Results 61 to 70 of about 3,296,549 (170)

MOLECULAR MECHANISMS OF OPTIC NERVE DAMAGE: THE ROLE OF ANTHOCYANOZIDES IN THE PREVENTION OF RETINAL GANGLION CELL DEATH

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, T. N. Kiseleva, Ì. S. Zaitsev   +2 more
doaj   +1 more source

Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones.

, 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., de Marco, A., Goloubinoff, P., Vigh, L.   +3 more
core   +1 more source

Human molecular chaperones share with SARS-CoV-2 antigenic epitopes potentially capable of eliciting autoimmunity against endothelial cells: possible role of molecular mimicry in COVID-19

, 2020
Severe acute respiratory syndrome corona virus 2 (SARS-CoV-2), the cause of COVID-19 disease, has the potential to elicit autoimmunity because mimicry of human molecular chaperones by viral proteins.
Legare S., Conway de Macario E., Macario A. J., Cappello F., Marino Gammazza A., Angileri F., Lo Bosco G., Fucarino A.   +7 more
core   +1 more source

An atlas of chaperone–protein interactions in Saccharomyces cerevisiae: implications to protein folding pathways in the cell

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, Yoshito Kakihara, Nevan Krogan, Jack Greenblatt, Andrew Emili, Zhaolei Zhang, Walid A Houry   +6 more
doaj   +1 more source

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
doaj   +1 more source

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   +1 more source

RNAi-Mediated Reverse Genetic Screen Identified Drosophila Chaperones Regulating Eye and Neuromuscular Junction Morphology

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, Bhagaban Mallik, Arpan Parichha, Valsakumar Amrutha, Chandan Sahi, Vimlesh Kumar   +5 more
doaj   +1 more source

Aggregation Prevention Assay for Chaperone Activity of Proteins Using Spectroflurometry

Bio-Protocol, 2017
The ability to stabilize other proteins against thermal aggregation is one of the major characteristics of chaperone proteins. Molecular chaperones bind to nonnative conformations of proteins.
Manish Bhuwan, Madhuri Suragani, Nasreen Ehtesham, Seyed Hasnain   +3 more
doaj   +1 more source

The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation

Nature Communications, 2019
Hsp90 is a molecular chaperone that acts together with co-chaperones to ensure folding and activation of many client proteins. Here authors show that a N-terminal motif in Aha-type co-chaperones modulates the apparent affinity of Hsp90 for nucleotide ...
Rebecca Mercier, Annemarie Wolmarans, Jonathan Schubert, Hannes Neuweiler, Jill L. Johnson, Paul LaPointe   +5 more
doaj   +1 more source

Hsp40 couples with the CSPalpha chaperone complex upon induction of the heat shock response.

PLoS ONE, 2009
In response to a conditioning stress, the expression of a set of molecular chaperones called heat shock proteins is increased. In neurons, stress-induced and constitutively expressed molecular chaperones protect against damage induced by ischemia and ...
Sarah J Gibbs, Brandy Barren, Katy E Beck, Juliane Proft, Xiaoxi Zhao, Tatiana Noskova, Andrew P Braun, Nikolai O Artemyev, Janice E A Braun   +8 more
doaj   +1 more source