Results 41 to 50 of about 183,487 (307)
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
doaj +1 more source
The SseC translocon component in Salmonella enterica serovar Typhimurium is chaperoned by SscA [PDF]
, 2013 Background: Salmonella enterica is a causative agent of foodborne gastroenteritis and the systemic disease known as typhoid fever. This bacterium uses two type three secretion systems (T3SSs) to translocate protein effectors into host cells to manipulate
Allison, Sarah E +4 more
core +1 more source
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
doaj +1 more source
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
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
doaj +1 more source
Chaperone driven polymer translocation through Nanopore: spatial distribution and binding energy
, 2016 Chaperones are binding proteins which work as a driving force to bias the biopolymer translocation by binding to it near the pore and preventing its backsliding. Chaperones may have different spatial distribution. Recently we show the importance of their
Abdolvahab, Rouhollah Haji
core +1 more source
Thermodynamic bounds on the ultra- and infra-affinity of Hsp70 for its substrates [PDF]
, 2017 The 70 kDa Heat Shock Proteins Hsp70 have several essential functions in living systems, such as protecting cells against protein aggregation, assisting protein folding, remodeling protein complexes and driving the translocation into organelles.
Hartich, David +3 more
core +2 more sources
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
openaire +4 more sources
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
Aging cellular networks: chaperones as major participants
, 2006 We increasingly rely on the network approach to understand the complexity of cellular functions. Chaperones (heat shock proteins) are key "networkers", which have among their functions to sequester and repair damaged protein. In order to link the network
Agoston +56 more
core +1 more source