Analysis of Huntington's Disease Modifiers Using the Hyperbolic Mapping of the Protein Interaction Network
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Aimilia-Christina Vagiona
- Pablo Mier
- Spyros Petrakis
- Miguel A Andrade-Navarro
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000801446500001&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.3390/ijms23105853
- eISSN
- 1422-0067
- Externe Identifier
- Clarivate Analytics Document Solution ID: 1O6NN
- PubMed Identifier: 35628660
- Ausgabe der Veröffentlichung
- 10
- Zeitschrift
- INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Schlüsselwörter
- Huntington's disease
- paralogy
- protein-protein interaction
- Artikelnummer
- ARTN 5853
- Datum der Veröffentlichung
- 2022
- Status
- Published
- Titel
- Analysis of Huntington's Disease Modifiers Using the Hyperbolic Mapping of the Protein Interaction Network
- Sub types
- Article
- Ausgabe der Zeitschrift
- 23
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Abstract
- <jats:p>Huntington’s disease (HD) is caused by the production of a mutant huntingtin (HTT) with an abnormally long poly-glutamine (polyQ) tract, forming aggregates and inclusions in neurons. Previous work by us and others has shown that an increase or decrease in polyQ-triggered aggregates can be passive simply due to the interaction of proteins with the aggregates. To search for proteins with active (functional) effects, which might be more effective in finding therapies and mechanisms of HD, we selected among the proteins that interact with HTT a total of 49 pairs of proteins that, while being paralogous to each other (and thus expected to have similar passive interaction with HTT), are located in different regions of the protein interaction network (suggesting participation in different pathways or complexes). Three of these 49 pairs contained members with opposite effects on HD, according to the literature. The negative members of the three pairs, MID1, IKBKG, and IKBKB, interact with PPP2CA and TUBB, which are known negative factors in HD, as well as with HSP90AA1 and RPS3. The positive members of the three pairs interact with HSPA9. Our results provide potential HD modifiers of functional relevance and reveal the dynamic aspect of paralog evolution within the interaction network.</jats:p>
- Autoren
- Aimilia-Christina Vagiona
- Pablo Mier
- Spyros Petrakis
- Miguel A Andrade-Navarro
- DOI
- 10.3390/ijms23105853
- eISSN
- 1422-0067
- Ausgabe der Veröffentlichung
- 10
- Zeitschrift
- International Journal of Molecular Sciences
- Sprache
- en
- Online publication date
- 2022
- Paginierung
- 5853 - 5853
- Status
- Published online
- Herausgeber
- MDPI AG
- Herausgeber URL
- http://dx.doi.org/10.3390/ijms23105853
- Datum der Datenerfassung
- 2022
- Titel
- Analysis of Huntington’s Disease Modifiers Using the Hyperbolic Mapping of the Protein Interaction Network
- Ausgabe der Zeitschrift
- 23
Datenquelle: Crossref
- Abstract
- Huntington's disease (HD) is caused by the production of a mutant huntingtin (HTT) with an abnormally long poly-glutamine (polyQ) tract, forming aggregates and inclusions in neurons. Previous work by us and others has shown that an increase or decrease in polyQ-triggered aggregates can be passive simply due to the interaction of proteins with the aggregates. To search for proteins with active (functional) effects, which might be more effective in finding therapies and mechanisms of HD, we selected among the proteins that interact with HTT a total of 49 pairs of proteins that, while being paralogous to each other (and thus expected to have similar passive interaction with HTT), are located in different regions of the protein interaction network (suggesting participation in different pathways or complexes). Three of these 49 pairs contained members with opposite effects on HD, according to the literature. The negative members of the three pairs, MID1, IKBKG, and IKBKB, interact with PPP2CA and TUBB, which are known negative factors in HD, as well as with HSP90AA1 and RPS3. The positive members of the three pairs interact with HSPA9. Our results provide potential HD modifiers of functional relevance and reveal the dynamic aspect of paralog evolution within the interaction network.
- Addresses
- Institute of Organismic and Molecular Evolution, Faculty of Biology, Johannes Gutenberg University, Hans-Dieter-Hüsch-Weg 15, 55128 Mainz, Germany.
- Autoren
- Aimilia-Christina Vagiona
- Pablo Mier
- Spyros Petrakis
- Miguel A Andrade-Navarro
- DOI
- 10.3390/ijms23105853
- eISSN
- 1422-0067
- Externe Identifier
- PubMed Identifier: 35628660
- PubMed Central ID: PMC9144261
- Open access
- true
- ISSN
- 1422-0067
- Ausgabe der Veröffentlichung
- 10
- Zeitschrift
- International journal of molecular sciences
- Schlüsselwörter
- Neurons
- Inclusion Bodies
- Humans
- Huntington Disease
- I-kappa B Kinase
- Protein Interaction Maps
- Sprache
- eng
- Medium
- Electronic
- Online publication date
- 2022
- Open access status
- Open Access
- Paginierung
- 5853
- Datum der Veröffentlichung
- 2022
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2022
- Titel
- Analysis of Huntington's Disease Modifiers Using the Hyperbolic Mapping of the Protein Interaction Network.
- Sub types
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 23
Files
https://www.mdpi.com/1422-0067/23/10/5853/pdf?version=1653362261 https://europepmc.org/articles/PMC9144261?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- Huntington's disease (HD) is caused by the production of a mutant huntingtin (HTT) with an abnormally long poly-glutamine (polyQ) tract, forming aggregates and inclusions in neurons. Previous work by us and others has shown that an increase or decrease in polyQ-triggered aggregates can be passive simply due to the interaction of proteins with the aggregates. To search for proteins with active (functional) effects, which might be more effective in finding therapies and mechanisms of HD, we selected among the proteins that interact with HTT a total of 49 pairs of proteins that, while being paralogous to each other (and thus expected to have similar passive interaction with HTT), are located in different regions of the protein interaction network (suggesting participation in different pathways or complexes). Three of these 49 pairs contained members with opposite effects on HD, according to the literature. The negative members of the three pairs, MID1, IKBKG, and IKBKB, interact with PPP2CA and TUBB, which are known negative factors in HD, as well as with HSP90AA1 and RPS3. The positive members of the three pairs interact with HSPA9. Our results provide potential HD modifiers of functional relevance and reveal the dynamic aspect of paralog evolution within the interaction network.
- Date of acceptance
- 2022
- Autoren
- Aimilia-Christina Vagiona
- Pablo Mier
- Spyros Petrakis
- Miguel A Andrade-Navarro
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/35628660
- DOI
- 10.3390/ijms23105853
- eISSN
- 1422-0067
- Externe Identifier
- PubMed Central ID: PMC9144261
- Ausgabe der Veröffentlichung
- 10
- Zeitschrift
- Int J Mol Sci
- Schlüsselwörter
- Huntington’s disease
- paralogy
- protein–protein interaction
- Humans
- Huntington Disease
- I-kappa B Kinase
- Inclusion Bodies
- Neurons
- Protein Interaction Maps
- Sprache
- eng
- Country
- Switzerland
- PII
- ijms23105853
- Datum der Veröffentlichung
- 2022
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2022
- Titel
- Analysis of Huntington's Disease Modifiers Using the Hyperbolic Mapping of the Protein Interaction Network.
- Sub types
- Journal Article
- Ausgabe der Zeitschrift
- 23
Datenquelle: PubMed
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