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関連する概念動画

Protein Digestion01:02

Protein Digestion

85.5K
Protein digestion begins in the stomach, where the highly acidic environment can easily disrupt protein structure by exposing the peptide bonds of polypeptide chains. After polypeptide chains are broken into individual amino acids by a series of digestive enzymes, the amino acids are transported to the liver via the bloodstream to produce energy.
85.5K
The Proteasome02:18

The Proteasome

7.7K
Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
2.9K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

4.3K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

2.8K
Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult...
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The Proteasome01:13

The Proteasome

1.6K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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Demonstration of Proteolytic Activation of the Epithelial Sodium Channel ENaC by Combining Current Measurements with Detection of Cleavage Fragments
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Demonstration of Proteolytic Activation of the Epithelial Sodium Channel ENaC by Combining Current Measurements with Detection of Cleavage Fragments

Published on: July 5, 2014

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プロエンケファリンの処理は組織特異的です.

D Liston, G Patey, J Rossier

    Science (New York, N.Y.)
    |August 17, 1984
    PubMed
    まとめ
    この要約は機械生成です。

    プロエンケファリンなどのニューロペプチド前駆体は,酵素によって処理されます. この研究は,プロエンケファリンの成熟のために,視床下部と副腎髄の異なる酵素経路を明らかにし,異なるペプチド製品を生成します.

    さらに関連する動画

    Processing of Human Cardiac Tissue Toward Extracellular Matrix Self-assembling Hydrogel for In Vitro and In Vivo Applications
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    Analysis of Transforming Growth Factor &#223; Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos
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    Demonstration of Proteolytic Activation of the Epithelial Sodium Channel ENaC by Combining Current Measurements with Detection of Cleavage Fragments
    08:56

    Demonstration of Proteolytic Activation of the Epithelial Sodium Channel ENaC by Combining Current Measurements with Detection of Cleavage Fragments

    Published on: July 5, 2014

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    Processing of Human Cardiac Tissue Toward Extracellular Matrix Self-assembling Hydrogel for In Vitro and In Vivo Applications
    08:41

    Processing of Human Cardiac Tissue Toward Extracellular Matrix Self-assembling Hydrogel for In Vitro and In Vivo Applications

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    Analysis of Transforming Growth Factor &#223; Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos
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    Analysis of Transforming Growth Factor ß Family Cleavage Products Secreted Into the Blastocoele of Xenopus laevis Embryos

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    科学分野:

    • 神経科学は神経科学である.
    • バイオケミストリー バイオケミストリー
    • 分子生物学は分子生物学である.

    背景:

    • 神経ペプチドは,大きな前駆体タンパク質から派生した重要なシグナル伝達分子です.
    • これらの前駆体から活性ペプチドへのタンパク質分解処理は不可欠ですが,機械的には不明です.
    • ニューロペプチドの処理を理解することは,ニューラル通信の解読の鍵です.

    研究 の 目的:

    • プロエンケファリン前駆体タンパク質加工の酵素メカニズムを調査する.
    • 2つの異なる牛の組織におけるプロエンケファリンの処理を比較するために: 視床下部と副腎髄.
    • ニューロペプチド成熟経路における組織特有の違いを特定する.

    主な方法:

    • 高分子量エンケファリンを含むペプチドの比較分析.
    • 牛の視床下部と副腎髄の抽出物における前駆体処理の生化学的特徴.
    • ニューロペプチド生物合成におけるプロテオリティックイベントの調査.

    主要な成果:

    • 高分子量エンケファリンを含むペプチドが,下垂体と副腎中枢に蓄積する点で有意な差異が観察されました.
    • これらの異なるペプチドプロファイルは,プロエンケファリンの前駆体に対する異なる酵素処理を示唆しています.
    • 少なくとも2つの異なるプロエンケファリン処理経路の証拠が特定されました.

    結論:

    • 神経ペプチド前駆体プロエンケファリンの処理は組織特異的です.
    • 異なる酵素メカニズムは,下垂体と副腎髄で作用し,異なる成熟したエンケファリンペプチドにつながります.
    • これは,神経ペプチド生物合成の複雑性と組織特異的な調節を強調しています.