M
Margaret J. Wheelock
Researcher at University of Nebraska Medical Center
Publications - 95
Citations - 11364
Margaret J. Wheelock is an academic researcher from University of Nebraska Medical Center. The author has contributed to research in topics: Cadherin & Catenin. The author has an hindex of 52, co-authored 95 publications receiving 11010 citations. Previous affiliations of Margaret J. Wheelock include Reading Hospital & University of Nebraska Medical Center College of Dentistry.
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N-cadherin promotes motility in human breast cancer cells regardless of their E-cadherin expression.
TL;DR: It is shown that N-cadherin promotes motility and invasion, and likely plays a direct role in promoting motility; that forced expression of E-cADherin in invasive, N- cadher in–positive cells does not reduce their motility or invasive capacity; and that cadherin-11 promotes epithelial cell motility in a manner similar to N-Cadhersin.
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Cadherins as modulators of cellular phenotype.
TL;DR: Cadherins have been implicated in a number of signaling pathways that regulate cellular behavior, and it is becoming increasingly clear that integration of information received from cell-cell signaling, cell-matrix signaling, and growth factor signaling determines ultimate cellular phenotype and behavior.
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Interaction of alpha-actinin with the cadherin/catenin cell-cell adhesion complex via alpha-catenin.
TL;DR: Evidence is presented that in fibroblasts alpha-actinin, but not vinculin, colocalizes extensively with the N-cadherin/catenin complex, and it is proposed that cadherin / catenin complexes are linked to the actin cytoskeleton via a direct association between alpha- actinin and alpha-caten in.
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The catenin/cadherin adhesion system is localized in synaptic junctions bordering transmitter release zones.
TL;DR: It is found that two classes of cadherin-associated proteins, alpha N- and beta-catenin, are broadly distributed in adult brains, colocalizing with a synaptic marker, synaptophysin, and these proteins were localized in synaptic junctions of various types, forming a symmetrical adhesion structure.
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Identification of a new catenin: the tyrosine kinase substrate p120cas associates with E-cadherin complexes.
TL;DR: In this paper, the authors showed that p120 associates with a complex containing E-cadherin, alpha-catenin, plakoglobin, and catenins.