Publications

Distefano Group Research Publications

74.        DeGraw, A. J.; Xu, J.; Distefano, M. D., Synthesis and characterization of caged isoprenoid diphosphates for the study of protein prenylation. Organic Letters 2007 , submitted.

73.        Lenevich, S.; Hosokawa, A.; Cramer, C. J.; Distefano, M. D., Transition State Analysis of Model and Enzymatic Prenylation Reactions. Journal of the American Chemical Society 2007 , in press.

72.        Hosokawa, A.; Wollack, J. W.; Zhang, Z.; Chen, L.; Barany, G.; Distefano, M. D., Evaluation of an alkyne-containing analogue of farnesyl diphosphate as a dual substrate for protein-prenyltransferases. International Journal of Peptide Research and Therapeutics 2007 , in press.

71.        DeGraw, A. J.; Zhao, Z.; Hsieh, J.; Jefferies, M.; Distefano, M. D.; Strickland, C. L.; Shintani, D.; Nural, H.; McMahan, C.; Xie, W., A photoactive isoprenoid diphosphate analogue   containing a stable phosphonate linkage: synthesis and biochemical studies with prenyltransferases. Journal of Organic Chemistry 2007 , in press.

70.        Duckworth, B. P.; Zhang, Z.; Hosokawa, A.; Distefano, M. D., Selective Labeling of Proteins using Protein Farnesyltransferase. ChemBioChem 2007, 8, (1), 98-105.

69.        Xu, J.; DeGraw, A. J.; Duckworth, B. P.; Lenevich, S.; Tann, C.-M.; Jenson, E. C.; Gruber, S. J.; Barany, G.; Distefano, M. D., Synthesis and Reactivity of 6,7-Dihydrogeranylazides: Reagents for Primary Azide Incorporation into Peptides and Subsequent Staudinger Ligation. Chemical Biology and Drug Design 2006, 68, 85-96.

68.        Duckworth, B. P.; Xu, J.; Taton, T. A.; Guo, A.; Distefano, M. D., Site-Specific, Covalent Attachment of Proteins to a Solid Surface. Bioconjugate Chemistry 2006, 17, (4), 967-974.

67.        Distefano, M. D.; Albers, L. N.; Xu, J.-H., Protein Prenylation. In Encyclopedic Reference of Genomics and Proteomics in Molecular Medicine , Ruckpaul, K.; Ganten, D., Eds. Springer-Verlag: Heidelberg, Germany, 2006 ; pp 349-354.

66.        Xu, J.-H.; Lenevich, S.; Boggs, J.; Mullen, D. G.; Barany, G.; Distefano Mark, D., Enzymatic Incorporation of Prenylazides into Peptides and Proteins: Tools for Selective Protein Labeling. In Understanding Biology Using Peptides: Proceedings of the 19th American Peptide Symposium , Blondelle, S. E., Ed. Kluwer Academic Publishers: Norwell, 2005 ; pp 297-299.

65.        Rose, M. W.; Xu, J.; Kale, T. A.; O'Doherty, G.; Barany, G.; Distefano, M. D., Enzymatic incorporation of orthogonally reactive prenylazide groups into peptides via protein farnesyltransferase: implications for selective protein labeling. Biopolymers 2005, 80, (2-3), 164-171.

64.        Rose, M. W.; Rose, N. D.; Boggs, J.; Lenevich, S.; Xu, J.; Barany, G.; Distefano, M. D., Evaluation of geranylazide and farnesylazide diphosphate for incorporation of prenylazides into a CAAX box-containing peptide using protein farnesyltransferase. J. Peptide. Res. 2005, 65, 529-537.

63.        Duckworth, B.; Distefano, M., Protein-based artificial enzymes. In Artificial Enzymes , Breslow, R., Ed. Wiley-VCH Verlag: Weinheim, Germany, 2005 ; pp 109-132.

62.        Adams, D. N.; Kao, E. Y.-C.; Hypolite, C. L.; Distefano, M. D.; Hu, W.-S.; Letourneau, P. C., Growth cones turn and migrate up an immobilized gradient of the laminin IKVAV peptide. Journal of Neurobiology 2004, 62, (1), 134-147.

61.        Turek-Etienne, T. C.; Strickland, C. L.; Distefano, M. D., Biochemical and Structural Studies with Prenyl Diphosphate Analogues Provide Insights into Isoprenoid Recognition by Protein Farnesyl Transferase. Biochemistry 2003, 42, (13), 3716-3724.

