Relevant bibliographies by topics / ERM PROTEINS

Contents

  1. Journal articles

Academic literature on the topic 'ERM PROTEINS'

Author: Grafiati
Published: 14 March 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'ERM PROTEINS.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "ERM PROTEINS"

1

McClatchey, Andrea I. "ERM proteins." Current Biology 22, no. 18 (2012): R784—R785. http://dx.doi.org/10.1016/j.cub.2012.07.057.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

McClatchey, Andrea I. "ERM proteins at a glance." Journal of Cell Science 127, no. 15 (2014): 3199–204. http://dx.doi.org/10.1242/jcs.098343.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Clucas, J., and F. Valderrama. "ERM proteins in cancer progression." Journal of Cell Science 127, no. 2 (2014): 267–75. http://dx.doi.org/10.1242/jcs.133108.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Clucas, J., and F. Valderrama. "ERM proteins in cancer progression." Journal of Cell Science 128, no. 6 (2015): 1253. http://dx.doi.org/10.1242/jcs.170027.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Bagchi, M., M. Katar, W. K. Lo, R. Yost, C. Hill, and H. Maisel. "ERM proteins of the lens." Journal of Cellular Biochemistry 92, no. 3 (2004): 626–30. http://dx.doi.org/10.1002/jcb.20062.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Kondo, Takahisa, Kosei Takeuchi, Yoshinori Doi, et al. "ERM (Ezrin/Radixin/Moesin)-based Molecular Mechanism of Microvillar Breakdown at an Early Stage of Apoptosis." Journal of Cell Biology 139, no. 3 (1997): 749–58. http://dx.doi.org/10.1083/jcb.139.3.749.

Full text
Abstract:
Breakdown of microvilli is a common early event in various types of apoptosis, but its molecular mechanism and implications remain unclear. ERM (ezrin/radixin/moesin) proteins are ubiquitously expressed microvillar proteins that are activated in the cytoplasm, translocate to the plasma membrane, and function as general actin filament/plasma membrane cross-linkers to form microvilli. Immunofluorescence microscopic and biochemical analyses revealed that, at the early phase of Fas ligand (FasL)–induced apoptosis in L cells expressing Fas (LHF), ERM proteins translocate from the plasma membranes o
APA, Harvard, Vancouver, ISO, and other styles
7

Yonemura, Shigenobu, Takeshi Matsui, Shoichiro Tsukita, and Sachiko Tsukita. "Rho-dependent and -independent activation mechanisms of ezrin/radixin/moesin proteins: an essential role for polyphosphoinositides in vivo." Journal of Cell Science 115, no. 12 (2002): 2569–80. http://dx.doi.org/10.1242/jcs.115.12.2569.

Full text
Abstract:
Ezrin/radixin/moesin (ERM) proteins crosslink actin filaments to plasma membranes and are involved in the organization of the cortical cytoskeleton,especially in the formation of microvilli. ERM proteins are reported to be activated as crosslinkers in a Rho-dependent manner and are stabilized when phosphorylated at their C-terminal threonine residue to create C-terminal threonine-phosphorylated ERM proteins (CPERMs). Using a CPERM-specific mAb, we have shown, in vivo, that treatment with C3 transferase (a Rho inactivator) or staurosporine (a protein kinase inhibitor) leads to the dephosphoryla
APA, Harvard, Vancouver, ISO, and other styles
8

Hirao, M., N. Sato, T. Kondo, et al. "Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway." Journal of Cell Biology 135, no. 1 (1996): 37–51. http://dx.doi.org/10.1083/jcb.135.1.37.

Full text
Abstract:
The ERM proteins, ezrin, radixin, and moesin, are involved in the actin filament/plasma membrane interaction as cross-linkers. CD44 has been identified as one of the major membrane binding partners for ERM proteins. To examine the CD44/ERM protein interaction in vitro, we produced mouse ezrin, radixin, moesin, and the glutathione-S-transferase (GST)/CD44 cytoplasmic domain fusion protein (GST-CD44cyt) by means of recombinant baculovirus infection, and constructed an in vitro assay for the binding between ERM proteins and the cytoplasmic domain of CD44. In this system, ERM proteins bound to GST
APA, Harvard, Vancouver, ISO, and other styles
9

Yonemura, Shigenobu, Sachiko Tsukita, and Shoichiro Tsukita. "Direct Involvement of Ezrin/Radixin/Moesin (ERM)-binding Membrane Proteins in the Organization of Microvilli in Collaboration with Activated ERM Proteins." Journal of Cell Biology 145, no. 7 (1999): 1497–509. http://dx.doi.org/10.1083/jcb.145.7.1497.

Full text
Abstract:
Ezrin/radixin/moesin (ERM) proteins have been thought to play a central role in the organization of cortical actin-based cytoskeletons including microvillar formation through cross-linking actin filaments and integral membrane proteins such as CD43, CD44, and ICAM-2. To examine the functions of these ERM-binding membrane proteins (ERMBMPs) in cortical morphogenesis, we overexpressed ERMBMPs (the extracellular domain of E-cadherin fused with the transmembrane/cytoplasmic domain of CD43, CD44, or ICAM-2) in various cultured cells. In cultured fibroblasts such as L and CV-1 cells, their overexpre
APA, Harvard, Vancouver, ISO, and other styles
10

Michie, Katharine A., Adam Bermeister, Neil O. Robertson, Sophia C. Goodchild, and Paul M. G. Curmi. "Two Sides of the Coin: Ezrin/Radixin/Moesin and Merlin Control Membrane Structure and Contact Inhibition." International Journal of Molecular Sciences 20, no. 8 (2019): 1996. http://dx.doi.org/10.3390/ijms20081996.

Full text
Abstract:
The merlin-ERM (ezrin, radixin, moesin) family of proteins plays a central role in linking the cellular membranes to the cortical actin cytoskeleton. Merlin regulates contact inhibition and is an integral part of cell–cell junctions, while ERM proteins, ezrin, radixin and moesin, assist in the formation and maintenance of specialized plasma membrane structures and membrane vesicle structures. These two protein families share a common evolutionary history, having arisen and separated via gene duplication near the origin of metazoa. During approximately 0.5 billion years of evolution, the merlin
APA, Harvard, Vancouver, ISO, and other styles
More sources
You might also be interested in the extended bibliographies on the topic 'ERM PROTEINS' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography