Publications

 

  1. Profiling Protease Activity in Laundry Detergents with Peptide Arrays and SAMDI Mass Spectrometry.  R. Dai, A. Ten and M. Mrksich.  Ind. & Eng. Chem. Res., in press.
  2. Storage of Information using Small Organic Molecules.  B. Cafferty, A. Ten, M. Fink, S. Morey, D. Preston, M. Mrksich and G.M. Whitesides.  ACS Central Science, in press.
  3. High-throughput mapping of COA metabolites by SAMDI-MS to optimize the cell-free biosynthesis of HMG-CoA. O’Kane, P.T., Dudley, Q.M., McMillan, A.K., Jewett, M.C., Mrksich M. Science Advances, 2019 5, 6. [PDF]
  4. Sequential Photoactivation of Self-Assembled Monolayers to Direct Cell Adhesion and Migration. Bugga, P., Mrksich, M. Langmuir2019, 35, 17, 5937-5943 [PDF]
  5. Using Peptide Arrays To Discover the Sequence-Specific Acetylation of the Histidine-Tyrosine Dyad. Szymczak, L., Mrksich, M. Biochemistry, 2019, 58, 13, 1810-1817 [PDF]
  6. Using Microfluidics and Imaging SAMDI-MS to Characterize Reaction Kinetics. Grant, J., O’Kane, P.T., Kimmel, B.R. and Mrksich, M. ACS Central Science, 2019, 5 (3), 486-493 [PDF]
  7. Exploration of the Nanomedicine-Design Space with High-Throughput Screening and Machine Learning. Yamankurt, G., Berns, E.J., Xue, A., Lee, A., Bagheri, N., Mrksich, M., Mirkin, C.A., Nature Biomedical Engineering., 2019 [PDF]
  8. A Photoactivatable Reaction for Covalent Nanoscale Patterning of Multiple Proteins.  S. Zhou, K. Metcalf, P. Bugga, J. Grant and M. Mrksich.  ACS App. Mat. & Int., 2018, 10, 40452-40459. [PDF]
  9. Long-Range Energy Transfer in Protein Megamolecules.  E.L. Taylor, K.J. Metcalf, B. Carlotti, C.-T. Lai, J.A. Modica, G.C. Schatz, M. Mrksich and T. Goodson.  J. Am. Chem. Soc., 2018, 140, 15731-15743. [PDF]
  10. High Throughput Enzyme Kinetics with 3D Microfluidics and Imaging SAMDI Mass Spectrometry.  Grant, J., Goudarzi, S.H. and Mrksich, M.  Anal. Chem., 2018, 90, 13096-13103. [PDF]
  11. Dynamic Substrates for Cell Biology.  Bugga, P. and Mrksich, M.  Curr. Op. Coll. & Inter. Sci., 2018, 38, 80-87.  [PDF]
  12. An Immobilized Enzyme Reactor for Spatiotemporal Control over Reaction Products.  Grant, J., Modica, J.A., Roll, J. Perkovich, P. and Mrksich, M.  Small, 2018, 31. [PDF]
  13. Single-Pot Glycoprotein Biosynthesis Using a Cell-Free Transcription-Translation System Enriched with Glycosylation Machinery.  T. Jaroentomeechai, J.C. Stark, A. Natarajan, C.J. Glasscock, L.E. Yates, K.J. Hsu, M. Mrksich, M.C. Jewett, and M.P. DeLisa.  Nature Comm., 2018, 9, 2686-2696. [PDF]
  14. An Unusual Salt Effect in an Interfacial Nucleophilic Substitution Reaction.  Li, S. and Mrksich, M.  Langmuir, 2018, 34, 6713-6718. [PDF]
  15. Traceless Immobilization of Analytes for High Throughput Experiments with SAMDI Mass Spectrometry.  Helal, K.Y., Alamgir, A., Berns, E.J. and Mrksich, M.  J. Am. Chem. Soc., 2018, 140, 8060-8063. [PDF]
