Articles with "misfolded proteins" as a keyword



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Prevalence and Clinical Phenotype of Quadruple Misfolded Proteins in Older Adults.

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Published in 2020 at "JAMA neurology"

DOI: 10.1001/jamaneurol.2020.1741

Abstract: Importance Quadruple misfolded proteins (tau neurofibrillary tangles, amyloid-β [Aβ], α-synuclein, and transactive response DNA-binding protein 43 [TDP-43]) in the same brain are relatively common in aging. However, the clinical presentation, associated factors, frequency in community-based… read more here.

Keywords: death; misfolded proteins; quadruple misfolded; disease ... See more keywords
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ER-to-Lysosome Associated Degradation (ERLAD) in a Nutshell: mammalian, yeast and plant ER-phagy as induced by misfolded proteins.

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Published in 2023 at "FEBS letters"

DOI: 10.1002/1873-3468.14674

Abstract: Conserved catabolic pathways operate to remove aberrant polypeptides from the endoplasmic reticulum (ER), the major biosynthetic organelle of eukaryotic cells. The best known are the ER-associated degradation (ERAD) pathways that control retro-translocation of terminally misfolded… read more here.

Keywords: lysosome associated; associated degradation; mammalian yeast; misfolded proteins ... See more keywords
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Harnessing Oncolytic Extracellular Vesicles for Tumor Cell-Preferential Cytoplasmic Delivery of Misfolded Proteins for Cancer Immunotherapy.

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Published in 2023 at "Small"

DOI: 10.1002/smll.202300527

Abstract: In this study, extracellular vesicles (EVs) are reimagined as more than just a cellular waste disposal system and are repurposed for cancer immunotherapy. Potent oncolytic EVs (bRSVF-EVs) loaded with misfolded proteins (MPs) are engineered, which… read more here.

Keywords: extracellular vesicles; misfolded proteins; tumor; delivery ... See more keywords
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The Cdc48 Complex Alleviates the Cytotoxicity of Misfolded Proteins by Regulating Ubiquitin Homeostasis.

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Published in 2020 at "Cell reports"

DOI: 10.1016/j.celrep.2020.107898

Abstract: The accumulation of misfolded proteins is associated with multiple neurodegenerative disorders, but it remains poorly defined how this accumulation causes cytotoxicity. Here, we demonstrate that the Cdc48/p97 segregase machinery drives the clearance of ubiquitinated model… read more here.

Keywords: misfolded proteins; cdc48; cdc48 deficiency; cdc48 complex ... See more keywords
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Hsp70 Trap Assay for Detection of Misfolded Subproteome Related to Myelodysplastic Syndromes.

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Published in 2019 at "Analytical chemistry"

DOI: 10.1021/acs.analchem.9b04175

Abstract: The onset and progression of numerous serious diseases (e.g. various types of malignancies, neurodegenerative diseases, and cardiac diseases) are, on a molecular level, associated with protein modifications and misfolding. Current methods for the detection of… read more here.

Keywords: myelodysplastic syndromes; detection; misfolded proteins; hsp70 trap ... See more keywords

ER-misfolded proteins become sequestered with mitochondria and impair mitochondrial function

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Published in 2021 at "Communications Biology"

DOI: 10.1038/s42003-021-02873-w

Abstract: Proteostasis is a challenge for cellular organisms, as all known protein synthesis machineries are error-prone. Here we show by cell fractionation and microscopy studies that misfolded proteins formed in the endoplasmic reticulum can become associated… read more here.

Keywords: misfolded proteins; sequestered mitochondria; mitochondrial function; become sequestered ... See more keywords
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Spatial sequestration of misfolded proteins in neurodegenerative diseases.

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Published in 2022 at "Biochemical Society transactions"

DOI: 10.1042/bst20210862

Abstract: Properly folded, functional proteins are essential for cell health. Cells sustain protein homeostasis, or proteostasis, via protein quality control (PQC) mechanisms. It is currently hypothesized that a breakdown in proteostasis during ageing leads to the… read more here.

Keywords: pqc compartments; sequestration; misfolded proteins; sequestration misfolded ... See more keywords
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Human pregnancy zone protein stabilizes misfolded proteins including preeclampsia- and Alzheimer’s-associated amyloid beta peptide

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Published in 2019 at "Proceedings of the National Academy of Sciences of the United States of America"

DOI: 10.1073/pnas.1817298116

Abstract: Significance Pregnancy is a unique physiological state involving biological stresses that promote protein damage (misfolding) within the maternal body. Currently, little is known regarding how the maternal body copes with elevated protein misfolding in pregnancy.… read more here.

Keywords: pregnancy; misfolded proteins; zone protein; pzp ... See more keywords
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Proper protein folding in the endoplasmic reticulum is required for attachment of a glycosylphosphatidylinositol anchor in plants.

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Published in 2021 at "Plant physiology"

DOI: 10.1093/plphys/kiab181

Abstract: Endoplasmic reticulum (ER) quality control processes recognize and eliminate misfolded proteins to maintain cellular protein homeostasis and prevent the accumulation of defective proteins in the secretory pathway. Glycosylphosphatidylinositol (GPI)-anchored proteins carry a glycolipid modification which… read more here.

Keywords: protein; gpi anchor; misfolded proteins; endoplasmic reticulum ... See more keywords
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PDE1 inhibition facilitates proteasomal degradation of misfolded proteins and protects against cardiac proteinopathy

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Published in 2019 at "Science Advances"

DOI: 10.1126/sciadv.aaw5870

Abstract: PDE1 inhibition enhances the proteasome and protects against proteinopathy and heart failure with preserved ejection fraction. No current treatment targets cardiac proteotoxicity or can reduce mortality of heart failure (HF) with preserved ejection fraction (HFpEF).… read more here.

Keywords: misfolded proteins; degradation misfolded; pde1 inhibition; inhibition ... See more keywords
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Abstract 4815: TMEM9 decreases ER stress-induced misfolded proteins via lysosomal protein degradation

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Published in 2023 at "Cancer Research"

DOI: 10.1158/1538-7445.am2023-4815

Abstract: The endoplasmic reticulum (ER) contributes to various protein modifications such as protein folding. Also, the ER-associated degradation (ERAD) complex removes defective proteins, which prevents the accumulation of misfolded proteins to avoid abnormality of physiological activity.… read more here.

Keywords: lysosomal protein; misfolded proteins; protein degradation; degradation ... See more keywords