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Eunju Kim

Publications and source records attributed to Eunju Kim.

6 recordsLinked to original sources
PubMed2006

Alternative splicing generates a novel non-secretable cytosolic isoform of NELL2.

NELL2 is as a neuron-specific secreted glycoprotein. The present study provides evidence of an alternatively spliced variant of the rat NELL2 gene that yields cytosolic NELL2 (cNELL2). cNELL2 was initially detected in the thymus and subsequently found to be ubiquitously expressed in many other tissues. The absence of the sequences corresponding to the third exon, which contains the terminal portion of the signal peptide, accounts for the uniform distribution of cNELL2 throughout the cytoplasm. This is in contrast to NELL2, which is preferentially located at distinct subcellular structures involved in the secretary process, such as endoplasmic reticulum and Golgi apparatus. Western blot analysis showed that cNELL2 was not present in the medium but only in lysates, while NELL2 was detected as a glycosylated larger form in both lysates and media. Immunoprecipitation analysis revealed that cNELL2 interacts with PKCbeta1. These results suggest that cNELL2 is involved in PKCbeta1-mediated intracellular signaling.

Alternative Splicing↗
PubMed2005

Crystal structure and morphology of poly(16-hexadecalactone) chain-folded lamellar crystals.

Solution-grown, chain-folded lamellar crystals of poly(16-hexadecalactone) (PHDL) were crystallized isothermally from 1-hexanol at 70 degrees C. The morphology of lozenge-shaped crystals was studied by TEM and AFM. The lamellae are ca. 10 nm thick and the chains run orthogonal to the lamellar surface with folding along (110) and (110) planes. The crystal structure of PHDL was determined by XRD and election diffraction of single crystals. The chains are in the 2(1) helix conformation close to all-trans and the structure consists of an orthorhombic unit cell with a P2(1)2(1)2(1) space group with the lattice constants a = 0.746 +/- 0.001 nm, b = 0.504 +/- 0.001 nm, and c (chain axis) = 4.116 +/- 0.003 nm. There are two chains per unit cell, which exist in an antiparallel arrangement. Molecular packing structure has been studied in detail, taking into account both diffraction data and energy calculations. The setting angles, with respect to a axis, were +/-40 degrees for the corner and center chains, respectively. By using the electron and XRD data, the best molecular packing model was refined to R-factors of 0.168 and 0.196, respectively. A brief comparison of chain-packing structure is also made with related polymer structures.

Crystallization↗
PubMed2005

POSBIOTM-NER: a trainable biomedical named-entity recognition system.

SUMMARY: POSBIOTM-NER is a trainable biomedical named-entity recognition system. POSBIOTM-NER can be automatically trained and adapted to new datasets without performance degradation, using CRF (conditional random field) machine learning techniques and automatic linguistic feature analysis. Currently, we have trained our system on three different datasets. GENIA-NER was trained based on GENIA Corpus, GENE-NER based on BioCreative data and GPCR-NER based on our own POSBIOTM/NE corpus, respectively, which would be used in GPCR-related pathway extraction.

Algorithms↗
PubMedDate not supplied

Crystal structure and morphology of poly(12-dodecalactone).

Poly(12-dodecalactone) (PDDL) crystals in the form of chain-folded lamellae were prepared by isothermal crystallization from a 1-hexanol solution. The lozenge-shaped crystals with and without spiral growth have been studied by transmission electron microscopy and atomic force microscopy. Wide-angle X-ray diffraction data, obtained from PDDL lamellae sedimented to form oriented mats and annealed solvent-cast film, were supplemented with morphological and structural data from electron microscopy. PDDL crystallizes as an orthorhombic form with a P2(1)2(1)2(1) space group and lattice constants of a = 0.746 +/- 0.001 nm, b = 0.500 +/- 0.001 nm, and c (chain axis) = 3.281 +/- 0.003 nm. There are two chains per unit cell, which existed in an antiparallel arrangement. The fiber repeat distance is appropriate for an all-trans backbone conformation for the straight stems. Molecular packing of this structure has been studied in detail, taking into account both diffraction data and energy calculations. The setting angles, with respect to the a axis, were +/-43 degrees for the corner and center chains according to intensity measurements and structure factor calculations. The optimized shift along the crystallographic c axis is 0.1c (0.328 nm). A final model was obtained to yield R = 0.180 with X-ray diffraction data and R = 0.162 with electron diffraction data. A brief comparison is also made with related polymer structures.

Biocompatible Materials↗