60.        Kale, T. A.; Raab, C.; Yu, N.; Aquino, E.; Dean, D. C.; Distefano, M. D., Synthesis of high specific activity 35S-labelled N-methanesulfonyl farnesylcysteine and a photoactive analog. Journal of Labelled Compounds & Radiopharmaceuticals 2003, 46, (1), 29-54.

59.        Kale, T. A.; Hsieh, S.-a. J.; Rose, M. W.; Distefano, M. D., Use of synthetic isoprenoid analogues for understanding protein prenyltransferase mechanism and structure. Current Topics in Medicinal Chemistry 2003, 3, (10), 1043-1074.

58.        Kale, T. A.; Distefano, M. D., Diazotrifluoropropionamido-Containing Prenylcysteines: Syntheses and Applications for Studying Isoprenoid-Protein Interactions. Organic Letters 2003, 5, (5), 609-612.

57.        Franklin, M. C.; Kadkhodayan, S.; Ackerly, H.; Alexandru, D.; Distefano, M. D.; Elliott, L. O.; Flygare, J. A.; Mausisa, G.; Okawa, D. C.; Ong, D.; Vucic, D.; Deshayes, K.; Fairbrother, W. J., Structure and Function Analysis of Peptide Antagonists of Melanoma Inhibitor of Apoptosis (ML-IAP). Biochemistry 2003, 42, (27), 8223-8231.

56.        Kale, T. A.; Turek, T. C.; Chang, V.; Gautam, N.; Distefano, M. D., Preparation and application of G protein g subunit-derived peptides incorporating a photoactive isoprenoid. Methods in Enzymology 2002, 344, (G Protein Pathways, Part B), 245-258.

55.        Haring, D.; Lees Mason, R.; Banaszak Leonard, J.; Distefano Mark, D., Exploring routes to stabilize a cationic pyridoxamine in an artificial transaminase: site-directed mutagenesis versus synthetic cofactors. Protein Engineering 2002, 15, (7), 603-10.

54.        Distefano, M. D.; Zhong, A.; Cochran, A. G., Quantifying b -Sheet stability by phage display. Journal of Molecular Biology 2002, 322, (1), 179-188.

53.        Turek, T. C.; Gaon, I.; Distefano, M. D.; Strickland, C. L., Synthesis of Farnesyl Diphosphate Analogues Containing Ether-Linked Photoactive Benzophenones and Their Application in Studies of Protein Prenyltransferases. Journal of Organic Chemistry 2001, 66, (10), 3253-3264.

52.        Tann, C.-M.; Qi, D.; Distefano, M. D., Enzyme design by chemical modification of protein scaffolds. Current Opinion in Chemical Biology 2001, 5, (6), 696-704.

51.        Qi, D.; Tann, C.-M.; Haring, D.; Distefano, M. D., Generation of new enzymes via covalent modification of existing proteins. Chemical Reviews 2001, 101, (10), 3081-3111.

50.        Kale, T. A.; Raab, C.; Yu, N.; Dean, D. C.; Distefano, M. D., A Photoactivatable Prenylated Cysteine Designed to Study Isoprenoid Recognition. Journal of the American Chemical Society 2001, 123, (19), 4373-4381.

49.        Häring, D.; Distefano, M. D., Specific Host-Guest Interactions in a Protein-Based Artificial Transaminase. Bioorganic and Medicinal Chemistry 2001, 9, 2461-2466.

48.        Haring, D.; Distefano, M. D., Converting a Fatty Acid Binding Protein to a Artificial Transaminase: Novel Catalysts by Chemical and Genetic Modification of a Protein Cavity. Journal of Molecular Catalysis. B, Enzymatic 2001, 11, 967-970.

47.        Haering, D.; Distefano, M. D., Enzymes by Design: Chemogenetic Assembly of Transamination Active Sites Containing Lysine Residues for Covalent Catalysis. Bioconjugate Chemistry 2001, 12, (3), 385-390.

46.        Clausen, V. A.; Edelstein, R. L.; Distefano, M. D., Stereochemical Analysis of the Reaction Catalyzed by Human Protein Geranylgeranyl Transferase. Biochemistry 2001, 40, (13), 3920-3930.

45.        Kuang, H.; Haring, D.; Qi, D.; Mazhary, A.; Distefano, M. D., Synthesis of a cationic pyridoxamine conjugation reagent and application to the mechanistic analysis of an artificial transaminase. Bioorganic & Medicinal Chemistry Letters 2000, 10, 2091-2095.

44.        Kale, T. A.; Distefano, M. D., Photoaffinity-labeled probes for the study of isoprenoid recognition sites. Peptides for the New Millennium, Proceedings of the American Peptide Symposium, 16th, Minneapolis, MN, United States, June 26-July 1, 1999 2000 , 109-110.