  16. Synthesis of Cyclic Megamolecules.  Modica, J.A., Lin, Y. and Mrksich, M.  J. Am. Chem. Soc., 2018, 140, 6391-6399. [PDF]
  17. Sirt1 Transgene Delivery Improves Diabetes-Impaired Wound Healing.  M.C. Jen, C. Duan, Y. Zhu, A.J. Lortie, H.-Y. Kuo, A.Y. Yang, M. Mrksich and G.A. Ameer.  Submitted to Proc. Natl. Acad. Sc., USA.  2018, 115, 6816-6821
  18. Combining SAMDI Mass Spectrometry and Peptide Arrays to Profile Phosphatase Activities. Szymczak, L.C., Huang, C.-F., Berns, E.J. and Mrksich, M., M.C., Methods in Enzymology, 2018, 607, in press. [PDF]
  19. Design of Glycosylation Sites by Rapid Synthesis and Analysis of Glycosyltransferases. Kightlinger, W., Lin, L., Rosztoczy, M., Li, W., DeLisa, M.P., Mrksich, M. and Jewett, M.C., Nat. Chem. Biol., 2018, 14, 627-635. [PDF]
  20. How Many Human Proteoforms are There? Kelleher, N.L., et al., Nat. Chem. Biol., 2018, 14, 206-214.
  21. Efficient Syntheses of Diverse, Medicinally Relevant Targets Planned by Computer and Executed in the Laboratory.  Klucznik, R., Mikulak, B., McCormack, M.P., Lima, H., Szymkuc, S., Bhowmick, M., Molga, K., Zhou, Y., Rickershauser, L., Gajewska, E.P., Toutchkine, A., Dittwald, P., Startek, M.P., Kirkovits, G.J., Roszak, R., Adamski, A., Sieredzinska, B., Mrksich, M., Trice, S.L.J. and Grzybowski, B.A.  Chem, 2018, 4, 522-532. [PDF]
  22. Peptide Arrays: Development and Application.  Szymczak, L.C., Kuo, H.-Y. and Mrksich, M., Anal. Chem., 2018, 90, 266-282 [PDF]
  23. Active Site Metal Identity Alters Histone Deacetylase 8 Substrate Selectivity: A Potential Novel Regulatory Mechanism.  Castaneda, C.A., Lopez, J.E., Joseph, C.G., Scholle, M.D., Mrksich, M. and Fierke, C.A., Biochemistry201756, in press.  [PDF]
  24. A Bottom-Up Proteomic Approach to Identify Substrate Specificity of Outer Membrane Protease OmpT. Wood, S.E., Sinsinbar, G.,Gudlur, S., Nallani, M., Huang, C.-F., Liedberg, B. and Mrksich, M.  Ang. Chem., 201756, in press. [PDF]
  25. Machine learning on Signal to Noise Ratio Improves Peptide Array Design in SAMDI Mass Spectrometry.  Xu, A., Szymczak, L., Mrksich, M. and Bagheri, N.  Anal. Chem., 201789, in press. [PDF]
  26. An Assay Based on SAMDI Mass Spectrometry for Profiling Protein Interaction Domains.  O’Kane, P. and Mrksich, M.  J. Am. Chem. Soc., 2017139, 10320-10327. [PDF]
  27. Peptide Delivery with Poly(Ethylene Glycol) Diacrylate Microneedles through Swelling Effect.  Liu, S., Xu, C., Yeo, D., Wiraja, C., Tey, H.L. and Mrksich, M. Bioeng. & Trans. Med., 20172, in press. [PDF]
  28. Nanopatterned Extracellular Matrices Enable Cell-Based Assays with a Mass Spectrometric Readout.  Cabezas, M., Mirkin, C.M. and Mrksich, M.  Nano Lett., 201717, 1373-1377. [PDF]
