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Prediction of localization and interactions of apoptotic proteins
M. Vařecha, M. Zimmermann, J. Amrichová, V. Ulman, P. Matula, M. Kozubek
Language English Country Great Britain
Document type Research Support, Non-U.S. Gov't
NLK
BioMedCentral
from 2008-12-01
BioMedCentral Open Access
from 2009
Directory of Open Access Journals
from 2009
Free Medical Journals
from 2009
PubMed Central
from 2009
Europe PubMed Central
from 2009
ProQuest Central
from 2009-01-01
Open Access Digital Library
from 2009-01-01
Open Access Digital Library
from 2009-01-01
Medline Complete (EBSCOhost)
from 1998-01-01
Health & Medicine (ProQuest)
from 2009-01-01
ROAD: Directory of Open Access Scholarly Resources
from 1994
Springer Nature OA/Free Journals
from 2008-12-01
- MeSH
- Apoptosis MeSH
- Models, Biological MeSH
- Endonucleases MeSH
- Microscopy, Fluorescence methods MeSH
- Caspases metabolism MeSH
- Protein Conformation MeSH
- Humans MeSH
- Models, Molecular MeSH
- Cell Line, Tumor MeSH
- Computer Simulation MeSH
- Proteomics methods MeSH
- Software MeSH
- Protein Structure, Tertiary MeSH
- Protein Binding MeSH
- Computational Biology methods MeSH
- Check Tag
- Humans MeSH
- Publication type
- Research Support, Non-U.S. Gov't MeSH
During apoptosis several mitochondrial proteins are released. Some of them participate in caspase-independent nuclear DNA degradation, especially apoptosis-inducing factor (AIF) and endonuclease G (endoG). Another interesting protein, which was expected to act similarly as AIF due to the high sequence homology with AIF is AIF-homologous mitochondrion-associated inducer of death (AMID). We studied the structure, cellular localization, and interactions of several proteins in silico and also in cells using fluorescent microscopy. We found the AMID protein to be cytoplasmic, most probably incorporated into the cytoplasmic side of the lipid membranes. Bioinformatic predictions were conducted to analyze the interactions of the studied proteins with each other and with other possible partners. We conducted molecular modeling of proteins with unknown 3D structures. These models were then refined by MolProbity server and employed in molecular docking simulations of interactions. Our results show data acquired using a combination of modern in silico methods and image analysis to understand the localization, interactions and functions of proteins AMID, AIF, endonuclease G, and other apoptosis-related proteins.
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- $a Centre for Biomedical Image Analysis, Faculty of Informatics, Masaryk University, Botanicka 68a, Brno 60200, Czech Republic. mvara@fi.muni.cz
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- $a During apoptosis several mitochondrial proteins are released. Some of them participate in caspase-independent nuclear DNA degradation, especially apoptosis-inducing factor (AIF) and endonuclease G (endoG). Another interesting protein, which was expected to act similarly as AIF due to the high sequence homology with AIF is AIF-homologous mitochondrion-associated inducer of death (AMID). We studied the structure, cellular localization, and interactions of several proteins in silico and also in cells using fluorescent microscopy. We found the AMID protein to be cytoplasmic, most probably incorporated into the cytoplasmic side of the lipid membranes. Bioinformatic predictions were conducted to analyze the interactions of the studied proteins with each other and with other possible partners. We conducted molecular modeling of proteins with unknown 3D structures. These models were then refined by MolProbity server and employed in molecular docking simulations of interactions. Our results show data acquired using a combination of modern in silico methods and image analysis to understand the localization, interactions and functions of proteins AMID, AIF, endonuclease G, and other apoptosis-related proteins.
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