Results 21 to 30 of about 110,947 (209)
Frontiers in Molecular Biosciences, 2022 As part of their life-cycle, malaria parasites undergo rapid cell multiplication and division, with one parasite giving rise to over 20 new parasites within the course of 48 h.
Julian Barth +2 more
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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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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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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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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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Frontiers in Molecular Neuroscience, 2017 Heat shock proteins (Hsps) are ubiquitously expressed chaperone proteins that enable cells to cope with environmental stresses that cause misfolding and denaturation of proteins.
Bernadett Kalmar +2 more
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Redefining Molecular Chaperones as Chaotropes [PDF]
, 2021 Molecular chaperones are the key instruments of bacterial protein homeostasis. Chaperones not only facilitate folding of client proteins, but also transport them, prevent their aggregation, dissolve aggregates and resolve misfolded states.
Macošek, Jakub +2 more
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