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Cited by 305

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Coassembly of TRP and TRPL Produces a Distinct Store-Operated Conductance

Open access
Xu, Xian-Zhong Shawn, Li, Hong-Sheng, Guggino, William B, Montell, Craig·1997·Cell

Abstract

The Drosophila retinal-specific protein, TRP (transient receptor potential), is the founding member of a family of store-operated channels (SOCs) conserved from C. elegans to humans. In vitro studies indicate that TRP is a SOC, but that the related retinal protein, TRPL, is constitutively active. In the current work, we report that coexpression of TRP and TRPL leads to a store-operated, outwardly rectifying current distinct from that owing to either TRP or TRPL alone. TRP and TRPL interact directly, indicating that the TRP-TRPL-dependent current is mediated by heteromultimeric association between the two subunits. We propose that the light-activated current in photoreceptor cells is produced by a combination of TRP homo- and TRP-TRPL heteromultimers.

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Metadata

Authors
Xu, X.-Z. S., Li, H.-S., Guggino, W. B., & Montell, C.
Venue
Cell
Publisher
Elsevier BV
Published
1997-06
Volume
89
Issue
7
Pages
1155-1164
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2081434136
Cited by
305
References
2
FWCI
13.04
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Coassembly of TRP and TRPL Produces a Distinct Store-Operated Conductance. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80302-5
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Xu, X.-Z. S., Li, H.-S., Guggino, W. B., & Montell, C. (1997). Coassembly of TRP and TRPL Produces a Distinct Store-Operated Conductance. Cell. https://doi.org/10.1016/s0092-8674(00)80302-5

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