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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
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Disease relevance of Gizzard

  • These results included studies with gizzard vinculin, its proteolytic head and tail fragments, and recombinant proteins containing various gizzard vinculin sequences fused to the maltose binding protein (MBP) of Escherichia coli [1].
  • We have isolated, without heat treatment, full-length recombinant chicken gizzard CaD overexpressed in insect cells (High-FiveTM) using a baculovirus expression system [2].
  • Polyclonal antibodies to the avian integrin alpha 1-subunit block attachment of embryonic gizzard cells to human and chick collagen IV completely and inhibit attachment to mouse Engelbreth-Holm-Swarm (EHS) tumor laminin partially [3].
  • Gout and mortality were absent at 0 and 500 micrograms/g. In addition to tissue urate deposition, necropsies revealed dehydration, swollen pale kidneys, hemorrhagic proventriculitis with mucosal necrosis, gizzard enlargement and lining discoloration, an increase in gall bladder size, and focal hepatic necrosis [4].
  • Pathogenicity by parenteral injection of fowl adenovirus isolated from gizzard erosion and resistance to reinfection in adenoviral gizzard erosion in chickens [5].

Psychiatry related information on Gizzard

  • To optimize the parameters of labeling protein with IIE, a systematic assessment of the effects of pH, reactant concentrations, and reaction time was made using purified cardiac actin and gizzard alpha-actinin [6].

High impact information on Gizzard

  • Limited chymotryptic cleavage of soluble chicken gizzard desmin protofilaments allows the characterization of three structurally distinct domains [7].
  • Mobility of microinjected rhodamine actin within living chicken gizzard cells determined by fluorescence photobleaching recovery [8].
  • A specific precipitating antibody against chicken gizzard myosin light chain kinase (MLCK) has been produced in rabbits [9].
  • Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca2+-and Sr2+-dependent changes in phosphorylation [10].
  • Here, we investigated the signaling pathways involved in de-differentiation of gizzard SMCs induced by PDGF-BB, bFGF, and EGF [11].

Chemical compound and disease context of Gizzard


Biological context of Gizzard


Anatomical context of Gizzard


Associations of Gizzard with chemical compounds

  • Rhodamine-labeled actin microinjected into living embryonic chicken gizzard cells became associated with its characteristic cytoskeletal structures [8].
  • The major proteins remaining in the ghosts comigrate, on polyacrylamide gels in the presence of SDS, with chicken gizzard actin, myosin, filamin, and a 110-kdalton protein [25].
  • We have reported that a glycoprotein of approximately 82 kD solubilized from gizzard muscles binds to NOF (ligand blotting) and inhibits the neurite promoting activity of NOF (inhibition assay) [26].
  • We have recorded electron microscope images of negatively stained thin filaments containing caldesmon and tropomyosin which were isolated from chicken gizzard smooth muscle in EGTA [27].
  • Proteins phosphorylated on tyrosine were found to be present in all the embryonic tissues examined, including heart, thigh, gizzard, intestine, lung, liver, kidney, brain, and lens, from 7 to 21 d of development in ovo, but were greatly reduced or absent in the same tissues taken from adult chickens [28].

Gene context of Gizzard

  • The subcellular distribution, the biochemical properties, as well as microsequencing data revealed that porcine platelet p83 is related to chicken gizzard zyxin and most likely represents the mammalian equivalent of the chicken protein [29].
  • Moreover, SOX9 is also expressed at the mesoderm of the pyloric sphincter, a structure that demarcates the gizzard from the duodenum [30].
  • One member of the S100 protein family is S100A11, first isolated from chicken gizzard and termed calgizzarin [31].
  • In the esophagus and gizzard, where HAND1 is not normally expressed, treatment with BMP4 induced the expression of transcripts encoding HAND1 in nonneural crest-derived cells [32].
  • In the present study, we produced a polyclonal antibody to chicken gizzard talin [33].

Analytical, diagnostic and therapeutic context of Gizzard

  • For this purpose, we used several monoclonal antibodies raised against chicken gizzard vinculin whose epitopes could be assigned to discrete regions in the vinculin sequence by immunoblotting of proteolytic fragments combined with N-terminal amino acid sequencing [34].
  • Finally, two-dimensional peptide mapping of iodinated tryptic peptides, as well as one-dimensional fingerprinting of partial tryptic, chymotryptic, papain, and S. aureus V8 protease digests, have revealed less than 5% homology between gizzard alpha-actinin and brush-border 95-kdalton polypeptide [23].
  • Antibodies to myosin light chain kinase, purified from turkey gizzard smooth muscle, were developed in rabbits and purified by affinity chromatography on a myosin light chain kinase-Sepharose 4B column [35].
  • The thermal and the urea-induced unfolding profiles of the coiled-coil alpha-helix of native and refolded tropomyosin from chicken gizzard were studied by circular dichroism [36].
  • A partial separation of the mRNAs coding for tropomyosins alpha 1 and gamma 1 was obtained by fractionation of gizzard RNA by zonal centrifugation in sucrose gradients [37].


