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Curriculum Vitae Ming-Daw Tsai, Ph. D


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"Phospholipids Chiral at Phosphorus. 20. Stereochemical Mechanism of Reactions Catalyzed by Phosphatidylinositide-Specific Phospholipase C From Bacillus Cereus and Guinea Pig Uterus". G. H. Lin, C. F. Bennett, and M.-D. Tsai, Biochemistry 29, 2747-2757 (1990).




  1. "Mechanism of Adenylate Kinase. 6. Are the Essential Lysines Essential?" G. Tian, H. Yan, R.-T. Jiang, F. Kishi, A. Nakazawa, and M.-D. Tsai, Biochemistry 29, 4296-4304 (1990).




  1. "Phospholipids Chiral at Phosphorus. 22. Synthesis of Dioleoylthiophosphatidylcholine and Stereospecificity of Lecithin-Cholesterol Acyltransferase". T. Rosario-Jansen, H. Pownall, R.-T. Jiang, and M.-D. Tsai, Bioorg. Chem. 18, 179-184 (1990).




  1. "A Novel Expression Vector for High-Level Synthesis and Secretion of Foreign Proteins in E. coli: Overproduction of Bovine Pancreatic Phospholipase A2." T. Deng, J. P. Noel, and M.-D. Tsai, Gene 93, 229-234 (1990).




  1. "Phospholipase A2 Engineering. 3. Replacement of Lysine-56 by Neutral Residues Improves Catalytic Potency Significantly, Alters Substrate Specificity, and Clarifies the Mechanism of Interfacial Recognition". J. P. Noel, T. Deng, K. J. Kelly, and M.-D. Tsai, J. Am. Chem. Soc. 112, 3704-3706 (1990).




  1. "Mechanism of Adenylate Kinase. 7. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot be Replaced by Lysine". H. Yan, Z. Shi, and M.-D. Tsai, Biochemistry 29, 6385-6392 (1990).




  1. "Phospholipase A2 Engineering. 4. Can the Active-Site Aspartate-99 Function Alone?" C. M. Dupureur, T. Deng, J.-G. Kwak, J. Noel, and M.-D. Tsai, J. Am. Chem. Soc. 112, 7074-7076 (1990).




  1. "Phospholipids Chiral at Phosphorus. 23. Dramatic Effect of P-Chirality on the Deuterium NMR Properties of the Choline Head Group of Phospholipids in the Liquid Crystalline Phase". W. M. Loffredo, R.-T. Jiang, and M.-D. Tsai, Biochemistry 29, 10912-10918 (1990).




  1. "Mechanism of Adenylate Kinase. 8. Critical Evaluation of the X-Ray Model and Assignment of the AMP Site." H. Yan, T. Dahnke, B. Zhou, A. Nakazawa, and M.-D. Tsai, Biochemistry 29, 10956-10964 (1990).




  1. "Phospholipids Chiral at Phosphorus. 21. Phospholipase Stereospecificity at Phosphorus." K. Bruzik and M.-D. Tsai, Methods Enzymol. 197, 258-269 (1991). (Review)




  1. "Phospholipids Chiral at Phosphorus. 24. Phosphorothioate Analogs of Phosphatidylinositol and Inositol 1,2-Cyclic Phosphate: Applications to the Mechanism of Phospholipase C." K. Bruzik, G. Lin, and M.-D. Tsai, ACS Symp. Series 463, 172-185 (1991). (Review)




  1. "Mechanism of Adenylate Kinase. 9. Demonstration of Functional Relationship Between Aspartate 93 and Mg2+ by Site-Directed Mutagenesis and Proton, 31P, and 25Mg NMR." H. Yan and M.-D. Tsai, Biochemistry 30, 5539-5546 (1991).




  1. "Mechanism of Adenylate Kinase. 10. Reversing Phosphorus Stereospecificity by Site-Directed Mutagenesis". R.-T. Jiang, T. Dahnke, and M.-D. Tsai, J. Am. Chem. Soc. 113, 5485-5486 (1991).




  1. "Mechanism of Adenylate Kinase. 11. Site-Directed Mutagenesis Versus X-Ray and NMR." M.-D. Tsai and H. Yan, Biochemistry 30, 6806-6818 (1991). [This is a Perspectives in Biochemistry article.]




  1. "Phospholipase A2 Engineering. 5. X-Ray Structural and Functional Evidence for the Interaction of Lysine-56 with Substrates." J. P. Noel, C. A. Bingman, T. Deng, C. M. Dupureur, K. J. Hamilton, R.-T. Jiang, J.-G. Kwak, C. Sekharudu, M. Sundaralingam, and M.-D. Tsai, Biochemistry 30, 11801-11811 (1991).




  1. "Mechanism of Adenylate Kinase. 12. Prediction and Demonstration of Enhancement of Phosphorus Stereospecificity by Site-Directed Mutagenesis". T. Dahnke, R.-T. Jiang, and M.-D. Tsai, J. Am. Chem. Soc. 113, 9388-9389 (1991).




  1. "Practical Synthesis of Enantiomerically Pure myo-Inositol Derivatives." K. S. Bruzik, J. Myers, and M.-D. Tsai, Tetrahedron Lett., 1009-1012 (1992).




  1. "Phospholipase A2 Engineering. 6. Single Amino Acid Substitutions of Active Site Residues Convert the Rigid Enzyme to Highly Flexible Conformational States." C. M. Dupureur, Y. Li, and M.-D. Tsai, J. Am. Chem. Soc. 114, 2748-2749 (1992).




  1. "Phospholipids Chiral at Phosphorus. 25. Stereochemical Mechanism for the Formation of Inositol 1-Phosphate Catalyzed by Phosphatidylinositide-Specific Phospholipase C." K. S. Bruzik, A. M. Morocho, D.-Y. Jhon, S. G. Rhee, and M.-D. Tsai, Biochemistry 31, 5183-5193 (1992).




  1. "Mechanism of Adenylate Kinase. 13. Structural and Functional Roles of The Conserved Arginine-97 and Arginine-132." T. Dahnke, Z. Shi, H. Yan, R.-T. Jiang, and M.-D. Tsai, Biochemistry 31, 6318-6328 (1992).




  1. "Phospholipase A2 Engineering. 7. Structural and Functional Roles of Highly Conserved Active Site Residues Tyrosine-52 and Tyrosine-73." C. M. Dupureur, B.-Z. Yu, M. Jain, J. P. Noel, T. Deng, Y. Li, I.-J. Byeon, and M.-D. Tsai, Biochemistry 31, 6402-6413 (1992).




  1. "Efficient and Systematic Syntheses of Enantiomerically Pure and Regiospecifically Protected Myo-Inositols." K. S. Bruzik and M.-D. Tsai, J. Am. Chem. Soc. 114, 6361-6374 (1992).




  1. "Interfacial Catalysis by Phospholipase A2: The Rate-Limiting Step for Enzymatic Turnover". M. K. Jain, B.-Z. Yu, J. Rogers, M. H. Gelb, M.-D. Tsai, E. K. Hendrickson, and H. S. Hendrickson, Biochemistry 31, 7841-7847 (1992).




  1. "Phospholipase A2 Engineering. 9. The Structural and Functional Roles of Aromaticity and Hydrophobicity in the Conserved Phenylalanine-22 and Phenylalanine-106 Aromatic Sandwich." C. M. Dupureur, B.-Z. Yu, J. A. Mamone, M. K. Jain, and M.-D. Tsai, Biochemistry 31, 10576-10583 (1992).




  1. "Crystal Structure of the Y52F,Y73F double mutant of phospholipase A2: increased hydrophobic interactions of the phenyl groups compensate for the disrupted hydrogen bonds of the tyrosines. " C. Sekharudu, B. Ramakrishnan, B. Huang, R.-T. Jiang, C. M. Dupureur, M.-D. Tsai, and M. Sundaralingam, Protein Science 1, 1585-1594 (1992).




  1. "Modification of a Bruker AM-600 Spectrometer for Double and Triple Resonance Three Dimensional and Four Dimensional Experiments Illustrated with Chicken Adenylate Kinase Resonance Assignments." E. S. Mooberry, A. S. Edison, F. Abildgaard, J. L. Markley, I.-J. L. Byeon, and M.-D. Tsai, Proceedings of the International Symposium on Spectroscopy and Structure of Molecules and Nuclei, N. R. Johnson, W. N. Shelton, and M. El-Sayed, Eds., World Scientific, pp. 375-380 (1992). (Review)




  1. "Mechanism of Adenylate Kinase. 14. What Can be Learned from a Mutant Enzyme with Minor Perturbation in Kinetic Parameters?" Z.-T. Shi, I.-J. L. Byeon, R.-T. Jiang, ande M.-D. Tsai, Biochemistry 32, 6450-6458 (1993).




  1. "Phospholipase A2 Engineering. 10. The Aspartate...Histidine Catalytic Diad Also Plays an Important Structural Role." Y. Li and M.-D. Tsai, J. Am. Chem. Soc. 115, 8523-8526 (1993).




  1. "Mechanism of Adenylate Kinase. 15. 1H, 13C, and 15N NMR Assignments, Secondary Structures, and Substrate Binding Sites." I.-J. L. Byeon, H. Yan, A. S. Edison, E. S. Mooberry, F. Abildgaard, J. L. Markley, and M.-D. Tsai, Biochemistry 32, 12508-12521 (1993).




