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Published in 2019 at "Journal of molecular biology"
DOI: 10.1016/j.jmb.2019.04.026
Abstract: During disease, cells experience various stresses that manifest as an accumulation of misfolded proteins and eventually lead to cell death. To combat this stress, cells activate a pathway called unfolded protein response that functions to…
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Keywords:
disease;
ampylation;
parkinson disease;
alpha synuclein ... See more keywords
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Published in 2021 at "Trends in microbiology"
DOI: 10.1016/j.tim.2021.08.003
Abstract: AMPylation, a post-translational modification (PTM) first discovered in the late 1960s, is catalyzed by adenosine monophosphate (AMP)-transferring enzymes. The observation that filamentation-induced-by-cyclic-AMP (fic) enzymes are associated with this unique PTM revealed that AMPylation plays a…
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Keywords:
fic enzymes;
ampylation;
lens fic;
revisiting ampylation ... See more keywords
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Published in 2021 at "Nature Communications"
DOI: 10.1038/s41467-021-22596-0
Abstract: To adapt to fluctuating protein folding loads in the endoplasmic reticulum (ER), the Hsp70 chaperone BiP is reversibly modified with adenosine monophosphate (AMP) by the ER-resident Fic-enzyme FICD/HYPE. The structural basis for BiP binding and…
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Keywords:
tpr motifs;
chaperone bip;
motifs ficd;
ampylation ... See more keywords
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Published in 2021 at "Open Biology"
DOI: 10.1098/rsob.210009
Abstract: Protein AMPylation refers to the covalent attachment of an AMP moiety to the amino acid side chains of target proteins using ATP as nucleotide donor. This process is catalysed by dedicated AMP transferases, called AMPylases.…
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Keywords:
protein ampylation;
ampylases protein;
fic non;
ampylation ... See more keywords
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Published in 2022 at "Cold Spring Harbor perspectives in biology"
DOI: 10.1101/cshperspect.a041265
Abstract: The endoplasmic reticulum (ER)-localized Hsp70 chaperone, BiP, undergoes a rapid, reversible and inactivating post-translational modification. This covalent modification complements the slower, conventional unfolded protein response (UPR) in matching the supply of active Hsp70 chaperone to…
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Keywords:
endoplasmic reticulum;
protein folding;
bip;
ampylation ... See more keywords
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2
Published in 2023 at "EMBO Molecular Medicine"
DOI: 10.15252/emmm.202216491
Abstract: Dysfunction of the endoplasmic reticulum (ER) in insulin‐producing beta cells results in cell loss and diabetes mellitus. Here we report on five individuals from three different consanguineous families with infancy‐onset diabetes mellitus and severe neurodevelopmental…
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Keywords:
endoplasmic reticulum;
onset diabetes;
infancy onset;
bip ... See more keywords
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Published in 2023 at "Frontiers in Chemistry"
DOI: 10.3389/fchem.2023.1077188
Abstract: DeAMPylation, as a reversible reaction of AMPylation and mediated by the endoplasmic reticulum-localized enzyme FICD (filamentation induced by cAMP domain protein, also known as HYPE), is an important process in protein posttranslational modifications (PTMs). Elucidating…
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Keywords:
deampylation;
assistant forms;
ampylation;
inhibitory assistant ... See more keywords