• International Journal of Industrial Entomology and Biomaterials
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• v.9 no.1
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• pp.149-153
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• 2004

Here we report the molecular cloning of a LIM protein cDNA of the CRP (cysteine-rich protein) family from the mulberry longicorn beetle, Apriona, geramri. The A. germari LIM protein cDNA contains an open reading frame of 276 bp encoding 92 amino acid residues with a calculated molecular weight of approximately 10 kDa. The A. germari LIM protein contains the cysteine-rich consensus sequence of LIM domain and the glycine-rich consensus sequence observed in cysteine-rich protein family 1 (CRP1). The potential nuclear targeting signal is retained. The deduced amino acid sequence of the A. germari LIM protein cDNA showed 81 % identity to both Bombyx mori muscle LIM protein (Mlp) and Drosophila melanogaster Mlp60A and 77% to Epiblema scudderiana Mlp. Northern blot analysis showed that A. germari LIM protein is highly expressed in epidermis and muscle, and less strongly in midgut, but not in the fat body.

• International Journal of Industrial Entomology and Biomaterials
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• v.11 no.1
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• pp.71-74
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• 2005

A LIM protein gene homologue of the CRP (cysteine­rich protein) family in the whiter-spotted flower chafer, Protaetia brevitarsis, was cloned. The P. brevitarsis LIM protein cDNA encodes a 92 amino acid polypep­tide with a predicted molecular mass of 10,030 Da and a pI of 8.57. The P. brevitarsis LIM protein contains the cysteine-rich consensus sequence of LIM domain and the glycine-rich consensus sequence observed in the cysteine-rich protein family 1 (CRPl). The potential nuclear targeting signal is retained. The deduced amino acid sequence of the P. brevitarsis LIM protein cDNA showed 92$\%$ identity to another beetle, Apriona germari LIM protein. Northern blot analysis showed that P. brevitarsis LIM protein is highly expressed in epidermis and midgut, but not in the fat body.

• Asian-Australasian Journal of Animal Sciences
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• v.20 no.10
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• pp.1473-1477
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• 2007

Four-and-a-half LIM-only protein 3 (FHL3) is a member of the LIM protein superfamily and can participate in mediating protein-protein interaction by binding one another through their LIM domains. In this study, the 5'- and 3'- cDNA ends were characterized by RACE (Rapid Amplification of the cDNA Ends) methodology in combination with in silico cloning based on the partial cDNA sequence obtained. Bioinformatics analysis showed FHL3 protein contained four LIM domains and four LIM zinc-binding domains. In silico mapping assigned this gene to the gene cluster MTF1-INPP5B-SF3A3-FHL3-CGI-94 on pig chromosome 6 where several QTL affecting intramuscular fat and eye muscle area had previously been identified. Transcription of the FHL3 gene was detected in spleen, liver, kidney, small intestine, skeletal muscle, fat and stomach, with the greatest expression in skeletal muscle. The A/G polymorphism in exon II was significantly associated with birth weight, average daily gain before weaning, drip loss rate, water holding capacity and intramuscular fat in a Landrace-derived pig population. Together, the present study provided the useful information for further studies to determine the roles of FHL3 gene in the regulation of skeletal muscle cell growth and differentiation in pigs.

• Proceedings of the Zoological Society Korea Conference
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• 1998.10b
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• pp.240.2-240
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• 1998

No Abstract, See Full Text

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2001.05a
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• pp.293-294
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• 2001

In nutrition studies of fish, determining the optimum dietary protein level for growth of fish is generally a primary consideration because protein is not only the major constituent of fish body, but also it has critical functions as enzymes and hormones. Many studies have been carried out to determine the protein requirements of fish, and the estimated protein requirements range from 30％ to 55％ of diet. (omitted)

• ETRI Journal
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• v.37 no.4
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• pp.813-823
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• 2015

Because protein is a primary element responsible for biological or biochemical roles in living bodies, protein function is the core and basis information for biomedical studies. However, recent advances in bio technologies have created an explosive increase in the amount of published literature; therefore, biomedical researchers have a hard time finding needed protein function information. In this paper, a classification system for biomedical literature providing protein function evidence is proposed. Note that, despite our best efforts, we have been unable to find previous studies on the proposed issue. To classify papers based on protein function evidence, we should consider whether the main claim of a paper is to assert a protein function. We, therefore, propose two novel features - protein and assertion. Our experimental results show a classification performance with 71.89% precision, 90.0% recall, and a 79.94% F-measure. In addition, to verify the usefulness of the proposed classification system, two case study applications are investigated - information retrieval for protein function and automatic summarization for protein function text. It is shown that the proposed classification system can be successfully applied to these applications.

• Proceedings of the Korean Magnetic Resonance Society Conference
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• 2002.01a
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• pp.26-26
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• 2002

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2003.05a
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• pp.239-241
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• 2003

Several nutrients in feed are needed for growth and maintenance of fish and protein among them is probably the most important factor influencing its growth and determining feed cost due to high Proportion. Besides, dietary energy level is critical because protein source in the feed was utilized as energy source when the feed deficient in energy was fed to fish, whereas when the feed excess in energy was fed to fish, feed consumption decreased and resulted in growth reduction due to lack of necessary other nutrients for the normal growth (Lovell 1989). (omitted)

• Journal of the Korean Magnetic Resonance Society
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• v.21 no.1
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• pp.26-30
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• 2017

Dynamic properties of proteins can present key information on protein-ligand and protein-protein interaction. Despite their usefulness, the properties of protein dynamics have not been obtained easily due to protein stability and short-term measurement. Here, it is shown that combined method for analysis of dynamical properties. It utilizes predicted order parameter and NMR relaxation data such as $T_1$, $T_2$, and heteronuclear NOE. The suggested method could be used to know the flexibility of protein roughly without precise dynamical parameters such as order parameters through model-free analysis.

• 대한생식의학회:학술대회논문집
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• 2005.11a
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• pp.123.2-124
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• 2005