  1. "Mechanism of Adenylate Kinase. 16. The Conserved Aspartates 140 and 141 Are Important for Transition State Stabilization Instead of Substrate-Induced Conformational Changes." T. Dahnke and M.-D. Tsai, J. Biol. Chem. 269, 8075-8081 (1994).




  1. "Toward the Mechanism of Phospohatidylinositide-Specific Phospholipase C." K. S. Bruzik and M.-D. Tsai, Bioorg. & Med. Chem. 2, 49-72 (1994).




  1. "Are D- and L-chiro-Phosphoinositides Substrates of Phosphatidylinositol-Specific Phospholipase C?" K. S. Bruzik, A. A. Hakeem, and M.-D. Tsai, Biochemistry 33, 8367-8374 (1994).




  1. "A Small, High-Copy-Number Vector Suitable for Both in vitro and in vivo Gene Expressions." B. Huang, Z. Shi, and M.-D. Tsai, Gene 151, 143-145 (1994).




  1. "Structure and Function of the Catalytic Site Mutant Asp 99 Asn of Phospholipase A2: Absence of the Conserved Structural Water." A. Kumar, C. Sekharudu, B. Ramakrishnan, C. M. Dupureur, H. Zhu, M.-D. Tsai, and M. Sundaralingam, Protein Science 3, 2082-2088 (1994).




  1. "Phospholipase A2 Engineering. 12. Structural and Functional Roles of the Highly Conserved Active Site Residue Aspartate-49." Y. Li, B.-Z. Yu, H. Zhu, M. K. Jain, and M.-D. Tsai, Biochemistry 33, 14714-14722 (1994).




  1. "Phospholipase A2 Engineering. 13. Conversion of Bovine Pancreatic Phospholipase A2 at a Single Site into a Competitor of Neurotoxic Phospholipase A2 by Site-Directed Mutagenesi." M.-C. Tzeng, C.-H. Yen, M.-J. Hseu, C. M. Dupureur, and M.-D. Tsai, J. Biol. Chem. 270, 2120-2123 (1995).




  1. "Mechanism of Adenylate Kinase. 17. Manipulating Phosphorus Stereospecificity of Adenylate Kinase by Site-Directed Mutagenesis." M.-D. Tsai, R.-T. Jiang, T. Dahnke, and Z. Shi, Methods Enzymol. 249, 425-443 (1995). (Review)




  1. "Mechanism of Adenylate Kinase. 18. The “Essential Lysine” Helps To Orient the Phosphates and the Active Site Residues to Proper Conformations." I.-J. L. Byeon, Z. Shi, and M.-D. Tsai, Biochemistry 34, 3172-3182 (1995).




  1. "Phospholipase A2 Engineering. 14. Probing the Structural and Functional Roles of N-Terminal Residues with Site-Directed Mutagenesis, X-ray, and NMR." X. Liu, H. Zhu, B. Huang, J. Rogers, B.-Z. Yu, A. Kumar, M. K. Jain, M. Sundaralingam, and M.-D. Tsai, Biochemistry 34, 7322-7334 (1995).




  1. "Immunogenicity and Conformational Properties of an N-linked Glycosylated Peptide Epitope of Human T-Lymphotropic Virus Type 1 (HTLV-1)." S. F. Conrad, I.-J. L Byeon, A. M. DiGeorge, M. D. Lairmore, M.-D. Tsai, and P. T. P. Kaumaya, Biomedical Peptides, Proteins, & Nucleic Acids 1, 83-92 (1995). (Review)




  1. "Binding Proteins on Synaptic Membranes for Crotoxin and Taipoxin, 2 Phospholipases A2 with Neurotoxicity." M. C. Tzeng, C. H. Yen, M. J. Hseu, C. C. Tseng, M.-D. Tsai, and C. M. Dupureur, Toxicon 33, 451-457 (1995).




  1. "Phospholipase A2 Engineering. 15. The Roles of Disulfide Bonds in Structure, Conformational Stability, and Catalytic Function.'' H. Zhu, C. M. Dupureur, X. Zhang, and M.-D. Tsai, Biochemistry 34, 15307-15314 (1995).




  1. "Design, Synthesis and Biochemical Applications of Analogs of Phosphatidylinositol", N. K. Bhamare, Y. Wang, M.-D. Tsai, K. S. Bruzik, Phosphorus, Sulfur, and Silicon 109-110, 317-320 (1996).




  1. "Structure-Function Relationship of Adenylate Kinase. 19. Glutamine-101 in AMP Specificity." S. Beichner, I.-J. L. Byeon, and M.-D. Tsai, PEPTIDES: Chemistry, Structure, and Biology, Kaumaya, P. T. P. and Hodges, R. S. (Eds.), Mayflower Scientific Ltd. (1996), Chapter 303, pp. 721-723. (Review)




  1. "DNA Polymerase : 1. Pre-Steady-State Kinetic Analysis and the Roles of Arginine-283 in Catalysis and Fidelity." B. G. Werneburg, J. Ahn, X. Zhong, R. J. Hondal, V. Kraynov, and M.-D. Tsai, Biochemistry 35, 7041-7050 (1996).




  1. "Mechanism of Adenylate Kinase. 20. Probing the Importance of the Aromaticity in Tyrosine-95 and the Ring Size in Proline-17 with Unnatural Amino Acids." Z. Zhao, X. Liu, Z. Shi, L. Danley, B. Huang, R.-T. Jiang, and M.-D. Tsai, J. Am. Chem. Soc. 118, 3535-3536 (1996).




  1. "Tumor Suppressor p16INK4A: 1. Structural Characterization of Wild-type and Mutant Proteins by NMR and Circular Dichroism." A. Tevelev, I.-J. L. Byeon, T. Selby, K. Ericson, H.-J. Kim, V. Kraynov, and M.-D. Tsai, Biochemistry 35, 9475-9487 (1996).




  1. "Splase: A New Class IIs Zinc Finger Restriction Enzyme with Specificity for Sp1 Binding Sites." B. Huang, C. J. Schaeffer, and M.-D. Tsai, J. Protein Chem. 15, 481-489 (1996).




  1. "Synthesis of Inositol Phosphodiesters by Phospholipase C-Catalyzed Transesterification". K. S. Bruzik, Z. Guan, S. Riddle, and M.-D. Tsai, J. Am. Chem. Soc. 118, 7679-7688 (1996).




  1. "Phospholipase A2 Engineering. 16. Deletion of the C-Terminus Segment Changes Substrate Specificity and Uncouples Calcium and Substrate Binding at the Zwitterionic Interface." B. Huang, B.-Z. Yu, J. Rogers, K. Sekar, M. Sundaralingam, M.-D. Tsai, and M. K. Jain, Biochemistry 35, 12164-12174 (1996).




  1. "Binding Proteins on Synaptic Membranes for Certain Phospholipases A2 with Presynaptic Toxicity". M.-C. Tzeng, C.-H. Yen, and M.-D. Tsai, in "Natural Toxins II", pp. 271-278, B. R. Singh and A. T. Tu, Eds., Plenum Press, New York (1996). [Also cited as Adv. Exp. Med. Biol. 391, 271-8 (1996).] (Review)




  1. "Splase: The Design of a New Restriction Enzyme with Specificity for Sp1 Binding Sites." B. Huang, C. J. Schaeffer, and M.-D. Tsai, in Perspectives on Protein Engineering 3 (Geisow, M. J., ed), BIODIGM, Nottingham (1996). (Review)




  1. "Effects of Glycosylation of a Peptide Epitope from HTLV-1 gp46 on Structure and Immunogenicity." S. F. Conrad, I.-J. L Byeon, A. M. DiGeorge, M. D. Lairmore, M.-D. Tsai, and P. T. P. Kaumaya, Pept.: Chem., Struct. Biol., Proc. Am. Pept. Symp., 14th, 448-9 (1996). (Review)




  1. "DNA Polymerase : 2. Structure-Fidelity Relationship from Pre-Steady-State Kinetic Analysis of All Possible Correct and Incorrect Base Pairs for Wild Type and R283A Mutant." J. Ahn, B. G. Werneburg, and M.-D. Tsai, Biochemistry 36, 1100-1107 (1997).




  1. "DNA Polymerase : 3. Analysis of the contribution of Tyrosine-271 and Asparagine-279 to Substrate Specificity and Fidelity of DNA Replication by Pre-steady-state Kinetics." V. S. Kraynov, B. G. Werneburg, X. Zhong, H. Lee, J. Ahn, and M.-D. Tsai, Biochem. J. 323, 103-111 (1997).




  1. "Phospholipase A2 Engineering. 17. Structural and Functional Roles of the Highly Conserved Active Site Residue Aspartate-99." K. Sekar, B.-Z. Yu, J. Rogers, J. Lutton, X. Liu, X. Chen, M.-D. Tsai, M. Jain, & M. Sundaralingam, Biochemistry 36, 3104-3114 (1997).




  1. "Synthesis of Enantiomerically Pure Phosphorothiolate Assay Substrate for Phosphatidylinositol-Specific Phospholipase C." Cornelia Mihai, Jan Mataka, Suzette Riddle, Ming-Daw Tsai, and Karol S. Bruzik, Bioorg. Med. Lett. 7, 1235-1238 (1997).




