Related Experiment Video

Updated: Aug 18, 2026

Ovariectomy and 17β-estradiol Replacement in Rats and Mice: A Visual Demonstration
06:51

Ovariectomy and 17β-estradiol Replacement in Rats and Mice: A Visual Demonstration

Published on: June 7, 2012

[Estradiol-induced formation of the polyribosomal complex synthesizing ceruloplasmin in rats]

O V Voronina, N K Monakhov

    Biokhimiia (Moscow, Russia)
    |June 1, 1980
    PubMed

    More Related Videos

    Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells10:24

    Visualization of Endoplasmic Reticulum Localized mRNAs in Mammalian Cells

    Published on: December 17, 2012

    An In Vivo Estrogen Deficiency Mouse Model for Screening Exogenous Estrogen Treatments of Cardiovascular Dysfunction After Menopause06:18

    An In Vivo Estrogen Deficiency Mouse Model for Screening Exogenous Estrogen Treatments of Cardiovascular Dysfunction After Menopause

    Published on: August 13, 2019

    Related Concept Videos

    Ribosomal RNA Synthesis02:53

    Ribosomal RNA Synthesis

    Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
    Ribosome biogenesis begins with the synthesis of 5S and 45S pre-rRNAs by distinct RNA polymerases. The primary transcripts are extensively processed and modified before they are bound and folded by ribosomal proteins and assembly factors,...
    Regulation of Nuclear Protein Sorting01:45

    Regulation of Nuclear Protein Sorting

    Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
    Directing Proteins to the Rough Endoplasmic Reticulum01:34

    Directing Proteins to the Rough Endoplasmic Reticulum

    The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
    Protein Modifications in the RER01:26

    Protein Modifications in the RER

    Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
    Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
    Post-translational Translocation of Proteins to the RER01:27

    Post-translational Translocation of Proteins to the RER

    A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
    Targeting proteins to the ER
    Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
    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...