نتایج جستجو برای: vimentin

تعداد نتایج: 6516  

2006
Connie L. Sommers Dorothy Walker-Jones Susan E. Heckford Peter Worland Eva Valverius Robin Clark Frank McCormick Martha Stampfer Silvia Abularach Edward P. Gelmann

To characterize differences in gene expression between hormonedependent and hormone-independent mammary carcinoma, we cloned complementary DNAs of genes expressed in a hormone-independent breast carcinoma cell line that were not expressed in a hormone-depend ent line. One clone, which was isolated in many copies, coded for the intermediate filament protein vimentin. A complementary DNA clone 1....

Journal: :Journal of virology 2014
Ning Du Haolong Cong Hongchao Tian Hua Zhang Wenliang Zhang Lei Song Po Tien

UNLABELLED Enterovirus 71 (EV71) is a highly transmissible pathogenic agent that causes severe central nervous system diseases in infected infants and young children. Here, we reported that EV71 VP1 protein could bind to vimentin intermediate filaments expressed on the host cell surface. Soluble vimentin or an antibody against vimentin could inhibit the binding of EV71 to host cells. Accompanie...

Journal: :PLoS ONE 2009
Billow A. Ahmed Irfan A. Bukhari Brandon C. Jeffus Justin T. Harney Sheeno Thyparambil Endrit Ziu Mony Fraer Nancy J. Rusch Piotr Zimniak Vladimir Lupashin Dale Tang Fusun Kilic

BACKGROUND The C-terminus of the serotonin transporter (SERT) contains binding domains for different proteins and is critical for its functional expression. In endogenous and heterologous expression systems, our proteomic and biochemical analysis demonstrated that an intermediate filament, vimentin, binds to the C-terminus of SERT. It has been reported that 5HT-stimulation of cells leads to dis...

Journal: :Journal of cell science 2008
Roland Bornheim Martin Müller Uschi Reuter Harald Herrmann Heinrich Büssow Thomas M Magin

Vimentin is the main intermediate filament (IF) protein of mesenchymal cells and tissues. Unlike other IF-/- mice, vimentin-/- mice provided no evidence of an involvement of vimentin in the development of a specific disease. Therefore, we generated two transgenic mouse lines, one with a (R113C) point mutation in the IF-consensus motif in coil1A and one with the complete deletion of coil 2B of t...

Journal: :The Journal of Cell Biology 1982
P Laurila I Virtanen V P Lehto T Vartio S Stenman

The expression of intermediate filaments of the keratin- and the vimentin-type was studied in heterokaryons of human fibroblasts and amnion epithelial cells by immunofluorescence microscopy. Fibroblasts and their homokaryons showed a fibrillar, vimentin-specific fluorescence throughout the cytoplasm but were negative when stained for keratin. Amnion epithelial cells and their homokaryons, on t...

Journal: :The Journal of Cell Biology 1985
S D Georgatos V T Marchesi

We have characterized the association of the intermediate filament protein, vimentin, with the plasma membrane, using radioiodinated lens vimentin and various preparations of human erythrocyte membrane vesicles. Inside-out membrane vesicles (IOVs), depleted of spectrin and actin, bind I125-vimentin in a saturable manner unlike resealed, right-side-out membranes which bind negligible amounts of ...

Journal: :Nanoscale 2021

We mechanically tested partially phosphorylated vimentin intermediate filaments using optical traps and found that the additional charges considerably soften filaments.

Journal: :Proceedings of the National Academy of Sciences 2017

2018
Pallab Ghosh Elizabeth M Halvorsen Dustin A Ammendolia Nirit Mor-Vaknin Mary X D O'Riordan John H Brumell David M Markovitz Darren E Higgins

Listeria monocytogenes is a facultative intracellular bacterial pathogen that is frequently associated with food-borne infection. Of particular concern is the ability of L. monocytogenes to breach the blood-brain barrier, leading to life-threatening meningitis and encephalitis. The mechanisms used by bacterial pathogens to infect the brain are not fully understood. Here we show that L. monocyto...

2013
Paola Bargagna-Mohan Sunil P. Deokule Kyle Thompson John Wizeman Cidambi Srinivasan Sunil Vooturi Uday B. Kompella Royce Mohan

Withaferin A (WFA) is a natural product that binds to soluble forms of the type III intermediate filament (IF) vimentin. Currently, it is unknown under what pathophysiological contexts vimentin is druggable, as cytoskeltal vimentin-IFs are abundantly expressed. To investigate druggability of vimentin, we exploited rabbit Tenon's capsule fibroblast (RbTCF) cell cultures and the rabbit glaucoma f...

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