Results 71 to 80 of about 94,343 (283)
Molecular chaperones and the protein production line [PDF]
, 1994 The folding of proteins to their active state in the cell, long thought to be a spontaneous process, requires the assistance of other proteins called molecular chaperones.
Lund, Peter A.
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Российский офтальмологический журнал, 2018 The literary review focuses on the dysfunction of endoplasmic reticulum (EPR), the role of EPR stress and oxidative stress in the pathogenesis of optic nerve damage.
V. V. Neroev +2 more
doaj +1 more source
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
Versatile vector tools for efficient protein screening across multiple expression systems
FEBS Open Bio, EarlyView.A unified vector toolkit enables rapid protein expression screening across E. coli, insect, and mammalian cells. A single primer pair amplifies the target gene, which is inserted into any vector via a standardized interface. This streamlined workflow eliminates repeated cloning steps, accelerating the identification of optimal expression conditions for
Zhimin Zhu +5 more
wiley +1 more source
Molecular Systems Biology, 2009 Molecular chaperones are known to be involved in many cellular functions, however, a detailed and comprehensive overview of the interactions between chaperones and their cofactors and substrates is still absent.
Yunchen Gong +6 more
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Probing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics. [PDF]
PLoS ONE, 2012 Deciphering functional mechanisms of the Hsp90 chaperone machinery is an important objective in cancer biology aiming to facilitate discovery of targeted anti-cancer therapies.
Anshuman Dixit, Gennady M Verkhivker
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Proteome-Wide Analyis of Chaperonin-Dependent Protein Folding in Escherichia coli [PDF]
, 2006 In Escherichia coli, the cylindrical chaperonin GroEL and its cofactor GroES promote the folding of a fraction of newly synthesized polypeptide chains by acting as an Anfinsen cage.
Maier, T., Maier, Tobias
core
Evaluating the involvement of autolysosomes in the nuclear translocation of fluorescent proteins
FEBS Open Bio, EarlyView.Endogenously expressed fluorescent proteins can be degraded by autophagy and transported to cell nuclei via the nuclear pore complex. But in some cell lines, for example, HeLa cells which are positive for immunoreactivity of a receptor ligand, such as UCN I, in cell nuclei, fusion of autolysosome with the nuclear envelope is involved in the nuclear ...
Keiichi Ikeda
wiley +1 more source
G3: Genes, Genomes, Genetics, 2017 Accumulation of toxic proteins in neurons has been linked with the onset of neurodegenerative diseases, which in many cases are characterized by altered neuronal function and synapse loss.
Sandeep Raut +5 more
doaj +1 more source
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
openaire +2 more sources