  1. Characterization of an F-actin-binding domain in the cytoskeletal protein vinculin. Menkel, A.R., Kroemker, M., Bubeck, P., Ronsiek, M., Nikolai, G., Jockusch, B.M. J. Cell Biol. (1994) [Pubmed]
  2. Heat treatment could affect the biochemical properties of caldesmon. Zhuang, S., Mabuchi, K., Wang, C.A. J. Biol. Chem. (1996) [Pubmed]
  3. An abundant chick gizzard integrin is the avian alpha 1 beta 1 integrin heterodimer and functions as a divalent cation-dependent collagen IV receptor. Syfrig, J., Mann, K., Paulsson, M. Exp. Cell Res. (1991) [Pubmed]
  4. Oosporein-toxicosis in the turkey poult. Pegram, R.A., Wyatt, R.D., Smith, T.L. Avian Dis. (1982) [Pubmed]
  5. Pathogenicity by parenteral injection of fowl adenovirus isolated from gizzard erosion and resistance to reinfection in adenoviral gizzard erosion in chickens. Ono, M., Okuda, Y., Shibata, I., Sato, S., Okada, K. Vet. Pathol. (2004) [Pubmed]
  6. Preparation and reactions of an iodinated imidoester reagent with actin and alpha-actinin. Bright, G.R., Spooner, B.S. Anal. Biochem. (1983) [Pubmed]
  7. Proteinchemical characterization of three structurally distinct domains along the protofilament unit of desmin 10 nm filaments. Geisler, N., Kaufmann, E., Weber, K. Cell (1982) [Pubmed]
  8. Mobility of microinjected rhodamine actin within living chicken gizzard cells determined by fluorescence photobleaching recovery. Kreis, T.E., Geiger, B., Schlessinger, J. Cell (1982) [Pubmed]
  9. Production and characterization of an antibody to myosin light chain kinase and intracellular localization of the enzyme. Guerriero, V., Rowley, D.R., Means, A.R. Cell (1981) [Pubmed]
  10. Chicken gizzard: relation between calcium-activated phosphorylation and contraction. Hoar, P.E., Kerrick, W.G., Cassidy, P.S. Science (1979) [Pubmed]
  11. Changes in the balance of phosphoinositide 3-kinase/protein kinase B (Akt) and the mitogen-activated protein kinases (ERK/p38MAPK) determine a phenotype of visceral and vascular smooth muscle cells. Hayashi, K., Takahashi, M., Kimura, K., Nishida, W., Saga, H., Sobue, K. J. Cell Biol. (1999) [Pubmed]
  12. Fumonisin toxicity in broiler chicks. Ledoux, D.R., Brown, T.P., Weibking, T.S., Rottinghaus, G.E. J. Vet. Diagn. Invest. (1992) [Pubmed]
  13. Effects of cimetidine on broiler fattening and on stress-induced gizzard erosion in chicken. Grabarević, Z., Dzaja, P., Perić, J., Serman, V., Bidin, Z., Mazija, H., Mas, N., Mikulec, Z., Culjak, K., Simec, Z., Njari, B. Acta Vet. Hung. (1999) [Pubmed]
  14. Pathogenicity of fowl adenovirus isolated from gizzard erosions to immuno-suppressed chickens. Muroga, N., Taharaguchi, S., Ohta, H., Yamazaki, K., Takase, K. J. Vet. Med. Sci. (2006) [Pubmed]
  15. Cloning and characterization of mammalian myosin regulatory light chain (RLC) cDNA: the RLC gene is expressed in smooth, sarcomeric, and nonmuscle tissues. Taubman, M.B., Grant, J.W., Nadal-Ginard, B. J. Cell Biol. (1987) [Pubmed]
  16. Bundling of actin filaments by alpha-actinin depends on its molecular length. Meyer, R.K., Aebi, U. J. Cell Biol. (1990) [Pubmed]
  17. Cloning and characterization of a vertebrate cellular myosin regulatory light chain complementary DNA. Zavodny, P.J., Petro, M.E., Lonial, H.K., Dailey, S.H., Narula, S.K., Leibowitz, P.J., Kumar, C.C. Circ. Res. (1990) [Pubmed]
  18. The chicken tropomyosin 1 gene generates nine mRNAs by alternative splicing. Forry-Schaudies, S., Hughes, S.H. J. Biol. Chem. (1991) [Pubmed]