43.        Distefano, M. D.; Kuang, H.; Qi, D.; Haring, D.; Ory, J.; Banaszak, L. J., Semisynthetic approaches for the design of proteins with catalytic activity using fatty acid binding protein as a scaffold. Peptides for the New Millennium, Proceedings of the American Peptide Symposium, 16th, Minneapolis, MN, United States, June 26-July 1, 1999 2000 , 500-502.

42.        Davies, R. R.; Kuang, H.; Qi, D.; Mazhary, A.; Mayaan, E.; Distefano, M. D., Artificial metalloenzymes based on protein cavities: exploring the effect of altering the metal ligand attachment position by site directed mutagenesis. Bioorganic & Medicinal Chemistry Letters 1999, 9, (1), 79-84.

41.        Weller, V. A.; Distefano, M. D., Measurement of the a -Secondary Kinetic Isotope Effect for a Prenyltransferase by MALDI Mass Spectrometry. Journal of the American Chemical Society 1998, 120, (31), 7975-7976.

40.        Turek, T. C.; Edelstein, R. L.; Gaon, I.; Weller, V. A.; Distefano, M. D., [32P]-labeled analogs of farnesyl and geranylgeranyl pyrophosphate: Synthesis and application in photoaffinity labeling experiments with protein prenyltransferases. In Synthesis and Applications of Isotopically Labelled Compounds 1997, Proceedings of the International Symposium, 6th, Philadelphia, PA, United States, Sept. 14-18, 1997 , 1998 ; 67-70.

39.        Tabakovic, I.; Gaon, I.; Distefano, M. D., Anodic oxidation of substituted [4-hydroxy-3-coumarinyl]-phenylthiomethanes in acetonitrile. Evidence for a cationic intermediate in carbon-sulfur bond fragmentation. Electrochimica Acta 1998, 43, (12-13), 1773-1778.

38.        Qi, D.; Kuang, H.; Distefano, M. D., Effects of metal ions on the rates and enantioselectivities of reactions catalyzed by a series of semisynthetic transaminases created by site directed mutagenesis. Bioorganic & Medicinal Chemistry Letters 1998, 8, (7), 875-880.

37.        Ory, J. J.; Mazhary, A.; Kuang, H.; Davies, R. R.; Distefano, M. D.; Banaszak, L. J., Structural characterization of two synthetic catalysts based on adipocyte lipid-binding protein. Protein Engineering 1998, 11, (4), 253-261.

36.        Kuang, H.; Distefano, M. D., Catalytic Enantioselective Reductive Amination in a Host-Guest System Based on a Protein Cavity. Journal of the American Chemical Society 1998, 120, (5), 1072-1073.

35.        Edelstein, R. L.; Weller, V. A.; Distefano, M. D.; Tung, J. S., Stereochemical Analysis of the Reaction Catalyzed by Yeast Protein Farnesyltransferase. Journal of Organic Chemistry 1998, 63, (16), 5298-5299.

34.        Distefano, M. D.; Kuang, H.; Qi, D.; Mazhary, A., The design of protein-based catalysts using semisynthetic methods. Current Opinion in Structural Biology 1998, 8, (4), 459-465.

33.        Turek, T. C.; Gaon, I.; Gamache, D.; Distefano, M. D., Synthesis and evaluation of benzophenone-based photoaffinity labeling analogs of prenyl pyrophosphates containing stable amide linkages. Bioorganic & Medicinal Chemistry Letters 1997, 7, (16), 2125-2130.

32.        Turek, T. C.; Gaon, I.; Distefano, M. D., Synthesis and rapid purification of 32P-labeled photoactive analogs of farnesyl pyrophosphate. Journal of Labelled Compounds & Radiopharmaceuticals 1997, 39, (2), 139-146.

31.        Kuang, H.; Davies, R. R.; Distefano, M. D., Modulation of the rate, enantioselectivity, and substrate specificity of semisynthetic transaminases based on lipid binding proteins using site directed mutagenesis. Bioorganic & Medicinal Chemistry Letters 1997, 7, (15), 2055-2060.

30.        Hypolite, C. L.; McLernon, T. L.; Adams, D. N.; Chapman, K. E.; Herbert, C. B.; Huang, C. C.; Distefano, M. D.; Hu, W.-S., Formation of Microscale Gradients of Protein Using Heterobifunctional Photolinkers. Bioconjugate Chemistry 1997, 8, (5), 658-663.

