Cell Signaling

Edited by Thomas W. Durso K.L. Schmeichel, M.C. Beckerle, "The LIM domain is a modular protein-binding interface," Cell, 79:211-9, 1994. (Cited in nearly 50 publications through August 1996) Comments by Mary C. Beckerle, University of Utah, Salt Lake City Its presence in several proteins that "play fundamental roles in development" is what led Karen L. Schmeichel and Mary C. Beckerle of the University of Utah, Salt Lake City, to begin studying the LIM domain, a zinc-binding protein sequence.

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Edited by Thomas W. Durso
K.L. Schmeichel, M.C. Beckerle, "The LIM domain is a modular protein-binding interface," Cell, 79:211-9, 1994. (Cited in nearly 50 publications through August 1996) Comments by Mary C. Beckerle, University of Utah, Salt Lake City

Its presence in several proteins that "play fundamental roles in development" is what led Karen L. Schmeichel and Mary C. Beckerle of the University of Utah, Salt Lake City, to begin studying the LIM domain, a zinc-binding protein sequence.

LIFE AND LIM: From left, coauthors Mary C. Beckerle and Karen L. Schmeichel investigated a protein domain with major developmental functions.

The LIM motif was first identified in three developmentally important transcription factors, Caenorhabditis elegans Lin-11, rat Isl-1, and C. elegans Mec-3, from which the acronym LIM is derived (G. Freyd et al., Nature, 344:876-9, 1990; O. Karlsson et al., Nature, 344:879-82, 1990).

The functions of LIM proteins include signal transduction, transcriptional ...

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