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Changill Ban, Ph.D. 

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1993-1996
1995-1996
1996-1999
 
1999-2002
 
 
2000-2002
 
2002-present
  

Ph.D., Ohio State University
Post Doc.,The Ohio State University
Visiting Fellow,LMB/NIDDK, National Institutes of Health
Principal Investigator, Research Scientist (II)Hauptman-Woodward Medical Research Institute
Assistant Professor, Medical School in SUNY at Buffalo
Adjunct Professor, Medical School in SUNY at Buffalo/HWI

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E-mail ciban@postech.ac.kr
Phone 054-279-2127 (office) 054-279-3388 (fax)

»ó¼¼ ÇÁ·ÎÇÊ ¹× ¿¬±¸½ÇÀû | ÁÖ¿ä ³í¹® Abstract
  Laboratory Biochemistry & Structural Biology Lab.

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dia_red.gif ÁßÁ¡¿¬±¸ºÐ¾ß (Research Interests)

Biochemistry and Structural Biology - a tool to unlock the secrets of human diseases

The revealing of human genome sequences promises an unprecedented potential for new discoveries in biomedical research.  Dr. Ban's research focuses are the determination of 3D protein structures by X-ray crystallography and NMR studies and the development of a detection method for protein-protein/DNA interactions using the biosensor technique.  The endeavor requires coordinated efforts from a number of disciplines including molecular biology, biochemistry, bioinformatics, and structural biology.  Research topics of Dr.Ban's laboratory include the followings:

Structural studies on DNA repairing protein

Hereditary nonpolyposis colorectal carcinoma (HNPCC) is caused by inherited mutations in some of the gene encoding components of a base-pair mismatch repair pathway.  Dr. Ban and his research staff  are focusing on the continuous structural studies of three proteins such as MutS, MutL and MutH as well as their human homologs.

 

Structural genomics of checkpoint proteins

Understanding the nature of interaction along the checkpoint cascade would reveal how malfunctions of those proteins lead to diseases such as human cancers.  "We will target more than 200 proteins involved in the checkpoint pathway," explains Dr. Ban.

Structural studies on ssDNA binding transcription factors

Transcription activation or repression of RNA polymerase II is often mediated by sequence-specific DNA-binding proteins (i.e. transcription activating factors) that respond to extracellular signals by interacting with critical cis-acting regulatory elements.  Here, they are focusing on structural studies of three key single-strand binding proteins, Pura, Pur¥â, and MSY1 that affect on the human neurodegenerative disease.

Development of electrochemical sensors for the detection and screening of interacting protein partners

Biotechnology and medical diagnostics are currently in need of devices capable of continuously and selectively detecting biological molecules.  "In this project, electrochemical biosensors detecting specific DNA interactions, DNA-protein interactions, and/or protein-protein interactions are under development," says Dr. Ban. .

 

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dia_red.gif ÁÖ¿ä³í¹® (Selected Publications)

Yang, W., Junop, M. S., Ban, C., Obmolova, G., Hsieh, P. (2000). DNA mismatch
repair: From structure to mechanism. Cold Spring Harbor Symposium on Biological responses to DNA damage, 65, 225-232.

Obmolova, G., Ban, C., Heish, P., & Yang, W. (2000). Crystal Structures of Mismatch Repair Protein MutS and its Complex with a Substrate DNA. Nature. 407, 703-710.

Ban, C., Junop, M. & Yang, W. (1999). Transformation of MutL by ATP Binding and Hydrolysis: A Switch in DNA Mismatch Repair. Cell. 97, 85-97.

Biswas, I., Ban, C., Fleming, K. G. Qin, J., Lary J. W., Yphantis D. A., Yang, W. & Hsieh, P. (1999). Oligomerization of a MutS Mismatch Repair Protein from Thermus Aquaticus. J. Biol. Chem. 274, 23673-23678.

Ban, C., & Yang, W. (1998). Crystal Structure and ATPase Activity of MutL: Implications for DNA Repair and Mutagenesis. Cell. 95, 541-552.

Ban, C., & Yang, W. (1998). Structure Basis of MutH Activation in E. coli. Mismatch Repair and Relationship of MutH to Restriction Endonucleases. EMBO J. 17, 1526-1534.

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    Postdoctoral fellows

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