29.        Herbert, C. B.; McLernon, T. L.; Hypolite, C. L.; Adams, D. N.; Pikus, L.; Huang, C. C.; Fields, G. B.; Letourneau, P. C.; Distefano, M. D.; Hu, W.-S., Micropatterning gradients and controlling surface densities of photoactivatable biomolecules on self-assembled monolayers of oligo(ethylene glycol) alkanethiolates. Chemistry & Biology 1997, 4, (10), 731-737.

28.        Edelstein, R. L.; Distefano, M. D., Photoaffinity Labeling of Yeast Farnesyl Protein Transferase and Enzymatic Synthesis of a Ras Protein Incorporating a Photoactive Isoprenoid. Biochemical and Biophysical Research Communications 1997, 235, 377-382.

27.        Edelstein, R. L.; Distefano, M. D., Photoaffinity labeling of yeast farnesyl protein transferase and enzymic synthesis of a Ras protein incorporating a photoactive isoprenoid. Biochemical and Biophysical Research Communications 1997, 235, (2), 377-382.

26.        Davies, R. R.; Distefano, M. D., A Semisynthetic Metalloenzyme Based on a Protein Cavity That Catalyzes the Enantioselective Hydrolysis of Ester and Amide Substrates. Journal of the American Chemical Society 1997, 119, (48), 11643-11652.

25.        Turek, T. C.; Gaon, I.; Distefano, M. D., Analogs of farnesyl pyrophosphate incorporating internal benzoylbenzoate esters: synthesis, inhibition kinetics and photoinactivation of yeast protein farnesyltransferase. Tetrahedron Letters 1996, 37, (28), 4845-4848.

24.        Kuang, H.; Brown, M. L.; Davies, R. R.; Young, E. C.; Distefano, M. D., Enantioselective Reductive Amination of a-Keto Acids to a-Amino Acids by a Pyridoxamine Cofactor in a Protein Cavity. Journal of the American Chemical Society 1996, 118, (44), 10702-10706.

23.        Gaon, I.; Turek, T. C.; Weller, V. A.; Edelstein, R. L.; Singh, S. K.; Distefano, M. D., Photoactive Analogs of Farnesyl Pyrophosphate Containing Benzoylbenzoate Esters: Synthesis and Application to Photoaffinity Labeling of Yeast Protein Farnesyltransferase. Journal of Organic Chemistry 1996, 61, (22), 7738-7745.

22.        Gaon, I.; Turek, T. C.; Distefano, M. D., Farnesyl and geranylgeranyl pyrophosphate analogs incorporating benzoylbenzyl ethers: synthesis and inhibition of yeast protein farnesyltransferase. Tetrahedron Letters 1996, 37, (49), 8833-8836.

21.        Distefano, M. D.; Dervan, P. B., Energetics of cooperative binding of oligonucleotides with discrete dimerization domains to DNA by triple helix formation. Proceedings of the National Academy of Sciences of the United States of America 1993, 90, (4), 1179-83.

20.        Colocci, N.; Distefano, M. D.; Dervan, P. B., Cooperative oligonucleotide-directed triple helix formation at adjacent DNA sites. Journal of the American Chemical Society 1993, 115, (11), 4468-73.

19.        Distefano, M. D.; Dervan, P. B., Ligand-promoted dimerization of oligonucleotides binding cooperatively to DNA. Journal of the American Chemical Society 1992, 114, (27), 11006-7.

18.        Schiering, N.; Kabsch, W.; Moore, M. J.; Distefano, M. D.; Walsh, C. T.; Pai, E. F., The Three Dimensional Structure of Mercuric Ion Reductase from Bacillus Strain RC607. In Flavins and Flavoproteins 1990 , ed.; Curti, B.; Ronchi, S.; Zanetti, G., 'Ed.'^'Eds.' Walter de Gruyter & Co.: Berlin, 1991, 'Vol.' p^pp 615-625.

17.        Schiering, N.; Kabsch, W.; Moore, M. J.; Distefano, M. D.; Walsh, C. T.; Pai, E. F., Structure of the Detoxification Catalyst Mercuric Ion Reductase from Bacillus sp. strain RC607. Nature 1991, 352, 168-172.

16.        Distefano, M. D.; Shin, J. A.; Dervan, P. B., Cooperative binding of oligonucleotides to DNA by triple helix formation: dimerization via Watson-Crick hydrogen bonds. Journal of the American Chemical Society 1991, 113, (15), 5901-2.

