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CAPZA1 capping protein (actin filament) muscle Z-line, alpha 1

CapZ alpha, CapZ alpha 1
Top mentioned proteins: Actin, Alpha-1, S-100, fibrillin-1, ACID
Papers on CapZ alpha
Disease Causing mutations in Inverted Formin 2 regulate its binding to G-actin, F-actin capping protein (CapZ alpha-1) and Profilin 2.
Welsh et al., Bristol, United Kingdom. In Biosci Rep, Feb 2016
Furthermore using a combination of GFP-INF2 expression in human podocytes and GFP-Trap purification coupled with Mass Spectrometry we demonstrate that INF2 interacts with profilin 2 and the F-actin capping protein, CapZ alpha-1.
Evolutionary conservation of the WASH complex, an actin polymerization machine involved in endosomal fission.
Gautreau et al., Gif-sur-Yvette, France. In Commun Integr Biol, 2010
This analysis supports the idea that the invention of the WASH complex has involved the incorporation of an independent complex, the CapZ alpha/beta heterodimer, forming the so-called Capping Protein (CP), as illustrated by the yeasts S. cerevisiae and S. pombe, which possess the CP heterodimer but no other subunits of the WASH complex.
S100A8 is identified as a biomarker of HPV18-infected oral squamous cell carcinomas by suppression subtraction hybridization, clinical proteomics analysis, and immunohistochemistry staining.
Tsai et al., Taiwan. In J Proteome Res, 2007
Clinical proteomics analysis indicated that there was over 10-fold overexpression of Stratifin, F-actin capping protein alpha-1 subunit (CapZ alpha-1), Apolipoprotein A-1 (ApoA-1), Heat-shock protein 27 (HSP27), Arginase-1, p16INK4A, and S100 calcium-binding protein A8 (S100A8) in HPV18+ OSCC.
Identification of novel citrullinated autoantigens of synovium in rheumatoid arthritis using a proteomic approach.
Kato et al., Kawasaki, Japan. In Arthritis Res Ther, 2005
They contained three fibrinogen derivatives and several novel citrullinated autoantigens (for example, asporin and F-actin capping protein alpha-1 subunit [CapZalpha-1]).
Interaction of actin with the capping protein, CapZ from sea bass (Dicentrarchus labrax) white skeletal muscle.
Roustan et al., Montpellier, France. In Comp Biochem Physiol B Biochem Mol Biol, 2000
Finally, the partial competition of antibodies directed against CapZ alpha or beta-subunits towards CapZ interaction with actin filaments suggests both subunits participate in the complex with actin.
Hydrophobic residues in the C-terminal region of S100A1 are essential for target protein binding but not for dimerization.
Gerke et al., M√ľnster, Germany. In Cell Calcium, 1998
Chemical cross-linking, ligand blotting and fluorescence emission spectroscopy reveal that removal of, or mutations within, the sequence encompassing residues 88-90 in the unique C-terminal region of S100A1 interfere with binding to CapZ alpha and to TRTK-12, a synthetic CapZ alpha peptide.
Identification of the binding site on S100B protein for the actin capping protein CapZ.
Roberts et al., Leicester, United Kingdom. In Protein Sci, 1997
We have made backbone assignments of the calcium-bound form of S100B and used chemical-shift changes in spectra of 15N-labeled protein to locate the site that binds a peptide corresponding to residues 265-276 from CapZ alpha, the actin capping protein.
Interaction of S100a0 protein with the actin capping protein, CapZ: characterization of a putative S100a0 binding site in CapZ alpha-subunit.
Jamieson et al., Cincinnati, United States. In Biochem Biophys Res Commun, 1996
TRTK-12, a peptide contained within the COOH-terminal region of CapZalpha, inhibited S100a0: CapZ interaction in a dose-dependent manner.
Characterization of S-100b binding epitopes. Identification of a novel target, the actin capping protein, CapZ.
Dimlich et al., Cincinnati, United States. In J Biol Chem, 1995
amino acids 265-276 in CapZ alpha 1 and CapZ alpha 2), was synthesized and shown by fluorescence spectrophotometry to bind S-100b in a Ca(2+)-dependent manner.
Variant cDNAs encoding proteins similar to the alpha subunit of chicken CapZ.
Casella et al., Saint Louis, United States. In Cell Motil Cytoskeleton, 1990
alpha 2 predicts a protein sequence that matches exactly the N-terminal sequence of 5 peptides prepared from CapZ alpha purified from chicken muscle, while the protein sequence predicted by alpha 1 matches the peptides well, but not exactly.
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