Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

12.8K
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,...
12.8K
Amyloid Fibrils03:03

Amyloid Fibrils

6.9K
6.9K
Alzheimer's Disease: Overview01:26

Alzheimer's Disease: Overview

2.0K
Alzheimer's Disease (AD) is a continually advancing neurodegenerative disorder, distinguished by escalating memory loss, cognitive dysfunction, and dementia. The disease unfolds in three stages: preclinical, mild cognitive impairment (MCI), and dementia. Its onset is insidious, and the progression gradual, with the cause not well explained by other disorders.
The clinical diagnosis of AD hinges on the presence of memory and other cognitive impairments. Biomarkers, such as changes in Aβ...
2.0K
Neural Regulation01:37

Neural Regulation

44.5K
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.
44.5K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

18.4K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
18.4K
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

3.0K
Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order...
3.0K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Interaction of cytochrome P450 3A4 with the hydrophilic ligand tetraethylene glycol.

Biochemical and biophysical research communications·2025
Same author

Interaction of cytochrome P450 3A4 with cannabinoids and the drug darifenacin.

The Journal of biological chemistry·2025
Same author

Evaluation of Larger Side-Group Functionalities and the Side/End-Group Interplay in Ritonavir-Like Inhibitors of CYP3A4.

Chemical biology & drug design·2025
Same author

Mixed Ru(II)-Ir(III) Complexes as Photoactive Inhibitors of the Major Human Drug Metabolizing Enzyme CYP3A4.

Inorganic chemistry·2024
Same author

Synthesis and anticancer properties of a hybrid molecule with the testosterone and estradiol head-groups.

Steroids·2024
Same author

Interaction of CYP3A4 with the inhibitor cobicistat: Structural and mechanistic insights and comparison with ritonavir.

Archives of biochemistry and biophysics·2024

Related Experiment Video

Updated: Mar 21, 2026

Abbiategrasso Brain Bank Protocol for Collecting, Processing and Characterizing Aging Brains
12:28

Abbiategrasso Brain Bank Protocol for Collecting, Processing and Characterizing Aging Brains

Published on: June 3, 2020

18.4K

Structure/Function Relations in AIFM1 Variants Associated with Neurodegenerative Disorders.

Irina F Sevrioukova1

  • 1Department of Molecular Biology and Biochemistry, University of California, Irvine, CA 92697-3900, USA.

Journal of Molecular Biology
|May 15, 2016
PubMed
Summary

Mutations in the AIFM1 gene cause neurodegenerative disorders. The severity depends on how mutations affect the apoptosis-inducing factor (AIF) protein

Keywords:
NADH bindingapoptosis-inducing factorcrystal structuremitochondrial flavoproteinpathologic mutation

More Related Videos

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models
08:33

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

Published on: March 24, 2019

8.0K
Author Spotlight: Decoding Mitochondrial Aging
08:48

Author Spotlight: Decoding Mitochondrial Aging

Published on: June 30, 2023

5.0K

Related Experiment Videos

Last Updated: Mar 21, 2026

Abbiategrasso Brain Bank Protocol for Collecting, Processing and Characterizing Aging Brains
12:28

Abbiategrasso Brain Bank Protocol for Collecting, Processing and Characterizing Aging Brains

Published on: June 3, 2020

18.4K
Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models
08:33

Characterizing Histone Post-translational Modification Alterations in Yeast Neurodegenerative Proteinopathy Models

Published on: March 24, 2019

8.0K
Author Spotlight: Decoding Mitochondrial Aging
08:48

Author Spotlight: Decoding Mitochondrial Aging

Published on: June 30, 2023

5.0K

Area of Science:

  • Biochemistry
  • Genetics
  • Neuroscience

Background:

  • The X-linked AIFM1 gene encodes mitochondrial apoptosis-inducing factor (AIF), crucial for energy metabolism and programmed cell death.
  • Mutations in AIFM1 are linked to neurodegenerative disorders with variable clinical presentations.

Purpose of the Study:

  • To structurally and functionally characterize four pathological variants of human AIF: V243L, G262S, G308E, and G338E.
  • To correlate the functional impact of these variants with observed clinical phenotypes.

Main Methods:

  • Structural and functional analysis of AIF variants.
  • Assessment of redox properties and mitochondrial respiration.
  • Correlation of molecular findings with clinical data.

Main Results:

  • The G308E variant severely impaired AIF's redox properties and mitochondrial respiration, correlating strongly with clinical phenotype.
  • V243L and G338E variants showed minimal to mild functional changes, suggesting disease onset is linked to reduced cellular expression.
  • AIF G262S exhibited more severe structural and redox alterations than predicted by its clinical phenotype.

Conclusions:

  • Phenotypic variability in AIFM1-related disorders is determined by the specific AIF feature affected (expression, structure, redox, or apoptogenic function) and its extent.
  • Severe neurodegeneration correlates with drastic reductions in AIF expression level and/or redox activity.
  • Less pronounced alterations in AIF function can lead to slowly progressive neurological disorders with a broad clinical spectrum.