Latrophilin fragments behave as independent proteins that associate and signal on binding of LTXN4C-Reference-Cited by-同舟云学术

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Latrophilin fragments behave as independent proteins that associate and signal on binding of LTXN4C

Published:2004-10-14 Issue:22 Volume:23 Page:4423-4433
ISSN:0261-4189
Container-title:The EMBO Journal
language:
Short-container-title:EMBO J

Author:

Volynski Kirill E,Silva John-Paul,Lelianova Vera G,Atiqur Rahman M,Hopkins Colin,Ushkaryov Yuri A

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference36 articles.

1. Cleavage of Ig-Hepta at a “SEA” Module and at a Conserved G Protein-coupled Receptor Proteolytic Site

2. α-Latrotoxin, Acting via Two Ca2+-dependent Pathways, Triggers Exocytosis of Two Pools of Synaptic Vesicles

3. Oligomerization of G-protein-coupled transmitter receptors

4. The α-Latrotoxin Mutant LTXN4CEnhances Spontaneous and Evoked Transmitter Release in CA3 Pyramidal Neurons

5. Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif

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4. Piconewton forces mediate GAIN domain dissociation of the latrophilin-3 adhesion GPCR;2023-01-13

5. GPR56 C‐terminal fragment mediates signal received by N‐terminal fragment of another adhesion GPCR Latrophilin1 in neurons;Genes to Cells;2022-12-11

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