Results 61 to 70 of about 110,947 (209)
Toxins, 2018 The Bordetella pertussis toxin (PT) is one important virulence factor causing the severe childhood disease whooping cough which still accounted for approximately 63,000 deaths worldwide in children in 2013.
Katharina Ernst +8 more
doaj +1 more source
Disruption of the Ubiquitin-Proteasome System and Elevated Endoplasmic Reticulum Stress in Epilepsy
Biomedicines, 2022 The epilepsies are a broad group of conditions characterized by repeated seizures, and together are one of the most common neurological disorders. Additionally, epilepsy is comorbid with many neurological disorders, including lysosomal storage diseases ...
Sarah Poliquin, Jing-Qiong Kang
doaj +1 more source
, 2022 The folding of proteins into their native structure is crucial for the functioning of all biological processes. Molecular chaperones are guardians of the proteome that assist in protein folding and prevent the accumulation of aberrant protein ...
Bardwell, James C. A. +3 more
core +1 more source
Pharmaceuticals, 2012 In this review, we focus on how inhibitors of Hsp90 can help prevent the resistance to anti-cancer drugs by synergistically increasing their cancer killing abilities and thereby allowing them to function at much lower concentrations than normally used ...
Douglas M. Ruden, Xiangyi Lu, Luan Wang
doaj +1 more source
Single-molecule fluorescence studies of Protein Folding and Molecular Chaperones [PDF]
, 2011 Folding of newly synthesized proteins is an essential part of protein biosynthesis and misfolding can result in protein aggregation which can also lead to several severe diseases.
Sikor, Martin
core
Abnormal Copper Homeostasis: Mechanisms and Roles in Neurodegeneration
Toxics, 2014 As a cofactor of proteins and enzymes involved in critical molecular pathways in mammals and low eukaryotes, copper is a transition metal essential for life.
Mario Manto
doaj +1 more source
Blood, 2009 AbstractMultisubunit complexes containing molecular chaperones regulate protein production, stability, and degradation in virtually every cell type. We are beginning to recognize how generalized and tissue-specific chaperones regulate specialized aspects of erythropoiesis.
Mitchell J, Weiss, Camila O, dos Santos
openaire +3 more sources
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
CSPα—Chaperoning Presynaptic Proteins
Frontiers in Cellular Neuroscience, 2014 Synaptic transmission relies critically on precisely regulated and exceedingly fast protein-protein interactions that involve voltage-gated channels, the exocytosis/endocytosis machinery as well as signaling pathways. Although we have gained an ever more
Julien eDonnelier +1 more
doaj +1 more source
BiomedicinesBackground: Recently identified Hero proteins, which possess chaperone-like functions, are promising candidates for research into atherosclerosis-related diseases, including ischemic stroke (IS).
Irina Shilenok +4 more
doaj +1 more source