15.        Raybuck, S. A.; Distefano, M. D.; Teo, B. K.; Orme-Johnson, W.; Walsh, C. T., An EXAFS investigation of Hg(II) binding to mercuric reductase: comparative analysis of the wild-type enzyme and a mutant enzyme generated by site-directed mutagenesis. Journal of the American Chemical Society 1990, 112, (5), 1983-9.

14.        Moore, M. J.; Distefano, M. D.; Zydowsky, L. D.; Cummings, R. T.; Walsh, C. T., Organomercurial lyase and mercuric ion reductase: nature's mercury detoxification catalysts. Accounts of Chemical Research 1990, 23, (9), 301-8.

13.        Miller, S. M.; Massey, V.; Ballou, D.; Williams, C. H., Jr.; Distefano, M. D.; Moore, M. J.; Walsh, C. T., Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase. Biochemistry 1990, 29, (11), 2831-41.

12.        Distefano, M. D.; Moore, M. J.; Walsh, C. T., Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: evidence from in vivo and in vitro heterodimer formation. Biochemistry 1990, 29, (11), 2703-13.

11.        Moore, M. J.; Distefano, M. D.; Walsh, C. T.; Schiering, N.; Pai, E. F., Purification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607. Journal of Biological Chemistry 1989, 264, (24), 14386-8.

10.        Miller, S. M.; Moore, M. J.; Massey, V.; Williams, C. H., Jr.; Distefano, M. D.; Ballou, D. P.; Walsh, C. T., Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase. Biochemistry 1989, 28, (3), 1194-205.

9.          Distefano, M. D.; Au, K. G.; Walsh, C. T., Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry. Biochemistry 1989, 28, (3), 1168-83.

8.          Walsh, C. T.; Distefano, M. D.; Moore, M. J.; Shewchuk, L. M.; Verdine, G. L., Molecular basis of bacterial resistance to organomercurial and inorganic mercuric salts. FASEB Journal 1988, 2, (2), 124-30.

7.          Walsh, C.; Distefano, M.; Moore, M., Mutagenesis of paired cysteine residues in the disulphide-containing flavoprotein mercuric ion reductase from mercury-resistant bacteria. Biochemical Society Transactions 1988, 16, (2), 90-1.

6.          Walsh, C. T., Moore, M. J., & Distefano, M. D., Conserved Cysteine Pairs of Mercuric Ion Reductase: An Investigation of Function Via Site-Directed Mutagenesis. In Flavins and Flavoproteins 1987 , ed.; Edmondson, D. E.; McCormick, D. B., 'Ed.'^'Eds.' Walter de Gruyter & Co.: Berlin, 1987, 'Vol.' p^pp 13-28.

5.          Walsh, C.; DiStefano, M.; Moore, M., Catalytic effects of mutagenesis of paired cysteine residues in the bacterial enzyme mercuric ion reductase. UCLA Symposia on Molecular and Cellular Biology, New Series 1987, 69, (Protein Struct., Folding, Des. 2), 283-92.

4.          Neidhard, D. J.; Distefano, M. D.; Tanizawa, K.; Soda, K.; Walsh, C. T.; Petsko, G. A., X-ray crystallographic studies of the alanine-specific racemase from Bacillus stearothermophilus. Overproduction, crystallization, and preliminary characterization. Journal of Biological Chemistry 1987, 262, (32), 15323-6.

3.          Moore, M. J.; Distefano, M. D.; Walsh, C. T.; Miller, S.; Massey, V.; Williams, C. H.; Ballou, D. P., The Penultimate Cysteines in Mercuric Reductase Aid in the Reduction of Mercury. In Flavins and Flavoproteins 1987 , ed.; Edmondson, D. E.; McCormick, D. B., 'Ed.'^'Eds.' Walter de Gruyter & Co.: Berlin, 1987, 'Vol.' p^pp 37-40.

2.          Massey, V.; Miller, S.; Ballou, D. P.; Williams, C. H.; Moore, M. J.; Distefano, M. D.; Walsh, C. T., Studies of the Active Site of Mercuric Reductase Employing Site Directed Mutants and the Thiol-Reactive Flavin, 6-SCN-FAD. In Flavins and Flavoproteins 1987 , ed.; Edmondson, D. E.; McCormick, D. B., 'Ed.'^'Eds.' Walter de Gruyter & Co.: Berlin, 1987, 'Vol.' p^pp 41-44.

1.          Kanazawa, T.; Distefano, M.; Bassham, J. A., Ammonia regulation of intermediary metabolism in photosynthesizing and respiring Chlorella pyrenoidosa: comparative effects of methylamine. Plant and Cell Physiology 1983, 24, (6), 979-86.