Rab3A is a new interacting partner of synaptotagmin I and may modulate synaptic membrane fusion through a competitive mechanism
• Rab3A has been found to be a novel interacting protein of synaptotagmin I. • Rab3A binds to synaptotagmin I in a Ca2+-independent manner. • KKKK motif in C2B domain of synaptotagmin I is a key site for Rab3A binding. • Rab3A competitively inhibits the binding of C2B in synaptotagmin I to syntaxin...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Xie, Chunliang [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2014 |
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| Schlagwörter: |
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| Umfang: |
5 |
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| Übergeordnetes Werk: |
Enthalten in: Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag - Zhang, Zhikun ELSEVIER, 2019, BBRC, Orlando, Fla |
|---|---|
| Übergeordnetes Werk: |
volume:444 ; year:2014 ; number:4 ; day:21 ; month:02 ; pages:491-495 ; extent:5 |
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| DOI / URN: |
10.1016/j.bbrc.2014.01.090 |
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Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag |
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Rab3A is a new interacting partner of synaptotagmin I and may modulate synaptic membrane fusion through a competitive mechanism |
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(DE-627)ELV01794144X (ELSEVIER)S0006-291X(14)00114-4 |
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Rab3A is a new interacting partner of synaptotagmin I and may modulate synaptic membrane fusion through a competitive mechanism |
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Xie, Chunliang |
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Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag |
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Preparation and characterization of glass-ceramics via co-sintering of coal fly ash and oil shale ash-derived amorphous slag |
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2014 |
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Xie, Chunliang |
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Elektronische Aufsätze |
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Xie, Chunliang |
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10.1016/j.bbrc.2014.01.090 |
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570 670 |
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rab3a is a new interacting partner of synaptotagmin i and may modulate synaptic membrane fusion through a competitive mechanism |
| title_auth |
Rab3A is a new interacting partner of synaptotagmin I and may modulate synaptic membrane fusion through a competitive mechanism |
| abstract |
• Rab3A has been found to be a novel interacting protein of synaptotagmin I. • Rab3A binds to synaptotagmin I in a Ca2+-independent manner. • KKKK motif in C2B domain of synaptotagmin I is a key site for Rab3A binding. • Rab3A competitively inhibits the binding of C2B in synaptotagmin I to syntaxin 1B. • Rab3A may regulate synaptic membrane fusion and exocytosis in a competitive manner. |
| abstractGer |
• Rab3A has been found to be a novel interacting protein of synaptotagmin I. • Rab3A binds to synaptotagmin I in a Ca2+-independent manner. • KKKK motif in C2B domain of synaptotagmin I is a key site for Rab3A binding. • Rab3A competitively inhibits the binding of C2B in synaptotagmin I to syntaxin 1B. • Rab3A may regulate synaptic membrane fusion and exocytosis in a competitive manner. |
| abstract_unstemmed |
• Rab3A has been found to be a novel interacting protein of synaptotagmin I. • Rab3A binds to synaptotagmin I in a Ca2+-independent manner. • KKKK motif in C2B domain of synaptotagmin I is a key site for Rab3A binding. • Rab3A competitively inhibits the binding of C2B in synaptotagmin I to syntaxin 1B. • Rab3A may regulate synaptic membrane fusion and exocytosis in a competitive manner. |
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Rab3A is a new interacting partner of synaptotagmin I and may modulate synaptic membrane fusion through a competitive mechanism |
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https://doi.org/10.1016/j.bbrc.2014.01.090 |
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Li, Jianglin Guo, Tianyao Yan, Yizhong Tang, Cheng Wang, Ying Chen, Ping Wang, Xianchun Liang, Songping |
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Li, Jianglin Guo, Tianyao Yan, Yizhong Tang, Cheng Wang, Ying Chen, Ping Wang, Xianchun Liang, Songping |
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2024-07-06T17:34:52.921Z |
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