نتایج جستجو برای: alpha tubulin

تعداد نتایج: 212164  

Journal: :The Journal of biological chemistry 2000
L Herreros J L Rodríguez-Fernandez M C Brown J L Alonso-Lebrero C Cabañas F Sánchez-Madrid N Longo C E Turner P Sánchez-Mateos

Paxillin is a focal adhesion-associated protein that functions as a multi-domain adapter protein, binding several structural and signaling molecules. alpha-Tubulin was identified as an interacting protein in a two-hybrid screen using the paxillin C-terminal LIM domain as a bait. In vitro binding assays with glutathione S-transferase-paxillin demonstrated an interaction of alpha-tubulin with the...

2014
Shengyan Xiao Zhongyuan Shen Xudong Tang Li Xu Xuliang Fu Yajie Yue Nan Li Wei Wang

We isolated a microsporidium from the silkworm, Bombyx mori, and classified it as Endoreticulatus sp. Zhenjiang based on morphological characteristics and phylogenetic analyses of ribosomal sequences. This microsporidium causes silkworm pebrine, although its original host and mode of transmission are unknown. To better understand its distribution and transmission mode, it is essential to have s...

Journal: :Journal of cell science 2005
Julia Vent Todd A Wyatt D David Smith Asok Banerjee Richard F Ludueña Joseph H Sisson Richard Hallworth

In previous studies in Drosophila, Nielsen et al. hypothesized that the beta tubulin C-terminal axonemal motif ;EGEFXXX', where X is an acidic amino acid, is required for ciliary function and assembly (Nielsen et al., 2001, Curr. Biol. 11, 529-533). This motif is present in some but not all mammalian beta tubulin isotypes. We therefore investigated whether this motif is important in ciliary fun...

Journal: :The Journal of Cell Biology 1995
H B Shu H C Joshi

alpha-, beta-, and gamma-tubulins are evolutionarily highly conserved members of the tubulin gene superfamily. While the abundant members, alpha- and beta-tubulins, constitute the building blocks of cellular microtubule polymers, gamma-tubulin is a low abundance protein which localized to the pericentriolar material and may play a role in microtubule assembly. To test whether gamma-tubulin medi...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1986
U Z Littauer D Giveon M Thierauf I Ginzburg H Ponstingl

A specific binding assay was developed that monitors the interaction of 125I-labeled microtubule-associated proteins (MAPs) with tubulin or its fragments bound to nitrocellulose membrane. To identify the tubulin-binding domains for MAPs we have examined the binding of rat brain 125I-labeled MAP2 or 125I-labeled tau factors to 60 peptides derived from porcine alpha- and beta-tubulin. MAP2 and ta...

2010
Bilal A. Azakir Sabrina Di Fulvio Christian Therrien Michael Sinnreich

Dysferlin is a type II transmembrane protein implicated in surface membrane repair in muscle. Mutations in dysferlin lead to limb girdle muscular dystrophy 2B, Miyoshi Myopathy and distal anterior compartment myopathy. Dysferlin's mode of action is not well understood and only a few protein binding partners have thus far been identified. Using affinity purification followed by liquid chromatogr...

2010
Jachen A. Solinger Roberta Paolinelli Holger Klöß Francesco Berlanda Scorza Stefano Marchesi Ursula Sauder Dai Mitsushima Fabrizio Capuani Stephen R. Stürzenbaum Giuseppe Cassata

Although acetylated alpha-tubulin is known to be a marker of stable microtubules in neurons, precise factors that regulate alpha-tubulin acetylation are, to date, largely unknown. Therefore, a genetic screen was employed in the nematode Caenorhabditis elegans that identified the Elongator complex as a possible regulator of alpha-tubulin acetylation. Detailed characterization of mutant animals r...

Journal: :The EMBO journal 2010
Seiichi Uchimura Yusuke Oguchi You Hachikubo Shin'ichi Ishiwata Etsuko Muto

Microtubule (MT) binding accelerates the rate of ATP hydrolysis in kinesin. To understand the underlying mechanism, using charged-to-alanine mutational analysis, we identified two independent sites in tubulin, which are critical for kinesin motility, namely, a cluster of negatively charged residues spanning the helix 11-12 (H11-12) loop and H12 of alpha-tubulin, and the negatively charged resid...

Journal: :Iranian biomedical journal 2007
Shahin Ahmadian Yaghub Pazhang Ahmad Shariftabrizi

BACKGROUND Microtubules (MT) are important components of cell cytoskeleton and play key roles in cell motility mitosis and meiosis. They are also the targets of several anticancer agents which indicating their importance in maintaining cell viability. Microtubular reorganization contributing to apoptotic morphology occurs in normal and neoplastic cells undergoing apoptosis induced by cytotoxic ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1984
L C Morejohn T E Bureau L P Tocchi D E Fosket

We have initiated immunological and drug-binding studies on the tubulins from different higher plant species. Antibodies were raised against electrophoretically separated rose (Rosa sp.) tubulin alpha- and beta-subunits and characterized by immunoblot autoradiographic assays. Each IgG preparation bound to its antigen and cross-reacted differentially with the respective tubulin subunits from an ...

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