HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). HSP70 and HSP90 interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP-dependent manner (1).

The results obtained in the cerebral cortex would suggest a rather sharp definition of “immature” neurons as non-newly generated, prenatally generated cells.

The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins. Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB.

Heterochromatin protein 1 (HP1) is a family of heterochromatic adaptor molecules involved in both gene silencing and higher-order chromatin structure (1).

With the rapid development of tumor immunotherapy, precise assessment of the tumor microenvironment (TME) has become a core prerequisite for interpreting immune escape mechanisms, screening populations benefiting from immunotherapy, and optimizing treatment regimens. Traditional single-marker immunohistochemistry (IHC) and immunofluorescence (IF) techniques can only detect a single marker, failing to comprehensively present the complex composition of immune cell subsets, marker co-expression characteristics, and intercellular spatial relationships in the TME, which is insufficient to meet the needs of precise immunotherapy research and clinical applications. Against this backdrop, multiplex immunohistochemistry (mIHC) and multiplex immunofluorescence (mIF) technologies have emerged and rapidly iterated, becoming core technologies for parsing TME heterogeneity and mining immunotherapy biomarkers due to their advantage of simultaneously detecting multiple markers in tissue sections.

Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin.

The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation.