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関連する概念動画

Pinocytosis00:43

Pinocytosis

62.7K
Cells use energy-requiring bulk transport mechanisms to transfer large particles, or large amounts of small particles, into or out of the cell. The cells envelop the particles in spherical membranes called vesicles or vacuoles. Vesicles that transport material into the cell are built from the cell membrane. These vesicles encapsulate external molecules and transport them into the cell in a process called endocytosis.
62.7K
Protein Transport into the Inner Mitochondrial Membrane01:34

Protein Transport into the Inner Mitochondrial Membrane

3.5K
Nuclear encoded mitochondrial precursors are imported to the inner membrane in a multistep process involving two separate translocons, TIM22 and TIM23. TIM23 is a cation-selective pore that remains closed by the N terminal segment of the protein. Negative charges on the TIM23 act as a receptor for the incoming precursor, pulling the positively charged matrix-targeting sequence for peptide insertion and translocation.
Transport of mitochondrial precursors across the TIM23 channel is driven by...
3.5K
Protein Transport to the Stroma01:24

Protein Transport to the Stroma

1.5K
Chloroplasts are triple membrane structures with an outer membrane, an inner membrane, and a thylakoid membrane, each containing distinct metabolite transporters, membrane translocons, and enzymes. Appropriate sorting and translocating these proteins to their correct membrane systems is essential for chloroplast function.
Protein complexes called the translocon of the outer chloroplast membrane or TOC complex, and the translocon of the inner chloroplast membrane or TIC complex mediate the...
1.5K
Protein Transport to the Outer Chloroplast Membrane01:11

Protein Transport to the Outer Chloroplast Membrane

1.6K
Chloroplast outer membrane proteins encoded by the nucleus are synthesized in the cytosol. Soon after synthesis, they bind cytosolic factors such as 14-3-3 protein and the Hsp70 chaperones that keep these precursors in an unfolded state until their translocation.
Two models describe the mechanism of precursor recognition and entry across the outer membrane through the TOC complex. Model 1 suggests the newly synthesized precursor binds to the TOC receptor 159 and forms a complex.
1.6K
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

4.4K
Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
4.4K
Protein Transport to the Inner Chloroplast Membrane01:18

Protein Transport to the Inner Chloroplast Membrane

1.7K
Proteins targeted to the inner chloroplast membrane, or plastid proteins, are transported by two general pathways: the stop-transfer and the re-insertion or post-import pathways. Most plastid proteins carry N-terminal transit sequences and internal import sequences targeting it to the specific chloroplast subcompartment. Proteins targeted by the stop-transfer pathway have internal hydrophobic sequences that inhibit their translocation into the stroma. As a result, these precursors are arrested...
1.7K

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関連する実験動画

Updated: May 5, 2026

Using Caco-2 Cells to Study Lipid Transport by the Intestine
07:00

Using Caco-2 Cells to Study Lipid Transport by the Intestine

Published on: August 20, 2015

18.9K

細胞タンパク質の折りたたみにおける分子チャペロン.

F U Hartl1

  • 1Howard Hughes Medical Institute, Memorial Sloan-Kettering Cancer Center, New York 10021, USA.

Nature
|June 13, 1996
PubMed
まとめ

分子チャペロンは,細胞内のタンパク質構造の誤折れを防止する不可欠なタンパク質です. Hsp70とチャペロニン系はATPに依存するメカニズムを使用して,特にストレス下では,タンパク質の折り畳みを支援します.

科学分野:

  • 細胞生物学 細胞生物学
  • バイオケミストリー バイオケミストリー
  • タンパク質の折りたたみ

背景:

  • 新しく合成されたタンパク質は,細胞内で適切に折りたたむために助けを必要とします.
  • 分子チャペロンは,タンパク質の誤折り防止に不可欠な保存されたタンパク質です.
  • 熱ショックなどの細胞ストレスは,タンパク質の誤折り合いのリスクを高めます.

研究 の 目的:

  • タンパク質の折りたたみにおける分子チャペロンメカニズムの理解を要約する.
  • Hsp70とチャペロニンファミリーの役割を強調する.
  • 新しいポリペプチド鎖を支援するチャペロンの協力的機能を記述する.

主な方法:

  • 分子チャペロンに関する既存の文献のレビュー.
  • ATPに依存するメカニズムの分析.
  • タンパク質の折りたたみにおけるチャペロン協力の検討.

主要な成果:

  • 分子チャペロンは,正常およびストレス条件下でのタンパク質構造の誤折れを防止します.
  • Hsp70とチャペロニン系は,タンパク質の折りたたみのためにATPに依存するメカニズムを使用します.

さらに関連する動画

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

10.6K

関連する実験動画

Last Updated: May 5, 2026

Using Caco-2 Cells to Study Lipid Transport by the Intestine
07:00

Using Caco-2 Cells to Study Lipid Transport by the Intestine

Published on: August 20, 2015

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Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution
11:55

Membrane Transport Processes Analyzed by a Highly Parallel Nanopore Chip System at Single Protein Resolution

Published on: August 16, 2016

11.4K
Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
10:26

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

10.6K
  • これらのチャペロンファミリーは協力して,新しいポリペプチド鎖の折りたたみを促進することができます.
  • 結論:

    • 分子チャペロンは,プロテオスタシスの維持に不可欠です.
    • ATPに依存するメカニズムは,シェーパロン機能の中心にある.
    • シェーパーロンの協同作用は,タンパク質の折りたたみにおける彼らの効率を高めます.