関連する実験動画

Updated: Aug 1, 2026

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates
11:49

A Novel Saturation Mutagenesis Approach: Single Step Characterization of Regulatory Protein Binding Sites in RNA Using Phosphorothioates

Published on: August 21, 2018

pp60v-srcの36キロダルトンの基板は,変換に敏感な方法でミリスチル化されます

J Soric, J A Gordon

    Science (New York, N.Y.)
    |November 1, 1985
    PubMed
    まとめ

    pp60v-srcキナーゼの基質である36kDのタンパク質は,アミド結合を通じてミリスティック酸で改変されます. このミリストイレーションは,ロース・サルコマウイルスに変異した細胞で減少する.

    さらに関連する動画

    Small-Scale Plasma Membrane Preparation for the Analysis of Candida albicans Cdr1-mGFPHis09:44

    Small-Scale Plasma Membrane Preparation for the Analysis of Candida albicans Cdr1-mGFPHis

    Published on: June 13, 2021

    Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates09:47

    Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates

    Published on: May 10, 2022

    関連する概念動画

    Covalently Linked Protein Regulators02:04

    Covalently Linked Protein Regulators

    Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
    These groups modify specific amino acids in a protein.
    Leaky Scanning02:28

    Leaky Scanning

    During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R stands for...
    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...
    Insertion of Single-pass Transmembrane Proteins in the RER01:26

    Insertion of Single-pass Transmembrane Proteins in the RER

    Integral membrane proteins are proteins adhered to the lipid bilayer of a cell organelle or membrane. They can be of two types: transmembrane integral proteins that span the lipid bilayer and monotopic proteins that are attached to either side of the membrane but do not pass through it.
    Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
    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...