  1. "PI-Specific Phospholipase C. 1. Kinetic and Stereochemical Evidence for an Interaction between Arginine-69 and the Phosphate Group of Phosphatidylinositol." Robert J. Hondal, Suzette R. Riddle, Alexander V. Kravchuk, Zhong Zhao, Karol S. Bruzik, and Ming-Daw Tsai, Biochemistry 36, 6633-6642 (1997).




  1. "Natural Product Chemistry: From Plants to Human." Ming-Daw Tsai, J. Chin. Chem. Soc. 44, 183-186 (1997). (Review)




  1. "Use of Unnatural Amino Acids to Probe the Importance of the Aromaticity in Tyrosine-95 and the Ring Size in Proline-17 in Adenylate Kinase." Z. Zhao, X. Liu, Z. Shi, B. Huang, R.-T. Jiang, and M.-D. Tsai, Youji Huaxue 17, 20-23 (1997).




  1. "Mechanism of PI-Specific Phospholipase C. 2. Reversal of a Thio Effect by Site-Directed Mutagenesis." Robert J. Hondal, Zhong Zhao, Karol S. Bruzik, and Ming-Daw Tsai, J. Am. Chem. Soc. 119, 5477-5478 (1997).




  1. "DNA Polymerase : 4. Multiple Conformational Changes in the Mechanism of Catalysis". Xuejun Zhong, Smita S. Patel, Brian G. Werneburg, and Ming-Daw Tsai, Biochemistry 36, 11891-11900 (1997).




  1. "Mechanism of PI-Specific Phospholipase C. 3. Elucidation of the Catalytic Mechanism and Comparison with Ribonuclease A." Robert J. Hondal, Zhong Zhao, Suzette R. Riddle, Alexander V. Kravchuk, Hua Liao, Karol S. Bruzik, and Ming-Daw Tsai, J. Am. Chem. Soc. 119, 9933-9934 (1997).




  1. "Crystal Structure of the Complex of Bovine Pancreatic Phospholipase A2 with a Transition State Analogue." K. Sekar, A. Kumar, X. Liu, M.-D. Tsai, M. Gelb, and M. Sundaralingam, Acta Crystallogr. D. Biol. Crystallogr. 54, 334-341 (1998).




  1. "1.72 A Resolution Refinement of the Trigonal Form of Bovine Pancreatic PhospholipaseA2." K. Sekar, A. Kumar, X. Liu, M.-D. Tsai, M. Gelb, and M. Sundaralingam, Acta Crystallogr. D. Biol. Crystallogr. 54, 342-346 (1998).




  1. "DNA Polymerase : 6. Effects of Gapped DNA Substrates on dNTP Specificity, Fidelity, Processivity, and Conformational Changes." Jinwoo Ahn, Vadim Kraynov, Xuejun Zhong, Brian G. Werneburg, and Ming-Daw Tsai, Biochem. J. 331, 79-87 (1998).




  1. "DNA Polymerase . 5. Dissecting the Functional Roles of the Two Metal Ions with Cr(III)dTTP" by Xuejun Zhong, Smita S. Patel, and Ming-Daw Tsai, J. Am. Chem. Soc. 120, 235-236 (1998).




  1. "Tumor Suppressor p16INK4A: Determination of Solution Structure and Analyses of Its Interaction with Cyclin-Dependent Kinase 4". In-Ja L. Byeon, Junan Li, Karen Ericson, Thomas L. Selby, Anton Tevelev, Hee-Jung Kim, Paul O'Maille, and Ming-Daw Tsai, Molecular Cell 1, 421-431 (1998).




  1. "Mechanism of PI-Specific Phospholipase C. 4. A Unified View of the Mechanism of Catalysis " Robert J. Hondal, Zhong Zhao, Alexander V. Kravchuk, Hua Liao, Suzette R. Riddle, Xiangjun Yue, Karol S. Bruzik, and Ming-Daw Tsai, Biochemistry 37, 4568-4580 (1998).




  1. "Mechanism of PI-Specific Phospholipase C. 5. The Mechanism of PI-PLC Revealed by Protein Engineering and Thio-PI Analogs." Robert J. Hondal, Zhong Zhao, Alexander V. Kravchuk, Hua Liao, Suzette R. Riddle, Karol S. Bruzik, and Ming-Daw Tsai, in Phosphoinositides: Chemistry, Biochemistry and Biomedical Applications, K. S. Bruzik, Ed. ACS Symp. Ser. vol. 718, pp. 109-120 (1998). (Review)




  1. "Cationic Residues 53 and 56 Control the Anion-Induced Interfacial k*cat-Activation of Pancreatic Phospholipase A2." Joseph Rogers, Bao-Zhu Yu, Ming-Daw Tsai, Otto Berg, and Mahendra K. Jain, Biochemistry 37, 9549-9556 (1998).




  1. “Identification of a Novel Catalytic Triad with Dual Functions in Enzymatic Cleavage of the P-O Bond”. Robert J. Kubiak, Robert J. Hondal, Xiangjun Yue, Ming-Daw Tsai, and Karol S. Bruzik, J. Am. Chem. Soc. 121, 488-489 (1999).




  1. “Structures of the Catalytic Site Mutants D99A and H48Q and the Calcium Loop Mutant D49E of Phospholipase A2”. K. Sekar, R. Biswas, Y. Li, M.-D. Tsai, and M. Sundaralingam, Acta Crystallogr. D55, 443-447 (1999).




  1. “Structural Analysis of Phospholipase A2 from Functional Perspective. 1. Functionally Relevant Solution Structure and Roles of the Hydrogen-Bonding Network”. Chunhua Yuan, In-Ja L. Byeon, Yishan Li, and Ming-Daw Tsai, Biochemistry 38, 2909-2918 (1999).




  1. “Structural Analysis of Phospholipase A2 from Functional Perspective. 2. Characterization of a Molten Globule-like State Induced by Site-Specific Mutagenesis”. Chunhua Yuan, In-Ja L. Byeon, Ming Jye Poi, and Ming-Daw Tsai, Biochemistry 38, 2919-2929 (1999).




  1. “Tumor Suppressor INK4: 3. Determination of the Solution Structure of p18INK4C and Demonstration of the Functional Significance of Loops in p18INK4C and p16INK4A.” Junan Li, In-Ja L. Byeon, Karen Ericson, Ming Jye Poi, Paul O’Maille, Thomas Selby, and Ming-Daw Tsai, Biochemistry 38, 2930-2940 (1999).




  1. “Contributions of Residues of Pancreatic Phospholipase A2 to Interfacial Binding, Catalysis and Activation”. Bao-Zhu Yu, Joseph Rogers, Ming-Daw Tsai, Charles Pidgeon, and Mahendra K. Jain, Biochemistry 38, 4875-4884 (1999).




  1. “Nucleoside Monophosphate Kinases: Structure, Mechanism, and Substrate Specificity.” Honggao Yan and Ming-Daw Tsai, Adv. Enzymol. And Related Area of Mol. Biol. 73: Mechanism of Enzyme Action, D. L. Purich, Ed., pp. 103-134 (1999). (Review)




  1. “Pancreatic Phospholipase A2: New Views on Old Issues”. Chunhua Yuan and Ming-Daw Tsai, BBALIP – Special Thematic Issue on “Lipids in the Center”, BBA-Mol. Cell. Biol. L 1441, 215-222 (1999).




  1. “Tumor Suppressor INK4: Comparisons of Conformational Properties between p16INK4A and p18INK4C.” Chunhua Yuan, Junan Li, Thomas L. Selby, In-Ja L. Byeon, and Ming-Daw Tsai, J. Mol. Biol. 294, 201-211 (1999).




  1. “Structure and Function of A New Phosphopeptide-Binding Domain Containing the FHA2 of Rad53” by Hua Liao, In-Ja L. Byeon, and Ming-Daw Tsai, J. Mol. Biol. 294, 1041-1049 (1999).




  1. “Tumor Suppressor INK4: Quantitative Structure-Function Analyses of p18INK4C as an Inhibitor of Cyclin-Dependent Kinase 4.” Junan Li, Ming Jye Poi, Dongyan Qin, Thomas L. Selby, In-Ja Byeon, and Ming-Daw Tsai, Biochemistry 39, 649-657 (2000).




  1. “Structure-Function Relationship of the INK4 Family of Tumor Suppressors”. Junan Li, In-Jia L. Byeon, Ming Jye Poi, Karen Ericson, Thomas Selby, Paul O’Maille, Dongyan Qin, and Ming-Daw Tsai, in DNA Alterations in Cancer: Genetic and Epigenetic Changes, Melanie Ehrlich, Ed., BioTechniques Books, Eaton Publishing, pp. 71-84 (2000). (Review)




  1. “Tumor Suppressor INK4: Refinement of p16INK4A Structure and Determination of p15INK4B Structure by Comparative Modeling and NMR Data”. Chunhua Yuan, Thomas L. Selby, Junan Li, In-Ja Byeon, and Ming-Daw Tsai, Protein Science 9, 1120-1128 (2000).




  1. “Kinetic Isotope Effects and Stereochemical Studies on a Ribonuclease Model: Hydrolysis Reactions of Uridine-3’-Nitrophenyl Phosphate”. Alvan C. Hengge, Karol S. Bruzik, Aleksandra E. Tobin, W. W. Cleland, and Ming-Daw Tsai, Bioorg. Chem. 28, 119-133 (2000).




