Results 81 to 90 of about 183,487 (307)
CSPα—Chaperoning Presynaptic Proteins
Frontiers in Cellular Neuroscience, 2014 Synaptic transmission relies critically on precisely regulated and exceedingly fast protein-protein interactions that involve voltage-gated channels, the exocytosis/endocytosis machinery as well as signaling pathways. Although we have gained an ever more
Julien eDonnelier +1 more
doaj +1 more source
Blood, 2009 AbstractMultisubunit complexes containing molecular chaperones regulate protein production, stability, and degradation in virtually every cell type. We are beginning to recognize how generalized and tissue-specific chaperones regulate specialized aspects of erythropoiesis.
Mitchell J, Weiss, Camila O, dos Santos
openaire +3 more sources
FEBS Open Bio, EarlyView.Activation of the mitochondrial protein OXR1 increases pSyn129 αSynuclein aggregation by lowering ATP levels and altering mitochondrial membrane potential, particularly in response to MSA‐derived fibrils. In contrast, ablation of the ER protein EMC4 enhances autophagic flux and lysosomal clearance, broadly reducing α‐synuclein aggregates.
Sandesh Neupane +11 more
wiley +1 more source
BiomedicinesBackground: Recently identified Hero proteins, which possess chaperone-like functions, are promising candidates for research into atherosclerosis-related diseases, including ischemic stroke (IS).
Irina Shilenok +4 more
doaj +1 more source
The refolding activity of the yeast heat shock proteins Ssa1 and Ssa2 defines their role in protein translocation. [PDF]
, 1996 Ssa1/2p, members of one of the yeast cytosolic hsp70 subfamilies, have been implicated in the translocation of secretory proteins into the lumen of the ER.
Bush, GL, Meyer, DI
core
Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA [PDF]
, 1994 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.
Craig, Elisabeth A. +3 more
core +4 more sources
FEBS Open Bio, EarlyView.Pharmacological inhibition of PERK in a DEN‐induced mouse model of liver cancer does not reduce tumor burden but alters cellular stress signaling. Despite blocking PERK activity, downstream stress responses, including CHOP expression, remain active, suggesting compensatory mechanisms within the unfolded protein response that may influence tumor ...
Ada Lerma‐Clavero +5 more
wiley +1 more source
Metallochaperones regulate intracellular copper levels. [PDF]
, 2013 Copper (Cu) is an important enzyme co-factor that is also extremely toxic at high intracellular concentrations, making active efflux mechanisms essential for preventing Cu accumulation. Here, we have investigated the mechanistic role of metallochaperones
Adams, Michael +9 more
core +1 more source
Mutant NPM1 in Acute Myeloid Leukemia Initiation and Maintenance
Aging and Cancer, EarlyView.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
Protein evolution speed depends on its stability and abundance and on chaperone concentrations. [PDF]
, 2018 Proteins evolve at different rates. What drives the speed of protein sequence changes? Two main factors are a protein's folding stability and aggregation propensity. By combining the hydrophobic-polar (HP) model with the Zwanzig-Szabo-Bagchi rate theory,
Agozzino, Luca, Dill, Ken A
core +1 more source