220]; NCT00009191

Neurotrophic factors

BDNF

Phase 1

[221–224]; NCT05040217

Neurotrophin receptor

LM11A-31

Phase 2

[225]; NCT03069014

  1. *Adapted from Table 1 of Peng L, Bestard-Lorigados I, Song W. Mol Psychiatry. 2022;27:2940–2949.

In this article, the captions for Figs. 3 and 4 were inadvertently swapped. The correct captions for these figures are shown below:

Figure 3. The effect of Aβ on synaptic transmission. APP can be cleaved by β-secretase at the Asp1 site, leading to the generation of membrane-bound C99, which is subsequently cleaved by γ-secretase to produce intracellular C-terminal fragments and Aβ. The increased presence of Aβ monomers promotes the formation of Aβ oligomers, which further induce tau phosphorylation, leading to the subsequent formation of neurofibrillary tangles and impairing LTP by disrupting the balance between glutamatergic and GABAergic activity. Aβ amyloid β protein, APP amyloid precursor protein, C99 C-terminal fragment of 99 amino acids, GABAergic gamma-aminobutyric acid (GABA)-ergic, LTP long-term potentiation.

Figure 4. NLRP3-mediated glia cells contribute to neuronal dysfunction. Aβ aggregation induces the activation and accumulation of NLRP3 inflammasome in microglia, which results in the secretion of IL-1β. The increased level of IL-1β further accelerates the senescence of astrocytes and reduces the phagocytic capacity of astrocytes, leading to the accumulation of synaptic debris and neuronal dysfunction. ApoE4 exacerbates this process by promoting the accumulation of C1q, resulting in hyperactive microglia and an intensified loss of synapses. Aβ amyloid β protein, ApoE4 apolipoprotein-E4, C1q complement 1q, IL-1β interleukin-1β, NLRP3 the NACHT, LRR and PYD domains-containing protein 3.

The original article has been corrected.