  1. “Structural Basis of the Anionic Interface Preference and kcat Activation of Pancreatic Phospholipase A2”. Bao-Zhu Yu, Ming Jye Poi, U.A. Ramagopal, Rinku Jain, S. Ramakumar, Otto Berg, Ming-Daw Tsai, K. Sekar, and Mahendra Kumar Jain, Biochemistry 39, 12312-12323 (2000).




  1. “Structure and Specificity of the Interaction between the FHA2 Domain of Rad53 and Phosphotyrosyl Peptides”. Peng Wang, In-Ja L. Byeon, Hua Liao, Kirk Beebe, Suganya Yongkiettrakul, Dehua Pei, and Ming-Daw Tsai, J. Mol. Biol. 302, 927-940 (2000).




  1. “Structure of the FHA1 Domain of Yeast Rad53 and Identification of Binding Sites for both FHA1 and Its Target Protein Rad9”. Hua Liao, Chunhua Yuan, Mei-I Su, Suganya Yongkiettrakul, Dongyan Qin, Hongyuan Li, In-Ja L. Byeon, Dehua Pei, and Ming-Daw Tsai, J. Mol. Biol. 304, 941-951 (2000).




  1. “DNA Polymerase : Contributions of Template-Positioning and dNTP Triphosphate-Binding Residues to Catalysis and Fidelity.” Vadim S. Kraynov, Alexander K. Showalter, Jia Liu, Xuejun Zhong and Ming-Daw Tsai, Biochemistry 39, 16008-16015 (2000).




  1. “Somatic INK4a-ARF Locus Mutations: A Significant Mechanism of Gene Inactivation in Squamous Cell Carcinomas of the Head and Neck.” Ming J. Poi, Thomas Yen, Junan Li, Huijuan Song, Jas C. Lang, Dave E. Schuller, Dennis K. Pearl, Bruce C. Casto, Ming-Daw Tsai, and Christopher M. Weghorst, Molecular Carcinogenesis 30, 26-36 (2001).




  1. “A DNA Polymerase with Specificity for Five Base Pairs”. Alexander K. Showalter and Ming-Daw Tsai, J. Am. Chem. Soc. 123, 1776-1777 (2001). (This paper has been featured in Chemical & Engineering News, March 12, 2001, p.60-61.)




  1. “Insight into the Catalytic Mechanism of DNA Polymerase : Structures of Intermediate Complexes”. Joseph W. Arndt, Weimin Gong, Xuejun Zhong, Alexander K. Showalter, Jia Liu, Christopher A. Dunlap, Zheng Lin, Chad Paxson, Ming-Daw Tsai, and Michael K. Chan, Biochemistry 40, 5368 -5375 (2001).




  1. “Involvement of Arg…Asp…His Catalytic Triad in Enzymatic Cleavage of the Phosphodiester Bond”. Robert J. Kubiak, Xiangjun Yue, Robert J. Hondal, Cornelia Mihai, Ming-Daw Tsai, and Karol S. Bruzik, Biochemistry 40, 5422-5432 (2001).




  1. “Mechanism of PI-PLC: Origin of Unusually High Nonbridging Thio Effects”. Alexander V. Kravchuk, Li Zhao, Robert J. Kubiak, Karol S. Bruzik, and Ming-Daw Tsai, Biochemistry 40, 5433-5439 (2001).




  1. “DNA Polymerase : Pre-steady-State Kinetic Analyses of dATPS Stereoselectivity and Alteration of the Stereoselectivity by Varying Metal Ions and by Site-Directed Mutagenesis.” Jia Liu and Ming-Daw Tsai, Biochemistry 40, 9014-9022 (2001).




  1. “Interfacial Enzymology: The Phospholipase A2-Paradigm”. Otto G. Berg, Michael Gelb, Ming-Daw Tsai, and Mahendra K. Jain, Chemical Reviews 101, 2613-2653 (2001). (Review)




  1. “Solution Structure of a Viral DNA Polymerase X and Evidence for a Mutagenic Function” by Alexander K. Showalter, In-Ja L. Byeon, Mei-I Su, and Ming-Daw Tsai, Nature Structural Biology 8, 942-946 (2001). (This paper has been featured in News & Views of NSB.)




  1. “Solution Structures of Two FHA1-Phosphothreonine Peptide Complexes Provide Insight into the Structural Basis of the Ligand Specificity of FHA1 from Yeast Rad53.” Yuan, C., Yongkiettrakul, S., Byeon, I.-J. L., Zhou, S., & Tsai, M.-D., J. Mol. Biol. 314, 563-575 (2001).




  1. “Solution Structure of the Yeast Rad53 FHA2 Complexed with a Phosphothreonine Peptide pTXXL: Comparison with the Structures of FHA2-pYXL and FHA1-pTXXD Complexes.” Byeon, I. -J. L., Yongkiettrakul, S., & Tsai, M.-D. J. Mol. Biol. 314, 577-588 (2001).




  1. “Novel Insights into the INK4-CDK4/6-Rb Pathway: Counter Action of Gankyrin Against INK4 Proteins Regulates the CDK4-Mediated Phosphorylation of Rb”. Junan Li and Ming-Daw Tsai, Biochemistry 41, 3977-3983 (2002).




  1. “FHA: A Signal Transduction Domain with Diverse Specificity and Function”. Ming-Daw Tsai, Structure 10, 887-888 (2002). (Review)




  1. “Structure-based Combinatorial Protein Engineering (Scope)” by Paul E. O’Maille, Marina Bakhtina, and Ming-Daw Tsai, J. Mol. Biol. 321, 677-691 (2002).




  1. “A Reexamination of the Nucleotide Incorporation Fidelity of DNA Polymerases”. Alexander K. Showalter and Ming-Daw Tsai, Biochemistry 41, 10571-10576 (2002). [New Concepts in Biochemistry] (This work has been featured in Chemical & Engineering News, May 13, 2002, p.44.)




  1. “Use of 2-Aminopurine and Tryptophan Fluorescence as Probe in Kinetic Analyses of DNA Polymerase ”. Christopher A. Dunlap and Ming-Daw Tsai, Biochemistry 41, 11226-11235 (2002).




  1. “Observation of Additional Calcium Ion in the Crystal Structure of the Triple Mutant K56,120,121M of Bovine Pancreatic Phospholipase A2”. V. Rajakannan, M. Yogavel, Ming-Jye Poi, A. Jeya Prakash, J. Jeyakanthan, D. Velmurugan, Ming-Daw Tsai and K. Sekar, J. Mol. Biol. 324, 755-762 (2002).




  1. “A Novel Calcium-Dependent Bacterial Phosphatidylinositol-Specific Phospholipase C Displaying Unprecedented Magnitudes of Thio Effect, Inverse Thio Effect, and Stereoselectivity”. Li Zhao, Yinghui Liu, Karol S. Bruzik, and Ming-Daw Tsai, J. Am. Chem. Soc. 125, 22-23 (2003).




  1. “Engineering a Catalytic Metal Binding Site into a Calcium-independent Phosphatidylinositol-Specific Phospholipase C Leads to Enhanced Stereoselectivity”. Alexander V. Kravchuk, Li Zhao, Karol S. Bruzik, and Ming-Daw Tsai, Biochemistry 42, 2422-2430 (2003).




  1. “Application of BrØnsted-type LFER in the Study of the Phospholipase C Mechanism”. Cornelia Mihai, Alexander V. Kravchuk, Ming-Daw Tsai and Karol S. Bruzik, J. Am. Chem. Soc. 115, 3236-3243 (2003).




  1. “Expression and Characterization of Syrian Golden Hamster p16, a Homologue of Human Tumor Suppressor p16INK4A.” Junan Li, Dongyan Qin, Thomas J. Knobloch, Ming-Daw Tsai, Christopher M. Weghorst, W. Scott Melvin, and Peter Muscarella, Biochem. Biophys. Res. Commun. 304, 241-247 (2003).




  1. “Interaction of Monodisperse Anionic Amphiphiles with the i-Face of Secreted Phospholipase A2”. Bao-Zhu Yu, Rafael Apitz-Castro, Ming-Daw Tsai, and Mahendra K. Jain, Biochemistry 42, 6293-6301 (2003).




  1. “A Low-Barrier Hydrogen Bond Between Histidine of Secreted Phospholipase A2 and a Transition State Analog Inhibitor”. Ming Jye Poi, John W. Tomaszewski, Chunhua Yuan, Christopher A. Dunlap, Niels H. Andersen, Michael H. Gelb, and Ming-Daw Tsai, J. Mol. Biol. 329, 997-1009 (2003).




  1. “Direct Binding of the N-terminus of HTLV-1 Tax Oncoprotein to Cyclin-dependent Kinase 4 Is a Dominant Path to Stimulate the Kinase Activity”. Junan Li, Hongyuan Li, and Ming-Daw Tsai, Biochemistry 42, 6921-6928 (2003).




  1. “Biocatalysis and Biotransformation Enzymology in the Genomic Era – Editorial Overview.” Tadhg P. Begley and Ming-Daw Tsai, Curr. Opin. Chem. Biol. 7, 228-229 (2003). (Review)




  1. “Diverse but Overlapping Functions of the Two Forkhead-associated (FHA) Domains in Rad53 Checkpoint Kinase Activation.” Brietta L. Pike, Suganya Yongkiettrakul, Ming-Daw Tsai, and Jorg Heierhorst, J. Biol. Chem. 278, 30421-30424 (2003).



