• 한국동물학회:학술대회논문집
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• 한국동물학회 2000년도 한국생물과학협회 학술발표대회
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• pp.233.2-234
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• 2000

No Abstract, See Full Text

• 한국생물물리학회:학술대회논문집
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• 한국생물물리학회 2002년도 제9회 학술 발표회 프로그램과 논문초록
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• pp.48-48
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• 2002

Glutathione (GSH) is most prevalent reducing thiols in eukaryotic cells and known that participates in many cellular processes. It was found that total amount of glutathione and the ratio of reduced to oxidized glutathione during development of Dictyostelium discoideum increase at the initial stage of the aggregation of amoeba.(omitted)

• 한국생물물리학회:학술대회논문집
• /
• 한국생물물리학회 2001년도 학술 발표회 진행표 및 논문초록
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• pp.50-50
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• 2001

Rhodobacter sphaeroides 2.4.1 is a facultatively photoheterotrophic bacterium. The AppA protein is required for increased photo system gene expression upon transition from aerobic respiration to anaerobic photosynthesis condition. This protein has FAD binding domain in amino terminus and cysteine-rich motif in carboxy terminus.(omitted)

• 한국생물물리학회:학술대회논문집
• /
• 한국생물물리학회 2001년도 학술 발표회 진행표 및 논문초록
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• pp.43-43
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• 2001

In cells of the eukaryotic microorganism Dictyostelium discoideum, at least eight small, four-EF hand calcium-binding proteins respectively are expressed at specific stages during development. One of these proteins, calcium-binding protein 3 (CBP3), first appears just prior to cell aggregation and then maintains relatively constant levels throughout development.(omitted)

• 한국환경성돌연변이발암원학회:학술대회논문집
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• 한국환경성돌연변이발암원학회 2004년도 춘계학술대회
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• pp.35-42
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• 2004

• 한국동물학회:학술대회논문집
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• 한국동물학회 1999년도 한국생물과학협회 학술발표대회
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• pp.232.1-232
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• 1999

No Abstract, See Full Text

• 한국동물학회:학술대회논문집
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• 한국동물학회 1999년도 한국생물과학협회 학술발표대회
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• pp.233.2-233
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• 1999

No Abstract, See Full Text

• 한국동물학회:학술대회논문집
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• 한국동물학회 1999년도 한국생물과학협회 학술발표대회
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• pp.234.1-234
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• 1999

No Abstract, See Full Text

• 한국동물학회:학술대회논문집
• /
• 한국동물학회 1999년도 한국생물과학협회 학술발표대회
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• pp.235.1-235
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• 1999

No Abstract, See Full Text

• BMB Reports
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• 제44권2호
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• pp.102-106
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• 2011

Thermodynamic stability and refolding kinetics of firefly luciferase and three representative mutants with depletion of negative charge on a flexible loop via substitution of Glu by Arg (ER mutant) or Lys (EK mutant) as well as insertion of another Arg in ER mutants (ERR mutant) was investigated. According to thermodynamic studies, structural stability of ERR and ER mutants are enhanced compared to WT protein, whereas, these mutants become prone to aggregation at higher temperatures. Accordingly, it was concluded that enhanced structural stability of mutants depends on more compactness of folded state, whereas aggregation at higher temperatures in mutants is due to weakening of intermolecular repulsive electrostatic interactions and increase of intermolecular hydrophobic interactions. Kinetic results indicate that early events of protein folding are accelerated in mutants.