Results 41 to 50 of about 110,947 (209)
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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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
openaire +2 more sources
, 2012 nefficient intracellular protein trafficking is a critical issue in the pathogenesis of a variety of diseases and in recombinant protein production.
Tonn, Torsten +19 more
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Quantitative patterns of Hsps in tubular adenoma compared with normal and tumor tissues reveal the value of Hsp10 and Hsp60 in early diagnosis of large bowel cancer [PDF]
, 2016 Large bowel carcinogenesis involves accumulation of genetic alterations leading to transformation of normal mucosa into dysplasia and, lastly, adenocarcinoma.
PITRUZZELLA, Alessandro +11 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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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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Frontiers in Neuroscience, 2019 Misfolding protein diseases are a wide class of disorders in which the aberrantly folded protein aggregates accumulate in affected cells. In the brain and in the skeletal muscle, misfolded protein accumulation induces a variety of cell dysfunctions that ...
Riccardo Cristofani +13 more
doaj +1 more source
, 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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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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, 2005 When massively expressed in bacteria, recombinant proteins often tend to misfold and accumulate as soluble and insoluble nonfunctional aggregates. A general strategy to improve the native folding of recombinant proteins is to increase the cellular ...
Diamant, S. +3 more
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