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Dynamic interaction of VCAM-1 and ICAM-1 with moesin and ezrin in a novel endothelial docking structure for adherent leukocytes
The results provide the first characterization of an endothelial docking structure that plays a key role in the firm adhesion of leukocytes to the endothelium during inflammation.
Direct binding of the Na--H exchanger NHE1 to ERM proteins regulates the cortical cytoskeleton and cell shape independently of H(+) translocation.
A network model for the organization of type IV collagen molecules in basement membranes.
- R. Timpl, H. Wiedemann, V. van Delden, H. Furthmayr, K. Kühn
- Biology, ChemistryEuropean journal of biochemistry
- 1 November 1981
Data indicate that the collagenous matrix of basement membranes consists of a regular network of type IV collagen molecules which is generated by two different interacting sites located at opposite ends of each molecule.
Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix.
Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides.
- F. Nakamura, L. Huang, K. Pestonjamasp, E. J. Luna, H. Furthmayr
- Biology, ChemistryMolecular biology of the cell
- 1 August 1999
Both polyphosphatidylinositides and phosphorylation can activate moesin's high-affinity F-actin binding site in vitro, and dual regulation by both mechanisms may be important for proper cellular control of moesIn-mediated linkages between the actin cytoskeleton and the plasma membrane.
Moesin Interacts with the Cytoplasmic Region of Intercellular Adhesion Molecule-3 and Is Redistributed to the Uropod of T Lymphocytes during Cell Polarization
- J. Serrador, J. Alonso-Lebrero, F. Sánchez‐Madrid
- BiologyThe Journal of cell biology
- 22 September 1997
Biochemical and immunofluorescence data indicate that moesin interacts with ICAM-3 and CD44 adhesion molecules in uropods of polarized T cells; these data suggest that these interactions participate in the formation of links between membrane receptors and the cytoskeleton, thereby regulating morphological changes during cell locomotion.
The glomerular epithelial cell anti-adhesin podocalyxin associates with the actin cytoskeleton through interactions with ezrin.
- R. Orlando, T. Takeda, M. Farquhar
- BiologyJournal of the American Society of Nephrology…
- 1 August 2001
Data indicate that in podocytes, podocalyxin is complexed with ezrin, which mediates its link to the actin cytoskeleton and likely contributes to maintaining the unique podocyte morphology.
Human glioma-mesenchymal extracellular matrix antigen defined by monoclonal antibody.
- M. Bourdon, C. Wikstrand, H. Furthmayr, T. Matthews, D. Bigner
- Biology, MedicineCancer research
- 1 June 1983
The distribution and localization of a glioma-associated antigen defined by monoclonal antibody 81C6 has been examined using human cultured cell lines and tissues and suggest that GMEM may be a useful marker of gliomas in vivo and in vitro.
Cysteine substitutions in epidermal growth factor-like domains of fibrillin-1: distinct effects on biochemical and clinical phenotypes.
- I. Schrijver, W. Liu, T. Brenn, H. Furthmayr, U. Francke
- Biology, MedicineAmerican journal of human genetics
- 1 October 1999
Ocular manifestations were among the most consistent features (ectopia lentis in 86%, myopia in 80%).
Moesin: a member of the protein 4.1-talin-ezrin family of proteins.
The data indicate that moesin is identical to the 77-kDa band that copurifies with ezrin in its isolation from human placenta, and a similar role for moesIn is implied by structure and domain predictions derived from the cDNA-deduced peptide sequence.