  29. Bifunctional Conjugates with Potent Inhibitory Activity Towards Cyclooxygenase and Histone Deacetylase.  Raji, Idris; Yadudu, Fatima; Janeira, Emily; Fathi, Shagayegh; Szymczak, Lindsey; Kornacki, James; Mrksich, Milan; Oyelere, Adegboyega.  Bioorg. & Med. Chem., 201725, 1202-1218.[PDF]
  30. Bisboronic Acids for Selective, Physiologically Relevant Direct Glucose Sensing with Surface-Enhanced Raman Spectroscopy.  Sharma, B, Bugga, P., Madison, L., Henry, A.I., Blaber, M., Greeneltch, N., Chiang, N., Mrksich, M., Schatz, G. Van Duyne, R.  J. Am. Chem. Soc., 2016138, 13952-13959.[PDF]
  31. Measuring Drug Metabolism Kinetics and Drug-Drug Interactions with SAMDI Mass Spectrometry.  Anderson, L., Berns, E., Bugga, P., George, A. and Mrksich, M.  Anal. Chem., 201688, 8604-8609.[PDF]
  32. Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks.  Peng, L., Modica, J.A., Howarth, A.J., Vargas, E., Moghadam, P.Z., Snurr, R.Z., Mrksich, M., Hupp, J.T. and Farha, O.K.  CHEM20161, 154-169. [PDF]
  33. Cellular Assays with a Molecular Endpoint Measured by SAMDI Mass Spectrometry.  Berns, E.J., Cabezas, M.D., and Mrksich, M.  Small201612, 3811-3818. [PDF]
  34. SIRT1 is a Critical Regulator of K562 Cell Growth, Survival, and Differentiation.  Duncan, M.T., DeLuca, T.A., Kuo, H.-Y., Yi, M., Mrksich, M. and Miller, W.M.  Exp. Cell Res.2016344, 40-52. [PDF]
  35. A Structure-Activity Relationship of Non-Peptide Macrocyclic Histone Deacetylase Inhibitors and Their Anti-Proliferative and Anti-Inflammatory Activities.  Tapadar, S., Fathi, S., Raji, I., Omesiete, W., Kornacki, J.R., Mwakwari, S.C., Miyata, M., Mitsutake, K., Li, J.D., Mrksich, M. and Oyelere, A.K.  Bioorg. Med. Chem.201523, 7543-7564. [PDF]
  36. Micropatterning Facilitates the Long-Term Growth and Analysis of iPSC-Derived Individual Human Neurons and Neuronal Networks.  Burbulla, L.F., Beaumont, K.G., Mrksich, M. and Krainc, D.  Advanced Healthcare Materials20165, 1894-1903. [PDF]
  37. SAMDI Mass Spectrometry–Enabled High–Throughput Optimization of a Traceless Petasis Reaction. Diagne, A.B., Li, S., Perkowski, G.A., Mrksich, M. and Thomson, R.J. ACS Combinatorial Chemistry.,2015 17, 658-662. [PDF]
  38. Discovery of SIRT3 Inhibitors Using SAMDI Mass Spectrometry. K. Patel, J. Sherrill, M. Mrksich and M.D. Scholle. J. Biomol. Screen., 2015 20, 842-848. [PDF]
  39. Design and Structure Activity Relationship of Tumor-Homing Histone Deacetylase Inhibitors Conjugated to Folic and Pteroic Acids. Q.H. Sodji, J.R. Kornacki, J.F. McDonald, M. Mrksich and A.K. Oyelere. Eur. J. Med. Chem., 2015 96, 340-359. [PDF]
  40. A Gene Expression-Based Comparison of Cell Adhesion to Extracellular Matrix and RGD-Terminated Monolayers. C.J. Sobers, S.E. Wood and M. Mrksich. Biomaterials, 201552, 385-394. [PDF]
  41. Acetyltransferase PCAF Regulates Crosstalk-Dependent Acetylation of Histone H3 by Distal Site Recognition. J.R. Kornacki, A.D. Stuparu and M. Mrksich. ACS Chemical Biology, 201510, 157-164[PDF]
