Results 61 to 70 of about 232,488 (209)

Identification of ERAD-dependent degrons for the endoplasmic reticulum lumen

open access: yeseLife
Degrons are minimal protein features that are sufficient to target proteins for degradation. In most cases, degrons allow recognition by components of the cytosolic ubiquitin proteasome system.
Rachel Sharninghausen   +3 more
doaj   +1 more source

Understanding the mammalian TRAP complex function(s) [PDF]

open access: yesOpen Biology, 2020
In eukaryotic cells, about one-third of the synthesized proteins are translocated into the endoplasmic reticulum; they are membrane or lumen resident proteins and proteins direct to the Golgi apparatus.
Antonietta Russo
doaj   +1 more source

Endoplasmic reticulum involvement in yeast cell death [PDF]

open access: yes, 2012
Yeast cells undergo programed cell death (PCD) with characteristic markers associated with apoptosis in mammalian cells including chromatin breakage, nuclear fragmentation, reactive oxygen species generation, and metacaspase activation.
Austriaco, Nicanor
core   +3 more sources

Specificity and Regulation of the Endoplasmic Reticulum‐Associated Degradation Machinery [PDF]

open access: yesTraffic, 2013
The endoplasmic reticulum‐associated degradation (ERAD) machinery selects native and misfolded polypeptides for dislocation across the ER membrane and proteasomal degradation. Regulated degradation of native proteins is an important aspect of cell physiology. For example, it contributes to the control of lipid biosynthesis, calcium homeostasis and ERAD
Merulla Jessica   +5 more
openaire   +2 more sources

Crosstalk between the ribosome quality control‐associated E3 ubiquitin ligases LTN1 and RNF10

open access: yesFEBS Letters, EarlyView.
Loss of the E3 ligase LTN1, the ubiquitin‐like modifier UFM1, or the deubiquitinating enzyme UFSP2 disrupts endoplasmic reticulum–ribosome quality control (ER‐RQC), a pathway that removes stalled ribosomes and faulty proteins. This disruption may trigger a compensatory response to ER‐RQC defects, including increased expression of the E3 ligase RNF10 ...
Yuxi Huang   +8 more
wiley   +1 more source

Structural biology of ferritin nanocages

open access: yesFEBS Letters, EarlyView.
Ferritin is a conserved iron‐storage protein that sequesters iron as a ferric mineral core within a nanocage, protecting cells from oxidative damage and maintaining iron homeostasis. This review discusses ferritin biology, structure, and function, and highlights recent cryo‐EM studies revealing mechanisms of ferritinophagy, cellular iron uptake, and ...
Eloise Mastrangelo, Flavio Di Pisa
wiley   +1 more source

Endoplasmic reticulum stress in lung cancer

open access: yesFrontiers in Oncology
Endoplasmic reticulum is the primary site of eukaryotic cells involved in biosynthesis, lipid metabolism, glucose metabolism, protein folding and secretion.
Donghuan Zhang   +6 more
doaj   +1 more source

Traffic into silence: endomembranes and post-transcriptional RNA silencing. [PDF]

open access: yes, 2014
microRNAs (miRNAs) and small interfering RNAs (siRNAs) are small RNAs that repress gene expression at the post-transcriptional level in plants and animals. Small RNAs guide Argonaute-containing RNA-induced silencing complexes to target RNAs in a sequence-
Chen, Xuemei   +2 more
core   +3 more sources

Potential therapeutic targeting of BKCa channels in glioblastoma treatment

open access: yesMolecular Oncology, EarlyView.
This review summarizes current insights into the role of BKCa and mitoBKCa channels in glioblastoma biology, their potential classification as oncochannels, and the emerging pharmacological strategies targeting these channels, emphasizing the translational challenges in developing BKCa‐directed therapies for glioblastoma treatment.
Kamila Maliszewska‐Olejniczak   +4 more
wiley   +1 more source

Molecular Approaches to the Treatment, Prophylaxis, and Diagnosis of Alzheimer’s Disease: Possible Involvement of HRD1, a Novel Molecule Related to Endoplasmic Reticulum Stress, in Alzheimer’s Disease

open access: yesJournal of Pharmacological Sciences, 2012
Endoplasmic reticulum (ER)-associated degradation (ERAD) is a protective mechanism against ER stress in which unfolded proteins accumulated in the ER are selectively transported to the cytosol for degradation by the ubiquitin–proteasome system. We cloned
Masayuki Kaneko   +2 more
doaj   +1 more source

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