Jove
Visualize
联系我们
JoVE
x logofacebook logolinkedin logoyoutube logo
关于 JoVE
概览领导团队博客JoVE 帮助中心
作者
出版流程编辑委员会范围与政策同行评审常见问题投稿
图书馆员
用户评价订阅访问资源图书馆顾问委员会常见问题
研究
JoVE JournalMethods CollectionsJoVE Encyclopedia of Experiments存档
教育
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab Manual教师资源中心教师网站
使用条款与条件
隐私政策
政策

相关概念视频

Neural Regulation01:37

Neural Regulation

40.2K
Digestion begins with a cephalic phase that prepares the digestive system to receive food. When our brain processes visual or olfactory information about food, it triggers impulses in the cranial nerves innervating the salivary glands and stomach to prepare for food.
40.2K
Amyloid Fibrils03:03

Amyloid Fibrils

9.9K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.9K
Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

2.4K
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...
2.4K
The Proteasome01:13

The Proteasome

1.2K
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...
1.2K

您也可能阅读

相关文章

通过共同作者、期刊和引用图与本文相关的文章。

排序
Same author

Trends in Postmenstrual Age at Discharge and Predictive Factors Among a Contemporary Cohort of Infants Born Preterm.

The Journal of pediatrics·2026
Same authorSame journal

PERK deficiency amplifies molecular, structural, and network vulnerability to repetitive mild traumatic brain injury.

Neurobiology of disease·2026
Same author

Robust tauopathy and memory deficits in a mouse model constitutively overexpressing human P301L MAPT.

Neurobiology of disease·2026
Same author

The Biological Fate of DBS Leads After 15 Years of Stimulation.

Movement disorders clinical practice·2026
Same author

Drivers of Research Participation Among Racially and Ethnically Underrepresented Women: Insights from Semi-Structured Interviews.

Journal of racial and ethnic health disparities·2026
Same author

Length of gestation and postpartum visit attendance.

Pregnancy (Hoboken, N.J.)·2026

相关实验视频

Updated: Sep 15, 2025

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons
10:03

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

10.7K

病理性α-synuclein扰乱了核完整性的核心.

Michael Millett1, Allison Comite1, Elisabeth Martin Castosa1

  • 1Department of Pharmacology & Therapeutics and Center for Translational Research in Neurodegeneration, University of Florida College of Medicine, Gainesville, FL 32610, United States of America.

Neurobiology of disease
|July 16, 2025
PubMed
概括

脑细胞核中的病理性α-synuclein (α-synuclein) 聚合物,在像Lewy体痴呆症这样的synucleinopathies中观察到,破坏核功能和完整性,导致DNA损伤和增加毒素敏感性.

关键词:
拉米诺病症是一种拉米诺病.莱维体痴呆症 (Lewy体痴呆症) 是一种疾病.核功能障碍 核功能障碍 核功能障碍 核功能障碍α-synuclein 是一种同核蛋白.

更多相关视频

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

17.5K
Technique for Intranasal Administration of α-Synuclein Aggregates
04:49

Technique for Intranasal Administration of α-Synuclein Aggregates

Published on: November 8, 2024

579

相关实验视频

Last Updated: Sep 15, 2025

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons
10:03

Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

Published on: August 16, 2020

10.7K
Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains
09:27

Sequential Extraction of Soluble and Insoluble Alpha-Synuclein from Parkinsonian Brains

Published on: January 5, 2016

17.5K
Technique for Intranasal Administration of α-Synuclein Aggregates
04:49

Technique for Intranasal Administration of α-Synuclein Aggregates

Published on: November 8, 2024

579

科学领域:

  • 神经科学是一个神经科学.
  • 分子生物学分子生物学
  • 细胞生物学 细胞生物学

背景情况:

  • 包括莱维体痴呆症在内的同核素病变,以病态的α-synuclein聚合物为特征.
  • 阿尔法-同核素在核功能中的确切作用仍然存在争议,并未被充分理解.
  • 新出现的证据表明,α-synuclein在突触调节中起作用,但其核存在和影响尚不清楚.

研究的目的:

  • 研究病理性α-synuclein在synucleinopathy模型和人体组织中的核定位.
  • 确定核α-synuclein积累对核完整性和功能的下游影响.
  • 阐明核α-synuclein在疾病发病过程中的作用.

主要方法:

  • 采用了突变核蛋白病变的小鼠和细胞培养模型,以及死后的利维体痴呆症人类大脑组织.
  • 使用定量超分辨率显微镜可视化核区内的α-synuclein定位.
  • 评估了核形态,DNA损伤标记 (53BP1),核外完整性,RNA定位,以及对核毒素的敏感性.

主要成果:

  • 病理性α-synuclein聚合物在小鼠模型和人类Lewy Body Dementia皮质的核内观察到.
  • 核α-synuclein积累与受影响组织中异常的核形态相关.
  • 在具有核α-synuclein的synucleinopathy模型中观察到高的DNA损伤标志物,核包膜损伤和改变的RNA局部化.

结论:

  • 这项研究使用先进显微镜严格证明了病理性α-synuclein的核定位.
  • 病理性α-synuclein的核积累破坏了核完整性和功能,导致疾病病理.
  • 这些发现提供了关于核α-synuclein在synucleinopathies中有害影响的新见解.