  1. “Crystal Structures of the Free and Anisic Acid Bound Triple Mutant of Phospholipase A2”. K. Sekar, S. Vaijayanthi Mala, M. Yogavel, D. Velmurugan, Ming-Jye Poi, B. S. Vishwanath, T. V. Gowda, A. Arokia Jeyaprakash and M.-D. Tsai, J. Mol. Biol. 333, 367-376 (2003).




  1. “Identification of Potential Binding Sites for the FHA Domain of Human Chk2 by in vitro Binding Studies.” Dongyan Qin, Hyun Lee, Chunhua Yuan, Yong Ju, and Ming-Daw Tsai, Biochem. Biophys. Res. Commun. 311, 803-808 (2003).




  1. “An NF-B-Specific Inhibitor, IB, Binds to and Inhibits Cyclin-Dependent Kinase 4”. Junan Li, Sang Hoon Joo, and Ming-Daw Tsai, Biochemistry 42, 13476-13483 (2003).




  1. “Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions.” Hongyuan Li, In-Ja L. Byeon, Yong Ju, and Ming-Daw Tsai, J. Mol. Biol. 335, 371-381 (2004).




  1. “Frequent p16INK4A/CDKN2A Alterations in Chemically Induced Syrian Golden Hamster Pancreatic Tumors”. Junan Li, Christopher M. Weghorst, Masahiro Tsutsumi, Ming J. Poi, Thomas J. Knobloch, Bruce C. Casto, W. Scott Melvin, Ming-Daw Tsai, and Peter Muscarella, Carcinogenesis 25, 263-268 (2004).




  1. The Ligand Specificity of Yeast Rad53 FHA Domains at the +3 Position Is Determined by Nonconserved Residues” by Suganya Yongkiettrakul, In-Ja L. Byeon, and Ming-Daw Tsai, Biochemistry 43, 3862-3869 (2004).




  1. “Mdt1, a Novel Rad53 FHA1 Domain-Interacting Protein, Modulates DNA Damage Tolerance and G2/M Cell Cycle Progression in Saccharomyces cerevisiae”. Brietta L. Pike, Suganya Yongkiettrakul, Ming-Daw Tsai, and Jorg Heierhorst. Mol. Cell. Biol. 24, 2779-2788 (2004).




  1. “The Nuclear Protein p34SEI-1 Regulates the Kinase Activity of Cyclin-dependent Kinase 4 in a Concentration-dependent Manner.” Junan Li, W. Scott Melvin, Ming-Daw Tsai, and Peter Muscarella, Biochemistry 43, 4394-4399 (2004).




  1. “Gene Library Synthesis by Structure-based Combinatorial Protein Engineering (SCOPE).” Paul E. O’Maille, Ming-Daw Tsai, and Joseph P. Noel, Methods in Enzymology 388, 75-91 (2004). (Review)




  1. “The Catalytic Role of Aspartate in a Short Strong Hydrogen Bond of the Asp274His32 Catalytic Dyad in Phosphatidylinositol-specific Phospholipase C Can Be Substituted by a Chloride Ion.” Li Zhao, Hua Liao, and Ming-Daw Tsai, J. Biol. Chem. 279, 31995-32000 (2004).




  1. “Solution Structure of Human Oncogenic Protein Gankyrin Containing Seven Ankyrin Repeats and Analysis of Its Structure-function Relationship”. Chunhua Yuan, Junan Li, Anjali Mahajan, Ming Jye Poi, In-Ja L. Byeon, and Ming-Daw Tsai, Biochemistry 43, 12152-12161 (2004).




  1. “Enzyme Reaction Mechanisms: Stereochemistry.” Ming-Daw Tsai, Li Zhao, and Brandon Lamarche, Encyclopedia in Biological Chemistry 2, 45-50 (2004). (Review)




  1. “Atomic resolution (0.97Å) structure of the triple mutant (K53,56,121M) of bovine pancreatic phospholipase A2”. K. Sekar, V. Rajakannan, D. Gayathri, D. Velmurugan, M.-J. Poi, M. Dauter, Z. Dauter and M.-D. Tsai, Acta Cryst. F61, 3-7 (2005).




  1. “Unusual Four-bond Secondary H/D Isotope Effect Supports a Short-Strong Hydrogen Bond between Phospholipase A2 and a Transition State Analogue Inhibitor.” Chunhua Yuan, Shengjiang Tu, Michael H. Gelb, and Ming-Daw Tsai, Biochemistry 44, 4748-4754 (2005).




  1. “Use of Viscogens, dNTPS and Rhodium(III) as Probes in Stopped-Flow Experiments to Obtain New Evidence for the Mechanism of Catalysis by DNA Polymerase ”Marina Bakhtina, Soojin Lee, Yu Wang, Chris Dunlap, Brandon Lamarche, and Ming-Daw Tsai, Biochemistry 44, 5177-5187 (2005).




  1. “An Error-Prone Viral DNA Ligase.” Brandon Lamarche, Alex Showalter, and Ming-Daw Tsai, Biochemistry 44, 8408-17 (2005).




  1. “X-ray structure of the R69D phosphatidylinositol-specific phospholipase C enzyme: insight into the role of calcium and surrounding amino acids in active site geometry and catalysis.” D. Apiyo, Li Zhao, Ming-Daw Tsai, and Thomas L. Selby, Biochemistry 44, 9980-9989 (2005).




  1. “Dissection of CDK4-binding and Transactivation Activities of p34SEI-1 and Comparison between Functions of p34SEI-1 and p16INK4”. Junan Li, Peter Muscarella, Sang Hoon Joo, Thomas, J. Knobloch, W. Scott Melvin, Christopher, M. Weghorst, and Ming-Daw Tsai, Biochemistry 44, 13246-13256 (2005).




  1. “FHA Domain-Ligand Interactions: Importance of Integrating Chemical and Biological Approaches”. Anjali Mahajan, Chunhua Yuan, Brietta L. Pike, Jorg Heierhorst, Chi-Fon Chang, and Ming-Daw Tsai, J. Am. Chem. Soc. 127, 14572-14573 (2005).



  1. “Sequential Phosphorylation and Multisite Interactions Characterize Specific Target Recognition by the FHA Domain of Ki-67”, by In-Ja L. Byeon, Hongyuan Li, Haiyan Song, Angela M. Gronenborn, and Ming-Daw Tsai, Nature Structural and Molecular Biology 12, 987-993 (2005).




  1. “Atomic Resolution Structure of the Double Mutant (K53,56M) of Bovine Pancreatic Phospholipase A2”. K. Sekar, M. Yogavel, D. Velmurugan, R.Krishna, M.-J. Poi, Z. Dauter, M. Dauter and M.-D. Tsai, Acta Cryst. F62, 1-5 (2006).




  1. “Contributions of an Endonuclease IV Homologue to DNA Repair in the African Swine Fever Virus”. B. Lamarche and M.-D. Tsai, Biochemistry 45, 2790-2803 (2006).




  1. “Mechanistic Comparison of High-fidelity and Error-prone DNA Polymerases and Ligases Related to DNA Repair”. Alexander K. Showalter, Brandon Lamarche, Marina Bakhtina, Mei-I Su, Kuo-Hsiang Tang, and Ming-Daw Tsai, Chemical Reviews 106, 340-360 (2006). (Review)




  1. “Third Calcium Ion Found in an Inhibitor Bound Phospholipase A2”. K. Sekar, D. Gayathri, D. Velmurugan, J. Jeyakanthan, T. Yamane, M.-J. Poi, and M.-D. Tsai, Acta Cryst. D62, 392-397 (2006).




  1. “Suggestive Evidence for the Involvement of Second Calcium and Surface Loop in Interfacial Binding: Monoclinic and Trigonal Crystal Structures of A Quadruple Mutant of Phospholipase A2.” K. Sekar, M. Yogavel, D. Velmurugan, M.-J. Poi, Z. Dauter, and M.-D. Tsai, Acta Cryst. D62, 717-724 (2006).



  1. “Glycopeptide Biosynthesis: Dbv21/Orf2* from dbv/tcp Gene Clusters Are NAc-Glm Teicoplanin Pseudoaglycone Deacetylases and Orf15 from cep Gene Cluster Is a Glc-1-P Thymidyltransferase”. Jin-Yuan Ho, Yu-Ting Huang, Chang-Jer Wu, Yi-Shan Li, Ming-Daw Tsai, and Tsung-Lin Li, J. Am. Chem. Soc. 128, 13694-13695 (2006).




  1. “ASFV DNA Polymerase X Is Extremely Error-Prone under Diverse Assay Conditions and within Multiple DNA Sequence Contexts.” Brandon J. Lamarche, Sandeep Kumar, and Ming-Daw Tsai, Biochemistry 45, 14826-14833 (2006).




  1. “Ankyrin repeat: a unique motif mediating protein-protein interactions”. Junan Li, Anjali Mahajan, and Ming-Daw Tsai, Biochemistry 45, 15168-15178 (2006). (Review)




  1. “Use of Damaged DNA and dNTP Substrates by the Error-Prone DNA Polymerase X from African Swine Fever Virus”. Sandeep Kumar, Brandon J. Lamarche, and Ming-Daw Tsai, Biochemistry 46, 3814-3825 (2007).




