Results 51 to 60 of about 3,296,549 (170)
Molecular chaperones and the protein production line
, 1994 The folding of proteins to their active state in the cell, long thought to be a spontaneous process, requires the assistance of other proteins called molecular chaperones.
Lund, Peter A.
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Artificial chaperones: from conventional designs to smart systems
NPG Asia MaterialsChaperones are essential for the functions of many biomacromolecules as they facilitate folding, stabilize conformation, and prevent aggregation.
Wancheng Zhang, Atsushi Maruyama
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The discovery of SycO reveals a new function for type three secretion effector chaperones [PDF]
, 2006 The Type Three Secretion (T3S) system is a device used by many Gram-negative pathogens that allows bacteria to deliver effector proteins straight into the eukaryotic cell cytosol.
Letzelter, Michel
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International Journal of Cell Biology, 2012 It is commonly believed that sustained elevations in the mitochondrial matrix Ca2+ concentration are a major feature of the intracellular cascade of lethal events during cerebral ischemia.
Yi-Bing Ouyang, Rona G. Giffard
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Acta Neuropathologica Communications, 2022 The most common inherited cause of two genetically and clinico-pathologically overlapping neurodegenerative diseases, amyotrophic lateral sclerosis (ALS) and frontotemporal dementia (FTD), is the presence of expanded GGGGCC intronic hexanucleotide ...
Feilin Liu +10 more
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Molecular Chaperones and Co-Chaperones in Parkinson Disease [PDF]
The Neuroscientist, 2012 Parkinson disease, a progressive neurodegenerative disorder, is caused by the pathological accumulation of proteins, including the ubiquitous presynaptic protein α-synuclein. Alterations in the metabolism of α-synuclein have clearly been linked to neurodegeneration, and early steps in the pathological sequence of this protein include the formation of ...
Hemi, Dimant +2 more
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Molecular HorticultureORANGE (OR) family proteins are DnaJE1 molecular chaperones ubiquitous and highly conserved in all plant species, indicating their important roles in plant growth and development.
Emalee Wrightstone +4 more
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Methylglyoxal alters the function and stability of critical components of the protein quality control. [PDF]
PLoS ONE, 2010 BACKGROUND: Increased production and accumulation of methylglyoxal (MGO), as well as increased modification of proteins by glycoxidation, are hallmarks of aging and diabetes.
Carla Figueira Bento +3 more
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How do Chaperones Bind (Partly) Unfolded Client Proteins?
Frontiers in Molecular Biosciences, 2021 Molecular chaperones are central to cellular protein homeostasis. Dynamic disorder is a key feature of the complexes of molecular chaperones and their client proteins, and it facilitates the client release towards a folded state or the handover to ...
Iva Sučec +3 more
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Applied Sciences, 2021 The chaperone (or chaperoning) system (CS) constitutes molecular chaperones, co-chaperones, and chaperone co-factors, interactors and receptors, and its canonical role is protein quality control.
Federica Scalia +5 more
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