Oligomerization of polytopic α-helical membrane proteins: causes and consequences
- Publication type:
- Journal article
- Metadata:
-
- Abstract
- <jats:title>Abstract</jats:title> <jats:p>Several polytopic α-helical membrane-integrated proteins appear to be organized in higher-ordered oligomeric complexes. While many aspects are still enigmatic, in recent years, the physiological impact of membrane protein oligomerization has been analyzed to some extent. In the present article, oligomerization of structurally well-defined membrane proteins is discussed. The available experimental information indicates the causes and physiological consequences of membrane protein oligomerization, including stabilization, cooperative functions, and control of specific activities. Based on the currently available observations, we aim to derive some general principles and discuss open questions.</jats:p>
- Autoren
- Florian Cymer
- Dirk Schneider
- DOI
- 10.1515/hsz-2012-0231
- eISSN
- 1437-4315
- ISSN
- 1431-6730
- Ausgabe der Veröffentlichung
- 11
- Zeitschrift
- bchm
- Sprache
- en
- Online publication date
- 2012
- Paginierung
- 1215 - 1230
- Datum der Veröffentlichung
- 2012
- Status
- Published
- Herausgeber
- Walter de Gruyter GmbH
- Herausgeber URL
- http://dx.doi.org/10.1515/hsz-2012-0231
- Datum der Datenerfassung
- 2022
- Titel
- Oligomerization of polytopic α-helical membrane proteins: causes and consequences
- Ausgabe der Zeitschrift
- 393
Data source: Crossref
- Other metadata sources:
-
- Abstract
- Several polytopic α-helical membrane-integrated proteins appear to be organized in higher-ordered oligomeric complexes. While many aspects are still enigmatic, in recent years, the physiological impact of membrane protein oligomerization has been analyzed to some extent. In the present article, oligomerization of structurally well-defined membrane proteins is discussed. The available experimental information indicates the causes and physiological consequences of membrane protein oligomerization, including stabilization, cooperative functions, and control of specific activities. Based on the currently available observations, we aim to derive some general principles and discuss open questions.
- Addresses
- Institut für Pharmazie und Biochemie, Johannes Gutenberg-Universität Mainz, Johann-Joachim-Becher-Weg 30, D-55128 Mainz, Deutschland. Florian.Cymer@dbb.su.se
- Autoren
- Florian Cymer
- Dirk Schneider
- DOI
- 10.1515/hsz-2012-0231
- eISSN
- 1437-4315
- Externe Identifier
- PubMed Identifier: 23096346
- Open access
- false
- ISSN
- 1431-6730
- Ausgabe der Veröffentlichung
- 11
- Zeitschrift
- Biological chemistry
- Schlüsselwörter
- Humans
- Membrane Proteins
- Protein Structure, Secondary
- Models, Molecular
- Protein Stability
- Sprache
- eng
- Medium
- Paginierung
- 1215 - 1230
- Datum der Veröffentlichung
- 2012
- Status
- Published
- Datum der Datenerfassung
- 2012
- Titel
- Oligomerization of polytopic α-helical membrane proteins: causes and consequences.
- Sub types
- Research Support, Non-U.S. Gov't
- Review
- Journal Article
- Ausgabe der Zeitschrift
- 393
Data source: Europe PubMed Central
- Abstract
- Several polytopic α-helical membrane-integrated proteins appear to be organized in higher-ordered oligomeric complexes. While many aspects are still enigmatic, in recent years, the physiological impact of membrane protein oligomerization has been analyzed to some extent. In the present article, oligomerization of structurally well-defined membrane proteins is discussed. The available experimental information indicates the causes and physiological consequences of membrane protein oligomerization, including stabilization, cooperative functions, and control of specific activities. Based on the currently available observations, we aim to derive some general principles and discuss open questions.
- Date of acceptance
- 2012
- Autoren
- Florian Cymer
- Dirk Schneider
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/23096346
- DOI
- 10.1515/hsz-2012-0231
- eISSN
- 1437-4315
- Ausgabe der Veröffentlichung
- 11
- Zeitschrift
- Biol Chem
- Schlüsselwörter
- Humans
- Membrane Proteins
- Models, Molecular
- Protein Stability
- Protein Structure, Secondary
- Sprache
- eng
- Country
- Germany
- Paginierung
- 1215 - 1230
- PII
- /j/bchm.just-accepted/hsz-2012-0231/hsz-2012-0231.xml
- Datum der Veröffentlichung
- 2012
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2014
- Titel
- Oligomerization of polytopic α-helical membrane proteins: causes and consequences.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Review
- Ausgabe der Zeitschrift
- 393
Data source: PubMed
- Beziehungen:
- Property of