  1. “Human DNA Ligase IV and the Ligase IV/XRCC4 Complex: Analysis of Nick Ligation Fidelity.” Yu Wang, Brandon J. Lamarche, and Ming-Daw Tsai, Biochemistry 46, 4962-4976 (2007).




  1. “A Unified Kinetic Mechanism Applicable to Multiple DNA Polymerases”. Marina Bakhtina, Michelle P. Roettger, Sandeep Kumar, and Ming-Daw Tsai, Biochemistry 46, 5463-5472 (2007).




  1. “Identification of Histone Demethylases from Sacchromyces cerevisiae”. Shengjiang Tu, Esther M. M. Bulloch, Lanhao Yang, Chen Ren, Pang-Hung Hsu, Wei-Chieh Huang, Chein-Hung Chen, Chung-Lin Liao, Hui-Ming Yu, Wan-Sheng Lo, Michael A. Freitas, Ming-Daw Tsai, J. Biol. Chem. 282, 14262-14271 (2007).




  1. “Human p16, a novel transcriptional variant of p16INK4A, coexpresses with p16INK4A in cancer cells and inhibits cell-cycle progression”. You-Chin Lin, Mitchell B. Diccianni, Youngjin Kim, Hsin-Hung Lin, Chien-Hsin Lee, Ruey-Jen Lin, Sang Hoon Joo, Junan Li, An-Suei Yang, Huan-Hsien Kuo, Ming-Daw Tsai, Alice L. Yu, Oncogene 26, 7017-7027 (2007).




  1. “Investigation of the Conformational States of Wzz and the Wzz-O-antigen Complex under Near-Physiological Conditions”. Kuo-Hsiang Tang, Hongjie Guo, Wen Yi, Ming-Daw Tsai, and Peng George Wang, Biochemistry 46, 11744-11752 (2007).




  1. “Dissection of Protein-Protein Interaction and CDK4 Inhibition in the Oncogenic versus Tumor Suppressing Functions of Gankyrin and P16.” Anjali Mahajan, Yi Guo, Christopher M. Weghorst, Chunhua Yuan, Ming-Daw Tsai, Junan Li, J. Mol. Biol. 373, 990-1005 (2007).




  1. “A Unique FMN-linked Primary Alcohol Oxidase for Glycopeptide A40926 Maturation”. Yi-Shan Li, Jin-Yuan Ho, Chia-Chi Huang, Syue-Yi Lyu, Chun-Yen Lee, Yu-Ting Huang, Chang-Jer Wu, Hsiu-Chien Chan, Chuan-Jiuan Huang, Ning-Shian Hsu, Ming-Daw Tsai, and Tsung-Lin Li, J. Am. Chem. Soc. 129, 13384-13385 (2007).




  1. “Identification of in Vivo Phosphorylation Sites and Their Functional Significance in the Sodium Iodide Symporter”. Douangsone D. Vadysirisack, Eric S.-W. Chen, Zhaoxia Zhang, Ming-Daw Tsai, Geen-Dong Chang, and Sissy M. Jhiang, J. Biol. Chem. 282, 36820-8 (2007).




  1. “Solution Structures of 2:1 and 1:1 DNA Polymerase-DNA Complexes Probed by Ultracentrifugation and Small-Angle X-ray Scattering”. Kuo-Hsiang Tang, Marc Niebuhr, Ann Aulabaugh, and Ming-Daw Tsai, Nucleic Acids Res. 36, 849-860 (2008).




  1. “The ARID domain of the H3K4 demethylase RBP2 binds to a DNACCGCCC motif”. Shengjiang Tu, Yu-Ching Teng, Chunhua Yuan, Ying-Ta Wu, Meng-Yu Chan, An-Ning Cheng, Po-Hsun Lin, Li-Jung Juan, and Ming-Daw Tsai, Nature Struc. Mol. Biol. 15, 419-421 (2008).




  1. “Structure and Function of 2:1 DNA Polymerase·DNA Complexes”. Kuo-Hsiang Tang and Ming-Daw Tsai, J. Cellular Physiology 216, 315-320 (2008). (Review)



  1. “Mismatched dNTP Incorporation by DNA Polymerase Does Not Proceed via Globally Different Conformational Pathways”. Kuo-Hsiang Tang, Marc Niebuhr, Chang-Shung Tung, Hsiu-chien Chan, Chia-Cheng Chou, and Ming-Daw Tsai, Nucleic Acids Res. 36, 2948-2957 (2008). [Faculty of 1000]




  1. “Diphosphothreonine-specific interaction between SQ/TQ cluster and an FHA domain in the Rad53-Dun1 kinase cascade”. Hyun Lee, Chunhua Yuan, Andrew Hammet, Anjali Mahajan, Eric S.-W. Chen, Ming-Ru Wu, Mei-I Su, Jörg Heierhorst, Ming-Daw Tsai, Mol. Cell 30, 767-778 (2008). [Faculty of 1000] (This paper has been featured in Science, Science Signaling, and Mol Cell.)




  1. “Altered Order of Substrate Binding by DNA Polymerase X from African Swine Fever Virus”. Sandeep Kumar, Marina Bakhtina, and Ming-Daw Tsai, Biochemistry 47, 7875-7887 (2008).




  1. “Mismatched and Matched dNTP Incorporation by DNA Polymerase β Proceed via Analogous Kinetic Pathways”. Michelle P. Roettger, Marina Bakhtina, and Ming-Daw Tsai, Biochemistry 47, 9718-9727 (2008).




  1. “Structure and Function of the Phosphothreonine-Specific FHA Domain”. Anjali Mahajan, Chunhua Yuan, Hyun Lee, Eric S.-W. Chen, Pei-Yu Wu, and Ming-Daw Tsai, Science Signaling 1, re12 (2008). (Review)




  1. “Humoral immunity against capsule polysaccharide protects host from magA+ Klebsiella pneumoniae-induced lethal disease through evading TLR4 signaling”. Ming-Fang Wu, Chih-Ya Yang, Tzu-Lung Lin, Jin-Town Wang, Feng-Ling Yang, Shih-HsiungWu, Bor-Shen Hu, Teh-Ying Chou, Ming-Daw Tsai, Chi-Hung Lin, Shie-Liang Hsieh, Infect. Immun. 77, 615-621 (2009).




  1. “AMP-Activated Protein Kinase Functionally Phosphorylates Endothelial Nitric Oxide Synthase Ser-633”. Zhen Chen, I-Chen Peng, Wei Sun, Mei-I Su, Pang-Hung Hsu, Yi Fu, Yi Zhu, Kathryn DeFea, Songqin Pan, Ming-Daw Tsai, and John Y-J. Shyy, Circulation Res. 104, 496-505 (2009).




  1. “Contribution of the Reverse Rate of the Conformational Step to Polymerase  Fidelity”. Marina Bakhtina, Michelle P. Roettger, and Ming-Daw Tsai, Biochemistry 48, 3197-3208 (2009).




  1. “Comparisons of the Conformational Stability of Cyclin-dependent Kinase (CDK) 4-Interacting Ankyrin Repeat (AR) Proteins”. Yi Guo, Anjali Mahajan, Chunhua Yuan, Sang Hoon Joo, Christopher M. Weghorst, Ming-Daw Tsai, and Junan Li, Biochemistry 48, 4050-4062 (2009).




  1. “Trans-Cyclization of Phosphatidylinositol Catalyzed by Phospholipase C from Streptomyces antibioticus”. Chuan Bai, Li Zhao, Mario Rebecchi, Ming-Daw Tsai, and Karol S. Bruzik, J. Am. Chem. Soc. 131, 8362-8363 (2009).




  1. “Unambiguous Determination of Isobaric Histone Modifications by Reverse-Phase Retention Time and High-Mass Accuracy”. Lanhao Yang, Shengjiang Tu, Chen Ren, Esther M. M. Bulloch, Chung-Lin Liao, Ming-Daw Tsai, Michael A. Freitas, Anal. Biochem. 396, 13-22 (2010).




  1. “JNK-Mediated Turn-Over and Stabilization of the Transcription Factor p45/NF-E2 During Differentiation of Murine Erythroleukemia Cells”. Tung-Liang Lee, Yu-Chiau Shyu, Pang-Hung Hsu, Chiung-Wen Chang, Shau-Ching Wen, Ming-Daw Tsai, and Che-Kun James Shen, Proc. Natl. Acad. Sci. 107, 52-57 (2010).




  1. “Unique Catalytic Mechanism of Phosphatidylinositol-Specific Phospholipase C from Streptomyces antibioticus”. Chaun Bai, Li Zhao, Ming-Daw Tsai, Karol S. Bruzik, J. Am. Chem. Soc. 132, 1210-1211 (2010).




  1. “Catalytic Mechanism of DNA Polymerases,” Michelle P. Roettger, Marina Bakhtina, Sandeep Kumar, and Ming-Daw Tsai, in “Comprehensive Natural Products II Chemistry and Biology”; Mander, L., Lui, H.-W, Eds.; Elsevier: Oxford; volume 8, pp349-383 (2010). (Review)




  1. “Nonhydrolyzable Analogs of Phosphatidylinositol as Ligands of Phospholipases C.” Cornelia Mihai , Xiangjun Yue, Li Zhao, Alex Kravchuk, Ming-Daw Tsai, and Karol S. Bruzik, New J. Chem. 34, 925-933 (2010). (Review)



  1. “Global Analysis of Modifications of Human BK Virus Structural proteins by Mass Spectrometry”, Fang, C.-Y.; Hsu, P.-H.; Chen, S.-Y.; Wang, M.; Chen, P.-L.; Chang, C.-F.; Chen, L.-S.; Shen, C.-H.; Ou, W.-C.; Tsai, M.-D.; Chang, D., Virology 402, 164-176 (2010).




