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1.  Morphological evidences in circumvallate papilla and von Ebners' gland development in mice 
Anatomy & Cell Biology  2011;44(4):274-283.
In rodents, the circumvallate papilla (CVP), with its underlying minor salivary gland, the von Ebners' gland (VEG), is located on the dorsal surface of the posterior tongue. Detailed morphological processes to form the proper structure of CVP and VEG have not been properly elucidated. In particular, the specific localization patterns of taste buds in CVP and the branching formation of VEG have not yet been elucidated. To understand the developmental mechanisms underlying CVP and VEG formation, detailed histological observations of CVP and VEG were examined using a three-dimensional computer-aided reconstruction method with serial histological sections and pan-Cytokeratins immunostainings. In addition, to define the developmental processes in CVP and VEG formation, we examined nerve innervations and cell proliferation using microinjections of AM1-43 and immunostainings with various markers, including phosphoinositide 3-kinase, Ki-67, PGP9.5, and Ulex europaeus agglutinin 1 (UEA1). Results revealed specific morphogenesis of CVP and VEG with nerve innervations patterns, evaluated by the coincided localization patterns of AM1-43 and UEA1. Based on these morphological and immunohistochemical results, we suggest that nerve innervations and cell proliferations play important roles in the positioning of taste buds in CVP and branching morphogenesis of VEG in tongue development.
doi:10.5115/acb.2011.44.4.274
PMCID: PMC3254881  PMID: 22254156
Circumvallate papilla; von Ebners glands; Epithelial differentiation; AM1-43 microinjections; 3D computer-aided reconstruction
2.  Purification, crystallization and preliminary crystallographic study of the putative enolase MJ0232 from the hyperthermophilic archaeon Methanococcus jannaschii  
The putative enolase MJ0232 from M. jannaschii was purified and crystallized. A native data set was collected to 1.85 Å resolution. Preliminary crystallographic analysis and a dynamic light-scattering experiment suggested biological relevance of the octameric state of MJ0232 in solution.
Enolase is a glycolytic enzyme that catalyzes the interconversion of phospho­enolpyruvate and 2-phosphoglycerate. In order to gain insight into the biological significance of the oligomeric state of this enzyme, the putative enolase MJ0232 from the hyperthermophilic archaeon Methanococcus jannaschii was cloned, overexpressed and purified. Crystals were obtained by the oil-microbatch method at 291 K using PEG 4000 as a precipitant. A native data set was collected to 1.85 Å resolution. The crystal belonged to the tetragonal space group I4, with unit-cell parameters a = 148.8, c = 91.2 Å. An initial model was obtained by molecular replacement, which revealed an octameric subunit association (a tetramer of dimers). This result is consistent with that from a dynamic light-scattering experiment, suggesting biological relevance of the octameric state of MJ0232 in solution.
doi:10.1107/S1744309108034180
PMCID: PMC2581696  PMID: 18997349
glycolysis; oligomers; phosphoenolpyruvate; enolases; hyperthermophiles; archaea
3.  Purification, crystallization and initial X-ray crystallographic analysis of the putative GTPase PH0525 from Pyrococcus horikoshii OT3 
The putative GTPase PH0525 from P. horikoshii OT3 was crystallized using the microbatch method. Crystals were formed under two different conditions, providing two distinct crystal forms. Diffraction data from the two forms were measured to resolution limits of 2.30 and 2.40 Å and processed in space groups P21 and C2221, respectively.
GTPases are involved in diverse cellular functions including cell proliferation, cytoskeleton organization and intracellular traffic. The putative GTPase PH0525 from Pyrococcus horikoshii OT3 has been overexpressed in Escherichia coli and purified. Two distinct crystal forms were grown by the microbatch method at 291 K using a very high protein concentration (80 mg ml−1). Native data sets extending to resolutions of 2.3 and 2.4 Å have been collected and processed in space groups P21 and C2221, respectively. Assuming the presence of one monomer per asymmetric unit gives V M values of 2.6 and 2.4 Å3 Da−1 for the P21 and C2221 forms, respectively, which is consistent with dynamic light-scattering experiments, which show a monomeric state of the protein in solution.
doi:10.1107/S1744309105027752
PMCID: PMC1991311  PMID: 16511188
GTP-binding protein; guanosine triphosphatase; Pyrococcus horikoshii OT3

Results 1-3 (3)