Results 31 to 40 of about 97,306 (265)
mSystems, 2021 Dynamical properties of gene regulatory networks are tuned to ensure bacterial survival. In mycobacteria, the MprAB-σE network responds to the presence of stressors, such as surfactants that cause surface stress.
Satyajit D. Rao +3 more
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RNA Biology, 2016 Recently, we found that RNA is a remarkably powerful chaperone that can bind to unfolded proteins and transfer them to Hsp70 for refolding. Combined with past studies on RNA-chaperone interactions, we propose a model for how chaperone RNA activity may contribute to the cellular response to stress.
Scott, Horowitz, James C A, Bardwell
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Non-Equilibrium Protein Folding and Activation by ATP-Driven Chaperones
Biomolecules, 2022 Recent experimental studies suggest that ATP-driven molecular chaperones can stabilize protein substrates in their native structures out of thermal equilibrium. The mechanism of such non-equilibrium protein folding is an open question. Based on available
Huafeng Xu
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β-secretase 1´s Targeting Reduces Hyperphosphorilated Tau, Implying Autophagy Actors in 3xTg-AD Mice
Frontiers in Cellular Neuroscience, 2016 β-site APP cleaving enzyme 1 (BACE1) initiates APP cleavage, which has been reported to be an inducer of tau pathology by altering proteasome functions in Alzheimer’s disease (AD).
Diego ePiedrahita +6 more
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Heat shock proteins and viral infection
Frontiers in Immunology, 2022 Heat shock proteins (HSPs) are a kind of proteins which mostly found in bacterial, plant and animal cells, in which they are involved in the monitoring and regulation of cellular life activities.
Xizhen Zhang +3 more
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, 2010 The maintenance of the levels and correct folding state of proteins (proteostasis) is a fundamental prerequisite for life. Life has evolved complex mechanisms to maintain proteostasis and many of these that operate inside cells are now well understood.
Dabbs, Rebecca A +4 more
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Co-chaperones are limiting in a depleted chaperone network [PDF]
Cellular and Molecular Life Sciences, 2010 To probe the limiting nodes in the chaperoning network which maintains cellular proteostasis, we expressed a dominant negative mutant of heat shock factor 1 (dnHSF1), the regulator of the cytoplasmic proteotoxic stress response. Microarray analysis of non-stressed dnHSF1 cells showed a two- or more fold decrease in the transcript level of 10 genes ...
Heldens, L. +6 more
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The Role of the Heat Shock Protein B8 (HSPB8) in Motoneuron Diseases
Frontiers in Molecular Neuroscience, 2017 Amyotrophic lateral sclerosis (ALS) and spinal and bulbar muscular atrophy (SBMA) are two motoneuron diseases (MNDs) characterized by aberrant protein behavior in affected cells.
Paola Rusmini +14 more
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Molecular Chaperones and Co-Chaperones in Parkinson Disease [PDF]
The Neuroscientist, 2012 Parkinson disease, a progressive neurodegenerative disorder, is caused by the pathological accumulation of proteins, including the ubiquitous presynaptic protein α-synuclein. Alterations in the metabolism of α-synuclein have clearly been linked to neurodegeneration, and early steps in the pathological sequence of this protein include the formation of ...
Hemi, Dimant +2 more
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The Crimson Conundrum: Heme Toxicity and Tolerance in GAS
Frontiers in Cellular and Infection Microbiology, 2014 The massive erythrocyte lysis caused by the Group A Streptococcus (GAS) suggests that the β-hemolytic pathogen is likely to encounter free heme during the course of infection.
ANKITA JAGDISH SACHLA +4 more
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