  1. “Contributions of conserved TPLH tetrapeptides to the conformational stability of ankyrin repeat proteins.” Yi Guo, Chunhua Yuan, Feng Tian, Kun Huang, Christopher M. Weghorst, Ming-Daw Tsai, Junan Li, J. Mol. Biol. 399, 168-181 (2010).




  1. “alpha-Helical burst on the folding pathway of FHA domains from Rad53 and Ki67”. Matsumura Y, Shinjo M, Mahajan A, Tsai MD, Kihara H, Biochimie 92, 1031-1039 (2010).




  1. “Database Search Algorithm for Identification of Intact Cross-Links in Proteins and Peptides Using Tandem Mass Spectrometry”. Hua Xu, Pang-Hung Hsu, Liwen Zhang, Ming-Daw Tsai, and Michael A. Freitas, J. Proteomics Res. 9, 3384-3393 (2010).




  1. “High-throughput identification of compounds targeting influenza RNA-dependent RNA polymerase activity”. Ching-Yao Su , Ting-Jen R. Cheng, Meng-I Lin, Shi-Yun Wang, Wen-I Huang, Shao-Ying Lin-Chu, Yu-Hou Chen, Chung-Yi Wu, Michael M. C. Lai, Wei-Chieh Cheng, Ying-Ta Wu, Ming-Daw Tsai, Yih-Shyun E. Cheng, and Chi-Huey Wong, Proc. Natl. Acad. Sci. USA, 107, 19151-6 (2010).




  1. “Regioselective deacetylation based on teicoplanin-complexed Orf2* crystal structures”. Hsiu-Chien Chan, Yu-Ting Huang, Syue-Yi Lyu, Chuen-Jiuan Huang, Yi-Shan Li, Yu-Chen Liu, Chia-Cheng Chou, Ming-Daw Tsai, and Tsung-Lin Li, Molecular BioSystems 7, 1224-1231 (2011).




  1. “The histone H3K36 demethylase Rph1/KDM4 regulates the expression of the photoreactivation gene PHR1”. Chung-Yi Liang, Pang-Hung Hsu, Dai-Fang Chou, Chao-Yu Pan, Wei-Chieh Huang, Ming-Daw Tsai, Wan-Sheng Lo, Nucl. Acids. Res. 39, 4151-4165 (2011).




  1. “Interception of teicoplanin oxidation intermediates yields new antimicrobial scaffolds”. Yu-Chen Liu, Yi-Shan Li, Syue-Yi Lyu, Li-Jen Hsu, Yu-Hou Chen, Yu-Ting Huang, Hsiu-Chien Chan, Chuen-Jiuan Huang, Gan-Hong Chen, Chia-Cheng Chou, Ming-Daw Tsai, and Tsung-Lin Li, Nature Chem. Biol. 7, 304-309 (2011).




  1. “Functions of some capsular polysaccharide biosynthetic genes in Klebsiella pneumonia NTUH K-2044”. Jin-Yuan Ho, Tzu-Lung Lin, Chun-Yen Li, Arwen Lee, An-Ning Cheng, Ming-Chuan Chen, Shih-Hsiung Wu, Jin-Town Wang, Tsung-Lin Li, and Ming-Daw Tsai, PLoS One, 6, e21664 (2011).




  1. “The Regulatory Mechanisms of Tumor Suppressor P16INK4A and Relevance to Cancer”. Junan Li, Ming-Jye Poi, and Ming-Daw Tsai, Biochemistry 50, 5566-5582 (2011). (Review)




  1. “The C-Terminus of Histone H2B Is Involved in Chromatin Compaction Specifically at Telomeres, Independently of Its Monoubiquitylation at Lysine 123”. Chen-Yi Wang, Chia-Yin Hua, Hsiang-En Hsu, Chia-Ling Hsu, Hsin-Yi Tseng, Duncan E. Wright, Pang-Hung Hsu, Chih-Hung Jen, Chia-Yeh Lin, Meng-Ying Wu, Min-Daw Tsai, Cheng-Fu Kao, PLoS One, 6, e22209 (2011).




  1. “Protein kinase A-mediated serine 35 phosphorylation dissociates histone H1.4 from mitotic chromosome”. Chi-Shuen Chu, Pang-Hung Hsu, Pei-Wen Lo, Elisabeth Scheer, Laszlo Tora, Heng-Jen Tsai, Ming-Daw Tsai, and Li-Jung Juan, J. Biol. Chem. 286, 35843-35851 (2011).




  1. “Kinetic mechanism of active site assembly and chemical catalysis of DNA Polymerase ”. Paul B. Balbo, Eric Chun-Wei Wang, and Ming-Daw Tsai, Biochemistry 50, 9865-9875 (2011).




  1. “E339…R416 salt bridge of nucleoprotein as a feasible target for influenza virus inhibitors”. Yu-Fang Shen, Yu-Hou Chen, Shao-Ying Chu, Meng-I Lin, Hua-Ting Hsu, Pei-Yu Wu, Chao-Jung Wu, Hui-Wen Liu, Fu-Yang Lin, Gialih Lin, Pang-Hung Hsu, An-Suei Yang, Yih-Shyun E. Cheng, Ying-Ta Wu, Chi-Huey Wong, and Ming-Daw Tsai, Proc. Natl. Acad. Sci. USA 108, 16515-16520 (2011).




  1. “Phosphorylation of NuSAP by Cdk1 regulates its interaction with microtubules in mitosis”. Han-Yi Chou, Ting-Huang Wang, Sheng-Chung Lee, Pang-Hung Hsu, Ming-Daw Tsai, Chih-Ning Chang, and Yung-Ming Jeng, Cell Cycle 10, 4083-4089 (2011).




  1. "Structural delineation of MDC1 FHA domain binding with CHK2 pThr68". Hsin-Hui Wu, Pei-Yu Wu, Kai-Fa Huang, Yu-Ya Kao, and Ming-Daw Tsai, Biochemistry 51, 575-577 (2012).




  1. “SUMOylation of Blimp-1 is critical for plasma cell differentiation.” Ying, Hsia-Yuan; Su, Shin-Tang; Hsu, Pang-Hung; Chang, Che-Chang; Lin, I-Ying; Tseng, Yu-Hsuan; Chen, Mei-Yu; Tsai, Ming-Daw; Shih, Hsiu-Ming; Lin, Kuo-I, EMBO Rep. 13, 631-637 (2012).




  1. “Intermolecular binding between TIFA-FHA and TIFA-pT mediates TNFα stimulation and NF-κB activation". Chia-Chi Flora Huang, Jui-Hung Weng, Tong-You Wade Wei, Pei-Yu Gabriel Wu, Pang-Hung Hsu, Yu-Hou Chen, Shun-Chang Wang, Dongyan Qin, Chin-Chun Hung, Shui-Tsong Chen, Andrew H.-J. Wang, John Y.-J. Shyy, and Ming-Daw Tsai, Mol. Cell Biol. 32, 2664-2673 (2012).




  1. “Loss of NPGPx, an oxidative stress sensor, compromises GRP78 chaperone activity and causes systemic oxidative stress, high tumor incidence and shortened lifespan.” Pei-Chi Wei, Yi-Hsuan Hsieh, Mei-I Su, X.-J. Jiang, Pang-Hung Hsu, Wen-Ting Lo, Yi-Cheng Chang, Yung-Ming Jeng, Ju-Ming Wang, Phang-lang Chen, Kao-Fen Lee, Ming-Daw Tsai, Jin-Yuh Shew and Wen-Hwa Lee, Mol. Cell 48, 747-759 (2012).




  1. “Amino acid substitutions of MagA in Klebsiella pneumoniae affect the biosynthesis of the capsular polysaccharide”. Tzu-Lung Lin, Feng-Ling Yang, Tsung-Lin Li, An-Suei Yang, Ming-Daw Tsai, Shih-Hsiung Wu, Jin-Town Wang, PLoS One, 7, e46783 (2012).




  1. “Ubc9 acetylation modulates distinct SUMO target modification and hypoxia response”. Yung-Lin Hsieh, Hong-Yi Kuo, Mandar T. Naik, Che-Chang Chang, Pei-Hsin Liao, Chun-Chen Ho, Tien-Chi Huang, Jen-Chong Jeng, Pang-Hung Hsu, Ming-Daw Tsai, Tai-Huang Huang, and Hsiu-Ming Shih, EMBO J. 32, 791-804 (2013).




  1. “Reversible acetylation regulates SIK2 and its function in autophagy”. Fu-Chia Yang, Bertrand Tan, Wei-Hao Chen, Ya-Huei Lin, Jing-Yi Huang, Hui-Yu Sun, Pang-Hung Hsu, Gunn-Guang Liou, James Shen, Ching-Jin Chang, Chau-Chung Han, Ming-Daw Tsai, and Sheng-Chung Lee, J. Biol. Chem. 288, 6227-6237 (2013).




