Dr. Anna Arbuzova
Profil
Zusammenfassung
Dr. Anna Arbuzova erforscht die Wechselwirkungen zwischen Biomolekülen und Membranen, insbesondere wie Proteine und Nukleinsäuren an Lipidschichten binden und dort funktionieren. Ihre Expertise umfasst die Charakterisierung dieser Prozesse mit biophysikalischen Methoden sowie die gezielte Funktionalisierung von Membranen für Anwendungen in Diagnostik und Wirkstoffabgabe.
Skills
Stammdaten
Identität, Organisation und Kontakt aus HU-FIS.
Forschungsthemen1
Supramolekulare Organisation von Cholesterol-modifizierten Nukleosiden in Mikroröhren: Charakterisierung und Funktionalisierung
Quelle ↗Förderer: DFG Eigene Stelle (Sachbeihilfe) Zeitraum: 06/2011 - 09/2015 Projektleitung: Dr. Anna Arbuzova, Prof. Dr. rer. nat. Andreas Herrmann
Mögliche Industrie-Partner136
Details nur für eingeloggte sichtbar
🔒 Das System hat 136 mögliche Industrie-Partner gefunden — Firmen, Scores und Begründungen sind nur für eingeloggte Nutzer:innen sichtbar. Anmelden
Publikationen25
Top 25 nach Zitationen — Quelle: OpenAlex (BAAI/bge-m3 embedded für Matching).
Biochemical Journal · 302 Zitationen · DOI
The proteins of the MARCKS (myristoylated alanine-rich C kinase substrate) family were first identified as prominent substrates of protein kinase C (PKC). Since then, these proteins have been implicated in the regulation of brain development and postnatal survival, cellular migration and adhesion, as well as endo-, exo- and phago-cytosis, and neurosecretion. The effector domain of MARCKS proteins is phosphorylated by PKC, binds to calmodulin and contributes to membrane binding. This multitude of mutually exclusive interactions allows cross-talk between the signal transduction pathways involving PKC and calmodulin. This review focuses on recent, mostly biophysical and biochemical results renewing interest in this protein family. MARCKS membrane binding is now understood at the molecular level. From a structural point of view, there is a consensus emerging that MARCKS proteins are "natively unfolded". Interestingly, domains similar to the effector domain have been discovered in other proteins. Furthermore, since the effector domain enhances the polymerization of actin in vitro, MARCKS proteins have been proposed to mediate regulation of the actin cytoskeleton. However, the recent observations that MARCKS might serve to sequester phosphatidylinositol 4,5-bisphosphate in the plasma membrane of unstimulated cells suggest an alternative model for the control of the actin cytoskeleton. While myristoylation is classically considered to be a co-translational, irreversible event, new reports on MARCKS proteins suggest a more dynamic picture of this protein modification. Finally, studies with mice lacking MARCKS proteins have investigated the functions of these proteins during embryonic development in the intact organism.
Biochemical Journal · 222 Zitationen · DOI
The proteins of the MARCKS (myristoylated alanine-rich C kinase substrate) family were first identified as prominent substrates of protein kinase C (PKC). Since then, these proteins have been implicated in the regulation of brain development and postnatal survival, cellular migration and adhesion, as well as endo-, exo- and phago-cytosis, and neurosecretion. The effector domain of MARCKS proteins is phosphorylated by PKC, binds to calmodulin and contributes to membrane binding. This multitude of mutually exclusive interactions allows cross-talk between the signal transduction pathways involving PKC and calmodulin. This review focuses on recent, mostly biophysical and biochemical results renewing interest in this protein family. MARCKS membrane binding is now understood at the molecular level. From a structural point of view, there is a consensus emerging that MARCKS proteins are ‘natively unfolded'. Interestingly, domains similar to the effector domain have been discovered in other proteins. Furthermore, since the effector domain enhances the polymerization of actin in vitro, MARCKS proteins have been proposed to mediate regulation of the actin cytoskeleton. However, the recent observations that MARCKS might serve to sequester phosphatidylinositol 4,5-bisphosphate in the plasma membrane of unstimulated cells suggest an alternative model for the control of the actin cytoskeleton. While myristoylation is classically considered to be a co-translational, irreversible event, new reports on MARCKS proteins suggest a more dynamic picture of this protein modification. Finally, studies with mice lacking MARCKS proteins have investigated the functions of these proteins during embryonic development in the intact organism.
Biophysical Journal · 183 Zitationen · DOI
Kooperationen0
Bestätigte Forscher↔Partner-Paare aus HU-FIS — Gold-Standard-Positive für das Matching.
Aus HU-FIS sind keine Kooperationen für diese Person gemeldet.