Results 101 to 110 of about 4,011,919 (357)

Heat Shock Proteins: A Review of the Molecular Chaperones for Plant Immunity

open access: yesPlant Pathology Journal, 2015
As sessile organisms, plants are exposed to persistently changing stresses and have to be able to interpret and respond to them. The stresses, drought, salinity, chemicals, cold and hot temperatures, and various pathogen attacks have interconnected ...
Chang-Jin Park, Y. Seo
semanticscholar   +1 more source

Targeting the ARRDC3–DRP1 Axis via hUMSC‐Derived Exosomal CRYAB for Neuroprotection in Cerebral Ischemia/Reperfusion Injury

open access: yesAdvanced Healthcare Materials, EarlyView.
Intranasally administered hUMSC‐derived exosomes modulate the CRYAB–ARRDC3–Drp1 axis, alleviating mitochondrial dysfunction and ferroptosis, enhancing neuronal survival, reducing oxidative stress, and promoting functional recovery in ischemia‐reperfusion injury, offering a promising therapeutic strategy for ischemic stroke.
Rong ji   +7 more
wiley   +1 more source

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

open access: yesNature 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   +5 more
doaj   +1 more source

Proteostasis collapse is a driver of cell aging and death. [PDF]

open access: yes, 2019
What molecular processes drive cell aging and death? Here, we model how proteostasis-i.e., the folding, chaperoning, and maintenance of protein function-collapses with age from slowed translation and cumulative oxidative damage.
de Graff, Adam MR   +2 more
core  

Chaperone driven polymer translocation through Nanopore: spatial distribution and binding energy

open access: yes, 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

Oxidative protein biogenesis and redox regulation in the mitochondrial intermembrane space [PDF]

open access: yes, 2016
Mitochondria are organelles that play a central role in cellular metabolism, as they are responsible for processes such as iron/sulfur cluster biogenesis, respiration and apoptosis.
MacPherson, Lisa   +2 more
core   +1 more source

Rational Design of Optical Single‐Walled Carbon Nanotube‐Based Nanosensors with Biological Recognition Elements

open access: yesAdvanced Sensor Research, EarlyView.
This Review focuses on assessing and providing perspective on the field of rationally‐designed optical sensors constructed with single‐walled carbon nanotubes. The literature is reviewed and evaluated for SWCNT‐based sensors constructed with biomolecular recognition elements, including proteins, peptides, and oligonucleotides, as well as their methods ...
Amelia K. Ryan   +4 more
wiley   +1 more source

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

open access: yesPLoS 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   +8 more
doaj   +1 more source

Heat shock factor 1 regulates lifespan as distinct from disease onset in prion disease [PDF]

open access: yes, 2008
Prion diseases are fatal, transmissible, neurodegenerative diseases caused by the misfolding of the prion protein (PrP). At present, the molecular pathways underlying prion-mediated neurotoxicity are largely unknown.
Aguzzi, Adriano   +8 more
core   +3 more sources

The nucleotide exchange factors of Hsp70 molecular chaperones

open access: yesFrontiers in Molecular Biosciences, 2015
Molecular chaperones of the Hsp70 family form an important hub in the cellular protein folding networks in bacteria and eukaryotes, connecting translation with the downstream machineries of protein folding and degradation.
A. Bracher, J. Verghese
semanticscholar   +1 more source

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