Results 1 to 10 of about 183,487 (307)

Neuroprotection Targeting Protein Misfolding on Chronic Cerebral Hypoperfusion in the Context of Metabolic Syndrome [PDF]

open access: yesFrontiers in Neuroscience, 2018
Metabolic syndrome (MetS) is a cluster of risk factors that lead to microvascular dysfunction and chronic cerebral hypoperfusion (CCH). Long-standing reduction in oxygen and energy supply leads to brain hypoxia and protein misfolding, thereby linking CCH
María I. Herrera   +9 more
doaj   +3 more sources

Chemical Chaperones Improve Protein Secretion and Rescue Mutant Factor VIII in Mice with Hemophilia A. [PDF]

open access: yes, 2012
nefficient intracellular protein trafficking is a critical issue in the pathogenesis of a variety of diseases and in recombinant protein production.
Abriss, Daniela   +9 more
core   +13 more sources

Molecular chaperones and Parkinson's disease

open access: yesNeurobiology of Disease, 2021
Parkinson's disease (PD) is a neurodegenerative disease characterized by progressive death of dopaminergic neurons in the substantia nigra and the formation of Lewy bodies (LBs). Mutations in PD-related genes lead to neuronal pathogenesis through various
Shenglan Hu   +7 more
doaj   +1 more source

Targeting Chaperone/Co-Chaperone Interactions with Small Molecules: A Novel Approach to Tackle Neurodegenerative Diseases

open access: yesCells, 2021
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

The unhappy chaperone [PDF]

open access: yesQRB Discovery, 2021
Abstract Chaperones protect other proteins against misfolding and aggregation, a key requirement for maintaining biological function. Experimental observations of changes in solubility of amyloid proteins in the presence of certain chaperones are discussed here in terms of thermodynamic driving forces.
Sara Linse   +2 more
openaire   +3 more sources

Arabinogalactan-Proteins as Boron-Acting Enzymes, Cross-Linking the Rhamnogalacturonan-II Domains of Pectin

open access: yesPlants, 2023
Most pectic rhamnogalacturonan-II (RG-II) domains in plant cell walls are borate-bridged dimers. However, the sub-cellular locations, pH dependence, reversibility and biocatalyst involvement in borate bridging remain uncertain. Experiments discussed here
Rifat Ara Begum, Stephen C. Fry
doaj   +1 more source

The DNAJ gene family in yerba mate (Ilex paraguariensis): genome-wide identification, structural characterization, orthology based classification and expression analysis [PDF]

open access: yesRodriguésia, 2023
Dry leaves and twigs of yerba mate are widely infusion-consumed in southern Southamerica. Endemic and adapted to the Atlantic Forest, its extensive full-sun monoculture links to diverse biotic (pest, pathogens) and abiotic stresses (solar radiation ...
Patricia Mabel Aguilera   +4 more
doaj   +1 more source

How DNA and RNA Viruses Exploit Host Chaperones to Promote Infection

open access: yesViruses, 2021
To initiate infection, a virus enters a host cell typically via receptor-dependent endocytosis. It then penetrates a subcellular membrane, reaching a destination that supports transcription, translation, and replication of the viral genome.
Kaitlyn Speckhart   +2 more
doaj   +1 more source

A network of cytosolic (co)chaperones promotes the biogenesis of mitochondrial signal-anchored outer membrane proteins

open access: yeseLife, 2022
Signal-anchored (SA) proteins are anchored into the mitochondrial outer membrane (OM) via a single transmembrane segment at their N-terminus while the bulk of the proteins is facing the cytosol.
Layla Drwesh   +9 more
doaj   +1 more source

Faithful chaperones [PDF]

open access: yesCellular and Molecular Life Sciences, 2011
This review describes the properties of some rare eukaryotic chaperones that each assist in the folding of only one target protein. In particular, we describe (1) the tubulin cofactors, (2) p47, which assists in the folding of collagen, (3) α-hemoglobin stabilizing protein (AHSP), (4) the adenovirus L4-100 K protein, which is a chaperone of the major ...
Szolajska, Ewa, Chroboczek, Jadwiga
openaire   +2 more sources

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