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AI‐enabled de novo design of a TREM1 binder, integrated into a BBB‐crossing and macrophage‐targeted nanoplatform, enables TREM1 degradation and attenuates neuroinflammation, thereby promoting neuroprotection and tissue repair after traumatic brain injury. ABSTRACT Secondary neuroinflammation drives progressive damage after traumatic brain injury (TBI),
Yimin Huang +19 more
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Heat shock proteins related signature characterizes immune status and predicts prognosis of gliomas. [PDF]
Sun Z +8 more
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Hippocampal CA2 perineuronal nets ensheathing excitatory pyramidal neurons are selectively vulnerable to repeated neonatal sevoflurane exposure. Epigenetic upregulation of MMP9 via reduced H3K27me3 disrupts PNN integrity, impairs BDNF–TrkB signaling, and causes synaptic protein loss and dendritic spine deficits, leading to persistent social and spatial
Lirong Liang +11 more
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Sarbecovirus ORF9b recruits host phosphatase PPM1A to suppress innate immunity through dual mechanisms. PPM1A directly dephosphorylates ORF9b to sustain its activity and indirectly downregulates STAT2 phosphorylation to impair interferon signaling. Pharmacological inhibition of PPM1A restores antiviral responses and limits sarbecovirus replication ...
Lixiang Xie +24 more
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Administration of opioids activates ephrinB2‐EphB1 receptor signaling. Activated EphB1 receptors induce GRK2‐mediated phosphorylation of MOR at Ser375, which initiates the internalization of MOR and reduces opioid antinociception at the behavioral level. ABSTRACT Opioids are the primary treatment for severe pain in clinical practice.
Bo Peng +7 more
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Current Protocols, 2022
AbstractHeat‐shock proteins (HSPs), or stress proteins, are abundant and highly conserved, present in all organisms and in all cells. Selected HSPs, also known as chaperones, play crucial roles in folding and unfolding of proteins, assembly of multiprotein complexes, transport and sorting of proteins into correct subcellular compartments, cell‐cycle ...
Adam T, Hagymasi +2 more
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AbstractHeat‐shock proteins (HSPs), or stress proteins, are abundant and highly conserved, present in all organisms and in all cells. Selected HSPs, also known as chaperones, play crucial roles in folding and unfolding of proteins, assembly of multiprotein complexes, transport and sorting of proteins into correct subcellular compartments, cell‐cycle ...
Adam T, Hagymasi +2 more
openaire +2 more sources
Endeavour, 1988
Abstract Bacteria, plans and animals are all very sensitive to small changes of temperature and, indeed, life of any sort is possible only within a relatively small temperature range. Although it is well established that heat stress induces tolerance to further heat stress, the nature of the response at the molecular level has been obscure.
S, Lindquist, E A, Craig
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Abstract Bacteria, plans and animals are all very sensitive to small changes of temperature and, indeed, life of any sort is possible only within a relatively small temperature range. Although it is well established that heat stress induces tolerance to further heat stress, the nature of the response at the molecular level has been obscure.
S, Lindquist, E A, Craig
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Current Protocols in Immunology, 2003
AbstractHeat‐shock proteins (HSPs), or stress proteins, are highly conserved and present in all organisms and in all cells of all organisms. Selected HSPs, also known as chaperones, play crucial roles in folding/unfolding of proteins, assembly of multiprotein complexes, transport/sorting of proteins into correct subcellular compartments, cell‐cycle ...
Zihai, Li, Pramod, Srivastava
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AbstractHeat‐shock proteins (HSPs), or stress proteins, are highly conserved and present in all organisms and in all cells of all organisms. Selected HSPs, also known as chaperones, play crucial roles in folding/unfolding of proteins, assembly of multiprotein complexes, transport/sorting of proteins into correct subcellular compartments, cell‐cycle ...
Zihai, Li, Pramod, Srivastava
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Heat shock proteins and effects of heat shock in plants
Plant Molecular Biology, 1982Soybean seedlings when exposed to a heat shock respond in a manner very similar to that exhibited by cultured cells, and reported earlier [2]. Maximum synthesis of heat shock proteins (HSPs) occurs at 40C. The heat shock response is maintained for a relatively short time under continuous high temperature.
M, Altschuler, J P, Mascarenhas
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Heat shock proteins in infection
Clinica Chimica Acta, 2019Heat shock proteins (HSPs) are constitutively expressed under physiological conditions in most organisms but their expression can significantly enhance in response to four types of stimuli including physical (e.g., radiation or heat shock), chemical and microbial (e.g., pathogenic bacteria, viruses, parasites and fungi) stimuli, and also dietary. These
Azam, Bolhassani, Elnaz, Agi
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