D. Ha

发表

Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product.

K. Tanaka, J. Seol, C. Chung, 1991, Biochemical and biophysical research communications.

The heat-shock protein ClpB in Escherichia coli is a protein-activated ATPase.

A. Goldberg, C. Chung, K. Woo, 1992, The Journal of biological chemistry.

Site-directed mutagenesis of the dual translational initiation sites of the clpB gene of Escherichia coli and characterization of its gene products.

K. Tanaka, J. Seol, C. Chung, 1993, The Journal of biological chemistry.

Hydrolysis of the IciA protein, an inhibitor of DNA replication initiation, by protease Do in Escherichia coli

S. Suh, J. Seol, C. Chung, 1993, FEBS letters.

Protease Ti from Escherichia coli requires ATP hydrolysis for protein breakdown but not for hydrolysis of small peptides.

A. Goldberg, C. Chung, K. Woo, 1989, The Journal of biological chemistry.

Multiple Ubiquitin C-terminal Hydrolases from Chick Skeletal Muscle (*)

K. Tanaka, C. Chung, S. K. Woo, 1995, The Journal of Biological Chemistry.

The 65-kDa protein derived from the internal translational initiation site of the clpA gene inhibits the ATP-dependent protease Ti in Escherichia coli.

J. Seol, C. Chung, M. Kang, 1994, The Journal of biological chemistry.

The 65‐kDa protein derived from the internal translational start site of the clpA gene blocks autodegradation of ClpA by the ATP‐dependent protease Ti in Escherichia coli

J. Seol, C. Chung, S. J. Yoo, 1995, FEBS letters.

Processing of Ada protein by two serine endoproteases Do and So from Escherichia coli

C. Chung, B. Hwang, C. S. Lee, 1990, FEBS letters.

Preferential degradation of the KMnO4-oxidized or N-ethylmaleimide-modified form of sarcoplasmic reticulum ATPase by calpain from chick skeletal muscle.

S. Chung, J. S. Lee, D. Ha, 1990, Biochimica et biophysica acta.

Purification and characterization of a poly-L-lysine-activated serine endoprotease from Lumbricus rubellus.

C. S. Chang, C. Chung, K. Woo, 1994, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.

Developmental regulation of proteolytic activities and subunit pattern of 20 S proteasome in chick embryonic muscle.

K. Tanaka, C. Chung, S. S. Kang, 1991, The Journal of biological chemistry.

Molecular cloning of complementary DNAs encoding two cationic peroxidases from cultivated peanut cells.

R. Esnault, C. Bréda, D. Buffard, 1990, Proceedings of the National Academy of Sciences of the United States of America.

Involvement of K(Ca) channels and stretch-activated channels in calcium influx, triggering membrane fusion of chick embryonic myoblasts.

M. Kang, D. Ha, J. Y. Park, 1996, Developmental biology.

Okadaic acid blocks membrane fusion of chick embryonic myoblasts in culture.

H. S. Kim, C. Chung, M. Kang, 1991, Biochemical and biophysical research communications.

Ubiquitin C-terminal hydrolases in chick skeletal muscle.

C. Chung, S. K. Woo, I. Park, 1996, Advances in experimental medicine and biology.

The P1 reactive site methionine residue of ecotin is not crucial for its specificity on target proteases. A potent inhibitor of pancreatic serine proteases from Escherichia coli.

S. Suh, J. Seol, C. Chung, 1994, The Journal of biological chemistry.

Involvement of transglutaminase in myofibril assembly of chick embryonic myoblasts in culture

K. Shin, S. Kang, M. Kang, 1995, The Journal of cell biology.

A candidate molecule for the matrix assembly receptor to the N-terminal 29-kDa fragment of fibronectin in chick myoblasts.

M. Kang, W. K. Song, D. Ha, 1994, The Journal of biological chemistry.

Cell‐penetrating inhibitors of calpain block both membrane fusion and filamin cleavage in chick embryonic myoblasts

C. Chung, J. Kambayashi, D. Ha, 1993, FEBS letters.

Nitric oxide as a messenger molecule for myoblast fusion.

K. H. Lee, C. Chung, W. Song, 1994, The Journal of biological chemistry.

Increase in the level of m-calpain correlates with the elevated cleavage of filamin during myogenic differentiation of embryonic muscle cells.

S. Chung, M. Kang, D. Ha, 1993, Biochimica et biophysica acta.

The biosynthesis of sarcoplasmic reticulum.

R. Boland, A. Martonosi, D. Ha, 1980, Federation proceedings.

Distinctive Roles of the Two ATP-binding Sites in ClpA, the ATPase Component of Protease Ti in Escherichia coli(*)

S. H. Baek, J. Seol, C. Chung, 1995, The Journal of Biological Chemistry.

Synthesis of the calcium transport ATPase of sarcoplasmic reticulum and other muscle proteins during development of muscles cells in vivo and in vitro.

R. Boland, A. Martonosi, D. Ha, 1979, Biochimica et biophysica acta.

5'-diphosphate-guanosine-3'-diphosphate (ppGpp) stimulates the degradation of certain proteins by ATP-dependent protease La from Escherichia coli

Sang Ki Park, Seung Ho Kim, K. Hahm, 1992 .

Molecular cloning of the Ecotin gene in Escherichia coli

S. Suh, J. Seol, A. Ichihara, 1991, FEBS letters.

Ca2+/calmodulin-dependent phosphorylation of the 100-kDa protein in chick embryonic muscle cells in culture.

H. S. Kim, M. Kang, D. Ha, 1992, Developmental biology.

Purothionin from wheat endosperm reversibly blocks myogenic differentiation of chick embryonic muscle cells in culture.

S. Suh, Y. Lee, D. Ha, 1989, Experimental cell research.

Sphingosine blocks both membrane fusion and calmodulin-dependent phosphorylation of the 100-kDa protein of chick embryonic myoblasts.

H. S. Kim, D. Ha, C. Chung, 1993, Experimental cell research.

Induction of protease La under stress and its effect on intracellular proteolysis in Escherichia coli.

C. Chung, K. Choi, C. S. Lee, 1991, Biochemistry international.

Requirement of ATP hydrolysis for assembly of ClpA/ClpP complex, the ATP-dependent protease Ti in Escherichia coli.

J. Seol, C. Chung, K. Woo, 1995, Biochemical and biophysical research communications.