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1 teins as endogenous postsynaptic ligands for latrophilins.
2 as interactors for the lectin-like domain of latrophilins.
3 rs: a G-protein-coupled receptor called CIRL/latrophilin 1 (CL1) and a cell-surface protein called ne
7 ons of soluble teneurin-binding fragments of latrophilin-1 decreased synapse density, suggesting that
10 ternative splicing at an N-terminal site; in latrophilin-1, this alternative splicing modulates teneu
13 deaminase, lipocalin 2, synaptotagmin 4, and latrophilin 2, whose time-dependent induction following
14 nd knockout mice, we show in this study that latrophilin-2 (Lphn2), a cell-adhesion G protein-coupled
16 s examined (megalin, thrombospondin-4, KR18, latrophilin-3, and phosphatidylinositol-3-OH kinase P101
17 hich shows approximately 65% identity to rat latrophilin, a G-coupled, seven span transmembrane prote
22 ndependent receptors for latrotoxin (CIRL or latrophilin) and neurexin 1 alpha receptors were found t
23 erve terminals, neurexins and CLs (CIRLs and latrophilins), and then executes a critical, second step
25 dhesion molecules, in addition to binding to latrophilins as heterophilic cell-adhesion molecules.
26 (2) a Ca(2+)-independent mechanism with CIRL/latrophilins as receptors, in which alpha-latrotoxin dir
27 1 decreased synapse density, suggesting that latrophilin binding to teneurin may directly or indirect
33 phan receptor lat-1, a homolog of vertebrate latrophilins, plays an essential role in the establishme
34 neuroligins, cerebellin/GluD complexes, and latrophilins, thereby shaping the input/output relations
35 l-surface receptors, neurexins and CLs (Cirl/latrophilins), which probably have a physiological funct
36 a, together with binding studies, prove that latrophilin, which is linked to G proteins and inositol
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