相关实验视频

Updated: Jan 16, 2026

Label-Free Imaging of Lipid Storage Dynamics in Caenorhabditis elegans using Stimulated Raman Scattering Microscopy
10:59

Label-Free Imaging of Lipid Storage Dynamics in Caenorhabditis elegans using Stimulated Raman Scattering Microscopy

Published on: May 28, 2021

4.7K

解读脂质和对ER信号网络,ERSU,UPR和ERAD的影响

Xia Li, Maho Niwa

    bioRxiv : the preprint server for biology
    |September 26, 2025
    PubMed
    概括

    脂质平衡对于酵母体内质网膜 (ER) 遗传至关重要. 保持适当的脂质稳定整合了ER压力检查点,确保了ER传输和细胞在压力下存活.

    更多相关视频

    Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons10:50

    Molecular Modulation by Lentivirus-Delivered Specific shRNAs in Endoplasmic Reticulum Stressed Neurons

    Published on: April 24, 2021

    1.3K
    Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer10:36

    Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer

    Published on: March 17, 2016

    10.9K

    相关概念视频

    Assembly of the Lipid Bilayer in the ER01:28

    Assembly of the Lipid Bilayer in the ER

    Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
    A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
    4.0K
    Regulation of the Unfolded Protein Response01:31

    Regulation of the Unfolded Protein Response

    Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
    2.9K
    The Unfolded Protein Response01:37

    The Unfolded Protein Response

    The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
    6.2K
    Smooth Endoplasmic Reticulum01:21

    Smooth Endoplasmic Reticulum

    Smooth endoplasmic reticulum or smooth ER is a sub-organelle with specialized functions in animal cells and plant cells. It is often associated with the tubule morphology of the endoplasmic reticulum.
    The ER provides optimal conditions for synthesizing steroid hormones and lipids, such as phospholipids and triglycerides. Traditionally, lipid metabolism was considered to be a smooth ER function. However, there is no direct evidence to prove that rough ER is completely excluded from lipid...
    7.8K
    Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal01:22

    Role of Ephrin-Eph Signalling in Intestinal Stem Cell Renewal

    Erythropoietin-producing hepatocellular carcinoma receptor (Eph) and its ligand, Eph receptor-interacting protein (Ephrin) were first discovered in the human carcinoma cell line, hence the name. Ephrin-Eph interaction guides cells to reach their appropriate location in adult tissues. They also play an essential role in the immune system by helping in immune cell migration, adhesion, and activation. Based on their structure and function, Eph is divided into two classes — EphA and EphB.
    2.6K
    The Endoplasmic Reticulum01:43

    The Endoplasmic Reticulum

    The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
    21.0K