• Proceedings of the Zoological Society Korea Conference
• /
• 2001.10a
• /
• pp.264.2-265
• /
• 2001

No Abstract, See Full Text

• Proceedings of the Zoological Society Korea Conference
• /
• 2003.08a
• /
• pp.177.4-177
• /
• 2003

No Abstract, See Full Text

• Proceedings of the Zoological Society Korea Conference
• /
• 2001.10a
• /
• pp.264.1-264
• /
• 2001

No Abstract, See Full Text

• Proceedings of the Korean Society for Applied Microbiology Conference
• /
• 2001.06a
• /
• pp.7-8
• /
• 2001

• Proceedings of the Korean Society of Plant Biotechnology Conference
• /
• 2002.04b
• /
• pp.163-163
• /
• 2002

• Proceedings of the Zoological Society Korea Conference
• /
• 2001.10a
• /
• pp.193.3-194
• /
• 2001

No Abstract, See Full Text

• 한국생물공학회:학술대회논문집
• /
• 2005.10a
• /
• pp.848-848
• /
• 2005

• Animal cells and systems
• /
• v.7 no.1
• /
• pp.81-87
• /
• 2003

While screening proteins that interact with DnaA protein, the initiator protein for Escherichia coil chromosomal DNA replication, we found a 52-kD sized protein which bound to DnaA protein in a salt-dependent manner. This protein was identified as trigger factor, a ribosome-associated peptidyl-prolyl- cisltrans isomerase with chaperone activity. Trigger factor was overproduced and purified to near homogeneity, and its effect on the function of DnaA protein was examined, Enhanced binding of DnaA protein to DnaA box with no apparent supershift in the gel-shift experiments suggested that trigger factor, by virtue of its chaperone activity, exerts a change on DnaA protein thus increasing its binding affinity for DnaA box.

• Proceedings of the Zoological Society Korea Conference
• /
• 2003.08a
• /
• pp.193.3-193
• /
• 2003

No Abstract, See Full Text

• Proceedings of the Zoological Society Korea Conference
• /
• 2003.08a
• /
• pp.194.3-194
• /
• 2003

No Abstract, See Full Text