Results 21 to 30 of about 183,487 (307)
The ESX-1 Substrate PPE68 Has a Key Function in ESX-1-Mediated Secretion in Mycobacterium marinum
mBio, 2022 Mycobacteria use specialized type VII secretion systems (T7SSs) to secrete proteins across their diderm cell envelope. One of the T7SS subtypes, named ESX-1, is a major virulence determinant in pathogenic species such as Mycobacterium tuberculosis and ...
Merel P. M. Damen +7 more
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Enzymes as chaperones and chaperones as enzymes
FEBS Letters, 1998 Chaperones and foldases are two groups of accessory proteins which assist maturation of nascent peptides into functional proteins in cells. Protein disulfide isomerase, a foldase, and ATP‐dependent proteases, responsible for degradation of misfolded proteins in cells, both have intrinsic chaperone activities.
Wang, Chih-Chen, Tsou, Chen-Lu
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Chaperones in Neurodegeneration [PDF]
The Journal of Neuroscience, 2015 Cellular protein homeostasis (proteostasis) maintains the integrity of the proteome and includes protein synthesis, folding, oligomerization, and turnover; chaperone proteins assist with all of these processes. Neurons appear to be especially susceptible to failures in proteostasis, and this is now increasingly recognized as a major origin of ...
Lindberg, Iris +5 more
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G3: Genes, Genomes, Genetics, 2017 Accumulation of toxic proteins in neurons has been linked with the onset of neurodegenerative diseases, which in many cases are characterized by altered neuronal function and synapse loss.
Sandeep Raut +5 more
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Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy [PDF]
, 2019 The process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins.
Cappello F. +4 more
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Targeting protein folding in N‐Myc‐driven medulloblastoma
Molecular Oncology, 2023 Selective targeting of N‐Myc‐driven Sonic hedgehog (SHH) medulloblastoma has been a challenge for many years and, despite decades of research, few targeted therapy opportunities exist. Recently, Kuzuoglu‐Ozturk et al.
Gintvile Valinciute, Martine F. Roussel
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Current Opinion in Structural Biology, 2014 The folding and assembly of myosin motor proteins is essential for most movement processes at the cellular, but also at the organism level. Importantly, myosins, which represent a very diverse family of proteins, require the activity of general and specialized folding factors to develop their full motor function.
Hellerschmied, Doris, Clausen, Tim
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Endoplasmic reticulum chaperones and their roles in the immunogenicity of cancer vaccines
Frontiers in Oncology, 2015 The endoplasmic reticulum (ER) is a major site of passage for proteins en route to other organelles, to the cell surface, and to the extracellular space.
Michael William Graner +2 more
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Regulation of CLC-1 chloride channel biosynthesis by FKBP8 and Hsp90β. [PDF]
, 2016 Mutations in human CLC-1 chloride channel are associated with the skeletal muscle disorder myotonia congenita. The disease-causing mutant A531V manifests enhanced proteasomal degradation of CLC-1.
Chen, Shu-Ching +7 more
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Molecular Systems Biology, 2009 Molecular chaperones are known to be involved in many cellular functions, however, a detailed and comprehensive overview of the interactions between chaperones and their cofactors and substrates is still absent.
Yunchen Gong +6 more
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