  1. “Phosphorylation of mRNA Decapping Protein Dcp1a by the ERK Signaling Pathway during Early Differentiation of 3T3-L1 Preadipocytes”. Chiang PY, Shen YF, Su YL, Kao CH, Lin NY, Hsu PH, Tsai MD, Wang SC, Chang GD, Lee SC, Chang CJ, PLoS One, 8, e61697 (2013).




  1. “Histone Demethylase RBP2 Promotes Lung Tumorigenesis and Cancer Metastasis”. Yu-Ching Teng, Cheng-Feng Lee, Ying-Shiuan Li, Yi-Ren Chen, Pei-Wen Hsiao, Meng-Yu Chan, Feng-Mao Lin, Hsien-Da Huang, Yen-Ting Chen, Yung-Ming Jeng, Chih-Hung Hsu, Qin Yan, Ming-Daw Tsai, and Li-Jung Juan, Cancer Research 73, 4711-4721 (2013).




  1. “Evidence that P12, a specific variant of P16INK4A, plays a suppressive role in human pancreatic carcinogenesis”. Poi MJ, Knobloch TJ, Yuan C, Tsai MD, Weghorst CM, Li J., Biochem. Biophys. Res. Commun. 436, 217-222 (2013)




  1. “Molecular basis of the essential S phase function of the Rad53 checkpoint kinase”. Hoch NC, Chen ES, Buckland R, Wang SC, Fazio A, Hammet A, Pellicioli A, Chabes A, Tsai MD, Heierhorst J, Mol Cell Biol. 33, 3202-3213 (2013).




  1. “Interaction between Salt-inducible Kinase 2 (SIK2) and p97/VCP Regulates ER-associated Protein Degradation in Mammalian Cells”. Yang FC, Lin YH, Chen WH, Huang JY, Chang HY, Su SH, Wang HT, Chiang CY, Hsu PH, Ming-Daw Tsai, Tan BC, Sheng-Chung Lee, J. Biol. Chem. 288, 33861-33872 (2013).




  1. “Use of quantitative mass spectrometric analysis to elucidate the mechanisms of phospho-priming and auto-activation of the checkpoint kinase Rad53 in vivo”. Eric S.-W. Chen, Nicolas C. Hoch, Shun-Chang Wang, Achille Pellicioli, Jörg Heierhorst, and Ming-Daw Tsai, Mol Cell Proteomics 13, 551-565 (2014).




  1. “Biosynthesis of Streptolidine Involved Two Unexpected Intermediates Produced by a Dihydroxylase and a Cyclase with Unusual Mechanisms”. Chin-Yuan Chang, Syue-Yi Lyu, Yu-Chen Liu, Ning-Shian Hsu, Chih-Chung Wu, Cheng-Fong Tang, Kuan-Hung Lin, Jin-Yuan Ho, Chang-Jer Wu, Ming-Daw Tsai, & Tsung-Lin Li, Angewandte Chemie 53, 1943-1948 (2014).




  1. “Tight Regulation of a Timed Nuclear Import Wave of EKLF by PKCq and FOE during Pro-E to Baso-E Transition”. Yu-Chiau Shyu, Tung-Liang Lee, Xin Chen, Pang-Hung Hsu, Shau-Ching Wen, Yi-Wei Liaw, Chi-Huan Lu, Po-Yen Hsu, Mu-Jie Lu, JauLang Hwang, Ming-Daw Tsai, Ming-Jing Hwang, Jim-Ray Chen, and Che-Kun James Shen, Dev Cell. 28, 409-422 (2014).




  1. “Fha Interaction with Phosphothreonine of TssL Activates Type VI Secretion in Agrobacterium tumefaciens”. Jer-Sheng Lin, Hsin-Hui Wu, Pang-Hung Hsu, Lay-Sun Ma, Yin-Yuin Pang, Ming-Daw Tsai, and Erh-Min Lai, PLoS Pathogens, e1003991 (2014).




  1. “Structure and mechanism of a non-heme iron-SAM dependent C-methyltransferase and its engineering to hydratase and O-methyltransferase”. Xiao-Wei Zou, Yu-Chen Liu, Ning-Shian Hsu, Chuen-Jiuan Huang, Syue-Yi Lyu, Hsiu-Chien Chan, Chin-Yuan Chang, Hsien-Wei Yeh, Kuan-Hung Lin, Chang-Jer Wu, Ming-Daw Tsai and Tsung-Lin Li, Acta Crystallographica Section D70, 1549-1560 (2014).




  1. “How a low-fidelity DNA polymerase chooses non-Watson-Crick from Watson-Crick incorporation”. Wen-Jin Wu, Mei-I Su, Jian-Li Wu, Sandeep Kumar, Liang-hin Lim, Chun-Wei Eric Wang, Frank H. T. Nelissen, Ming-Chuan Chad Chen, Jurgen F. Doreleijers, Sybren S. Wijmenga, and Ming-Daw Tsai, J. Am. Chem. Soc. 136, 4927-4937 (2014). [Featured in ASBMB TODAY http://wildtypes.asbmb.org/2014/03/20/how-a-polymerase-bypasses-the-rules-of-watson-crick-base-pairing/ ] [ http://www.asbmb.org/asbmbtoday/ ]




  1. “How DNA Polymerases Catalyze DNA Replication, Repair, and Mutation”. Ming-Daw Tsai, Biochemistry 53, 2749-2751 (2014).




  1. “Multiple complexes of long-aliphatic N-acyltransferases led to synthesis of 2,6-diacylated/2-acyl-substituted glycopeptide antibiotics effectively killing VRE”. Lyu, Syue-Yi; Liu, Yu-Chen; Chang, Chin-Yuan; Huang, Chuen-Jiuan; Chiu, Ya-Huang; Huang, Chun-Man; Hsu, Ning-Shian; Lin, Kuan-Hung; Wu, Chang-Jer; Tsai, Ming-Daw; Li, Tsung-Lin. J. Am. Chem. Soc. 136, 10989-10995 (2014).




  1. “Ultrafast water dynamics at the interface of polymerase-DNA binding complex”. Yi Yang, Yangzhong Qin, Qing Ding, Marina Bakhtina, Lijuan Wang, Ming-Daw Tsai, and Dongping Zhong, Biochemistry 53, 5405-5413 (2014).




  1. “PP2A and Aurora differentially modify Cdc13 to promote telomerase release from telomeres at G2/M phase”. Zih-Jie Shen , Pang-Hung Hsu , Yu-Tai Su , Chia-Wei Yang , Li Kao , Shun-Fu Tseng , Ming-Daw Tsai, and Shu-Chun Teng, Nature Commun. 5, 5312 (2014).




  1. “A ribonuclease coordinates siRNA amplification and mRNA cleavage during RNAi”. Hsin-Yue Tsai, Chun-Chieh G. Chen, James Moresco, Darryl Conte Jr, Daniel A. Chaves, Shohei Mitani, John Yates III, Ming-Daw Tsai, and Craig C. Mello, Cell, 160(3), 407-419 (2015).




  1. “The RNA recognition motif of NIFK is required for rRNA maturation during cell cycle progression”. Wen An Pan, Hsin-Yue Tsai, Shun-Chang Wang, Michael Hsiao, Pei-Yu Gabriel Wu, and Ming-Daw Tsai, RNA Biology, 12(3), 255-267 (2015).




  1. “PHRF1 promotes genome integrity by modulating non-homologous end-joining". by Chi-Fang Chang, Ming-Ying Yu, Jin-Yu Lee, Po-Chen Chu, Pei-Yu Wu, and Ming-Daw Tsai, and Mau-Sun Chang, Cell Death and Disease, 6, e1716 (2015).




  1. “Uncovering the mechanism of FHA domain-mediated TIFA oligomerization that plays a central role in immune responses”. Jui-Hung Weng, Yin-Cheng Hsieh, Chia-Chi Flora Huang, Kai-Fa Huang, Chun-Jung Chen, and Ming-Daw Tsai, Biochemistry, 54(40), 6219-6229 (2015).



  1. “Protein Arginine Methyltransferase 8: Tetrameric Structure and Protein Substrate Specificity”. Wei-Chao Lee, Wen-Ling Lin, Tsutomu Matsui, Eric S.-W. Chen, Tong-You Wade Wei, Wen-Hsuan Lin, Hao Hu, Yujun George Zheng, Ming-Daw Tsai, and Meng-Chiao Ho, Biochemistry, accepted (2015).




  1. “Structural Mechanism for the Fidelity Modulation of DNA Polymerase ”. Mu-Sen Liu, Hsin-Yue Tsai, Xiao-Xia Liu, Meng-Chiao Ho, Wen-Jin Wu, and Ming-Daw Tsai, J. Am. Chem. Soc. 138, 2389-2398 (2016).




  1. “The Nucleolar Protein NIFK Promotes Cancer Progression via CK1/β-catenin in Metastasis and Ki-67-dependent Cell Proliferation”.  Tsung-Chieh Lin, Chia-Yi Su, Pei-Yu Wu, Tsung-Ching Lai, Wen-An Pan, Yi-Hua Jan, Yu-Chang Chang, Chi-Tai Yeh, Chi-Long Chen, Luo-Ping Ger, Hong-Tai Chang, Chih-Jen Yang, Ming-Shyan Huang, Yu-Peng Liu, Yuan-Feng Lin, John Y.-J. Shyy, Ming-Daw Tsai, and Michael Hsiao, eLife, 5, e11288 (2016).

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