Results 21 to 30 of about 4,011,919 (357)
Genetic polymorphisms of Ca2+ transport proteins and molecular chaperones in mitochondria-associated endoplasmic reticulum membrane and non-alcoholic fatty liver disease. [PDF]
Tang Z +10 more
europepmc +3 more sources
The dysfunction of the proteostasis network is a molecular hallmark of neurodegenerative diseases such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease, and amyotrophic lateral sclerosis. Molecular chaperones are a major component of the
Lisha Wang +4 more
doaj +1 more source
Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery
Modulation of protein fate decision and protein homeostasis plays a significant role in altering the protein level, which acts as an orientation to develop drugs with new mechanisms.
Lei Wang +3 more
doaj +1 more source
The Chemical Biology of Molecular Chaperones—Implications for Modulation of Proteostasis
Kristoffer Brandvold +1 more
openalex +2 more sources
Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum [PDF]
The plant cytotoxin ricin enters target mammalian cells by receptor-mediated endocytosis and undergoes retrograde transport to the endoplasmic reticulum (ER).
Argent +32 more
core +4 more sources
Molecular Chaperones: Molecular Assembly Line Brings Metabolism and Immunity in Shape
Molecular chaperones are a set of conserved proteins that have evolved to assist the folding of many newly synthesized proteins by preventing their misfolding under conditions such as elevated temperatures, hypoxia, acidosis and nutrient deprivation ...
Haoxin Zhao +2 more
doaj +1 more source
Molecular Chaperone Receptors [PDF]
Extracellular heat shock proteins (HSP) play important roles in cell signaling and immunity. Many of these effects are mediated by surface receptors expressed on a wide range of cell types. We have investigated the nature of such proteins by cloning candidate receptors into cells (CHO-K1) with the rare property of being null for HSP binding. Using this
Ayesha, Murshid +3 more
openaire +2 more sources
Recent advances in understanding catalysis of protein folding by molecular chaperones
Molecular chaperones are highly conserved proteins that promote proper folding of other proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking, the assembly of oligomeric complexes, and recovery from stress‐induced ...
D. Balchin, M. Hayer-Hartl, F. Hartl
semanticscholar +1 more source
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.
A. Marino Gammazza +7 more
semanticscholar +1 more source
Molecular Chaperones: A Double-Edged Sword in Neurodegenerative Diseases
Aberrant accumulation of misfolded proteins into amyloid deposits is a hallmark in many age-related neurodegenerative diseases, including Alzheimer’s disease (AD), Parkinson’s disease (PD), Huntington’s disease (HD), and amyotrophic lateral sclerosis ...
Jessica Tittelmeier +2 more
semanticscholar +1 more source