  19. Role of myosin phosphatase isoforms in cGMP-mediated smooth muscle relaxation. Khatri, J.J., Joyce, K.M., Brozovich, F.V., Fisher, S.A. J. Biol. Chem. (2001) [Pubmed]
  20. Identification and localization of immunoreactive forms of caldesmon in smooth and nonmuscle cells: a comparison with the distributions of tropomyosin and alpha-actinin. Bretscher, A., Lynch, W. J. Cell Biol. (1985) [Pubmed]
  21. Nerve fibers in culture and their interactions with non-neural cells visualized by immunofluorescence. Jockusch, H., Jockusch, B.M., Burger, M.M. J. Cell Biol. (1979) [Pubmed]
  22. Molecular cloning, expression, and mapping of the high affinity actin-capping domain of chicken cardiac tensin. Chuang, J.Z., Lin, D.C., Lin, S. J. Cell Biol. (1995) [Pubmed]
  23. Comparison of intestinal brush-border 95-Kdalton polypeptide and alpha-actinins. Craig, S.W., Lancashire, C.L. J. Cell Biol. (1980) [Pubmed]
  24. Switching of filamin polypeptides during myogenesis in vitro. Gomer, R.H., Lazarides, E. J. Cell Biol. (1983) [Pubmed]
  25. Transmembrane linkage between surface glycoproteins and components of the cytoplasm in neutrophil leukocytes. Sheterline, P., Hopkins, C.R. J. Cell Biol. (1981) [Pubmed]
  26. Purification and characterization of an 82-kD membrane protein as a neurite outgrowth factor binding protein: possible involvement of NOF binding protein in axonal outgrowth in developing retina. Taniura, H., Kuo, C.H., Hayashi, Y., Miki, N. J. Cell Biol. (1991) [Pubmed]
  27. Three-dimensional reconstruction of caldesmon-containing smooth muscle thin filaments. Vibert, P., Craig, R., Lehman, W. J. Cell Biol. (1993) [Pubmed]
  28. Tyrosine phosphorylated proteins in different tissues during chick embryo development. Maher, P.A., Pasquale, E.B. J. Cell Biol. (1988) [Pubmed]
  29. Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Reinhard, M., Jouvenal, K., Tripier, D., Walter, U. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  30. SOX9 specifies the pyloric sphincter epithelium through mesenchymal-epithelial signals. Moniot, B., Biau, S., Faure, S., Nielsen, C.M., Berta, P., Roberts, D.J., de Santa Barbara, P. Development (2004) [Pubmed]
  31. 1H, 15N and 13C resonance assignments of rabbit apo-S100A11. Rintala, A.C., Schönekess, B.O., Walsh, M.P., Shaw, G.S. J. Biomol. NMR (2002) [Pubmed]
  32. Transcripts encoding HAND genes are differentially expressed and regulated by BMP4 and GDNF in developing avian gut. Wu, X., Howard, M.J. Gene Expr. (2002) [Pubmed]
  33. Identification and localization of talin in chick retinal pigment epithelial cells. Philp, N.J., Yoon, M.Y., Hock, R.S. Exp. Eye Res. (1990) [Pubmed]
  34. Antibody mapping of functional domains in vinculin. Westmeyer, A., Ruhnau, K., Wegner, A., Jockusch, B.M. EMBO J. (1990) [Pubmed]
  35. Characterization of antibodies to smooth muscle myosin kinase and their use in localizing myosin kinase in nonmuscle cells. de Lanerolle, P., Adelstein, R.S., Feramisco, J.R., Burridge, K. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  36. Unfolding/refolding studies of smooth muscle tropomyosin. Evidence for a chain exchange mechanism in the preferential assembly of the native heterodimer. Lehrer, S.S., Qian, Y. J. Biol. Chem. (1990) [Pubmed]
  37. Separation of the mRNAs coding for different forms of chick embryo gizzard tropomyosin. Segura, M., Saborío, J.L. J. Biol. Chem. (1982) [Pubmed]
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