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Title
STIM Proteins: An Ever-Expanding Family
Authors
Keywords
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Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 22, Issue 1, Pages 378
Publisher
MDPI AG
Online
2021-01-01
DOI
10.3390/ijms22010378
References
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Note: Only part of the references are listed.- Optogenetic engineering to probe the molecular choreography of STIM1-mediated cell signaling
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- STIM1L is a new actin-binding splice variant involved in fast repetitive Ca2+release
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- STIM proteins: integrators of signalling pathways in development, differentiation and disease
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- STIM1 Clusters and Activates CRAC Channels via Direct Binding of a Cytosolic Domain to Orai1
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- IP3 receptor subtype-dependent activation of store-operated calcium entry through ICRAC
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- Visualizing the store-operated channel complex assembly in real time: Identification of SERCA2 as a new member
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- Mechanistic view on domains mediating STIM1-Orai coupling
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- A Cytosolic Homomerization and a Modulatory Domain within STIM1 C Terminus Determine Coupling to ORAI1 Channels
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- A Ca2+Release-activated Ca2+(CRAC) Modulatory Domain (CMD) within STIM1 Mediates Fast Ca2+-dependent Inactivation of ORAI1 Channels
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- Molecular Determinants of the Coupling between STIM1 and Orai Channels
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- The Short N-terminal Domains of STIM1 and STIM2 Control the Activation Kinetics of Orai1 Channels
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- Biophysical characterization of the EF-hand and SAM domain containing Ca2+ sensory region of STIM1 and STIM2
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- Structural and Mechanistic Insights into STIM1-Mediated Initiation of Store-Operated Calcium Entry
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- STIM1 Is a MT-Plus-End-Tracking Protein Involved in Remodeling of the ER
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- Dynamic Coupling of the Putative Coiled-coil Domain of ORAI1 with STIM1 Mediates ORAI1 Channel Activation
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- Oligomerization of STIM1 couples ER calcium depletion to CRAC channel activation
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