Results 81 to 90 of about 94,343 (283)
Molecular chaperones and neuronal proteostasis. [PDF]
Protein homeostasis (proteostasis) is essential for maintaining the functionality of the proteome. The disruption of proteostasis, due to genetic mutations or an age-related decline, leads to aberrantly folded proteins that typically lose their function.
Smith, HL, Li, W, Cheetham, ME
core
Mutant NPM1 in Acute Myeloid Leukemia Initiation and Maintenance
NPM1 mutations drive acute myeloid leukemia by acting as neomorphic transcriptional regulators that cooperate with Menin–MLL and XPO1 to sustain HOX/MEIS1 expression and block differentiation. Targeting these mutant‐specific transcriptional dependencies provides a rational therapeutic strategy for NPM1‐mutated AML.
Yanan Jiang +3 more
wiley +1 more source
Chromatin homeostasis mediates essential processes in eukaryotes, where histone chaperones have emerged as major regulatory factors during DNA replication, repair, and transcription.
Pedro Buzón +5 more
doaj +1 more source
Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA [PDF]
Mitochondrial heat shock protein 70 (mt-Hsp70) has been shown to play an important role in facilitating import into, as well as folding and assembly of nuclear-encoded proteins in the mitochondrial matrix.
W Neupert +7 more
core +1 more source
ABSTRACT Objective Variants in SLC6A1, encoding the GABA transporter 1 (GAT‐1), cause epilepsy, autism spectrum disorder, and developmental delay via loss of GABA uptake, impaired trafficking, and ER retention. We previously found that 4‐Phenylbutyrate (PBA), an FDA‐approved drug, restores GABA uptake and reduces seizures in SLC6A1‐related disorders ...
Melissa B. DeLeeuw +5 more
wiley +1 more source
Aggregation Prevention Assay for Chaperone Activity of Proteins Using Spectroflurometry
The ability to stabilize other proteins against thermal aggregation is one of the major characteristics of chaperone proteins. Molecular chaperones bind to nonnative conformations of proteins.
Manish Bhuwan +3 more
doaj +1 more source
Structural and functional characterization of Pseudomonas aeruginosa CupB chaperones [PDF]
Pseudomonas aeruginosa, an important human pathogen, is estimated to be responsible for,10% of nosocomial infections worldwide. The pathogenesis of P. aeruginosa starts from its colonization in the damaged tissue or medical devices (e. g.
Filloux, A. +23 more
core +1 more source
We measure the cell‐specific responses of administering infusible ECM (iECM) in acute myocardial infarction (MI) across multiple timepoints. Using single‐nucleus RNA sequencing and spatial transcriptomics, we measure macrophage activation, fibroblast remodeling, increased vascular development, lymphangiogenesis, cardioprotection, and neurogenesis ...
Joshua M. Mesfin +18 more
wiley +1 more source
Malectin alleviates high glucose‐induced ER stress and damage in placental trophoblasts, a function dependent on its six critical carbohydrate‐binding residues. In a GDM mouse model, administration of TAT‐Malectin ameliorated hyperglycemia and placental ER stress and prevented fetal macrosomia.
Jiahui Zhu +12 more
wiley +1 more source
Hsp90 is a molecular chaperone that acts together with co-chaperones to ensure folding and activation of many client proteins. Here authors show that a N-terminal motif in Aha-type co-chaperones modulates the apparent affinity of Hsp90 for nucleotide ...
Rebecca Mercier +5 more
doaj +1 more source

