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Cited by 604

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

Structure of the ERM Protein Moesin Reveals the FERM Domain Fold Masked by an Extended Actin Binding Tail Domain

Open access
Pearson, Matthew A., Reczek, David, Bretscher, Anthony, Karplus, P.Andrew·2000·Cell

Abstract

The ezrin-radixin-moesin (ERM) protein family link actin filaments of cell surface structures to the plasma membrane, using a C-terminal F-actin binding segment and an N-terminal FERM domain, a common membrane binding module. ERM proteins are regulated by an intramolecular association of the FERM and C-terminal tail domains that masks their binding sites. The crystal structure of a dormant moesin FERM/tail complex reveals that the FERM domain has three compact lobes including an integrated PTB/PH/ EVH1 fold, with the C-terminal segment bound as an extended peptide masking a large surface of the FERM domain. This extended binding mode suggests a novel mechanism for how different signals could produce varying levels of activation. Sequence conservation suggests a similar regulation of the tumor suppressor merlin.

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Crossref · 10.1016/s0092-8674(00)80836-3

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Metadata

Authors
Pearson, M. A., Reczek, D., Bretscher, A., & Karplus, P. A.
Venue
Cell
Publisher
Elsevier BV
Published
2000-04
Volume
101
Issue
3
Pages
259-270
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2112981236
Cited by
604
References
2
FWCI
14.19
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Structure of the ERM Protein Moesin Reveals the FERM Domain Fold Masked by an Extended Actin Binding Tail Domain. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80836-3
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Pearson, M. A., Reczek, D., Bretscher, A., & Karplus, P. A. (2000). Structure of the ERM Protein Moesin Reveals the FERM Domain Fold Masked by an Extended Actin Binding Tail Domain. Cell. https://doi.org/10.1016/s0092-8674(00)80836-3

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