  42. Structural, Kinetic and Proteomic Characterization of Acetyl Phosphate-Dependent Bacterial Protein Acetylation.  M.L. Kuhn, B. Zemaitaitis, L.I. Hu, A. Sahu, D. Sorensen, G. Minasov, B.P. Lima, M. Scholle, M. Mrksich, W.F. Anderson, B.W. Gibson, B. Schilling and A.J. Wolfe.  PLOS One2014 DOI: 10.1371/journal.pone.0094816[PDF]
  43. Combinatorial Screening of Mesenchymal Stem Cell Adhesion and Differentiation Using Polymer Pen Lithography.  M.D. Cabezas, D.J. Eichelsdoefer, K.A. Brown, M. Mrksich and C.A. Mirkin.  Methods in Cell Biology2014119, 261-276. [PDF]
  44. Self-Assembled Monolayer Facilitates Epithelial-Mesenchymal Interactions Mimicking Odontogenesis.  T. Muni, M. Mrksich and A. George.  Connective Tissue Res.2014, 55, 26-33[PDF]
  45. Phenotypic Differences in hiPSC NPCs Derived from Patients with Schizophrenia. K. Brennand, J.N. Savas, Y. Kim, N. Tran, A. Simone, K. Hashimoto-Torii, K.G. Beaumont, H.J. Kim, A. Topol, I. Ladran, M. Abdelrahim, B. Matikainen-Ankney, S. Chao, M. Mrksich, P. Rakic, G. Fang, B. Zhang, J.R. Yates III, F.H. Gage. Mol. Psych.2014, 1-8. [PDF]
  46. Geometric Control of Cytoskeletal Elements:  Impact on Vimentin Intermediate Filaments.  S.H. Shabbir, M.M. Cleland, R.D. Goldman and M. Mrksich.  Biomaterials2014, 35, 1359-1366[PDF]
  47. Synthesis and Structure-Activity Relationship of 3-Hydroxypyridine-2-thione-Based Histone Deactylase Inhibitors.  Q.H. Sodji, V. Patil, J.R. Kornacki, M. Mrksich and A.K. Oyelere.  J. Med. Chem.2013, 56, 9969-9981[PDF]
  48. Profiling Deacetylase Activities in Cell Lysates with Peptide Arrays and SAMDI Mass Spectrometry.  H.-Y. Kuo, T.A. DeLuca, W.M. Miller and M. Mrksich.  Anal. Chem.2013, 85, 10635-10642[PDF]
  49. Circadian Clock NAD+ Cycle Drives Mitochondrial Oxidative Metabolism in Mice.  C.B. Peek, A.H. Affinati, K.M. Ramsey, H.-Y. Kuo, J.M. Denu, W. Yu, N.S. Chandel, L.A. Sena, B. Marcheva, Y. Kobayashi, C. Omura, D. Levine, D. Gius, C.B. Newgard, E. Goetzman, M. Mrksich and J. Bass . Science2013, 342, 591. [PDF]
  50. Plectin-Containing, Centrally Localized Focal Adhesions Exert Traction Forces in Primary Lung Epithelial Cells. J. L. Eisenberg, K. G. Beaumont, D. Takawira, S. B. Hopkinson, M. Mrksich, G. R. S. Budinger, J. C. R. Jones. J. Cell. Sci. 2013126, 3746-3755. [PDF] + Cover Photo
  51. A Self-Adjuvanting Supramolecular Vaccine Carrying a Folded Protein Antigen. G.A. Hudalla, J.A. Modica, Y.F. Tian, J.S. Rudra, A.S. Chong, T. Sun, M. Mrksich and J.H. Collier. Adv. Healthcare Mater.20132, 1114-1119. [PDF]
  52. 3-Hydroxypyridin-2-thione as Novel Zinc Binding Group for Selective Histone Deacetylase Inhibition. V. Patil, Q.H. Sodji, J.R. Kornacki, M. Mrksich, and A.K. Oyelere. J. Med. Chem. 201356, 3492-3506. [PDF]
  53. Nanopatterned Substrates Increase Surface Sensitivity for Real-Time Biosensing. J.Y. Lin, A.D. Stuparu, M.D. Huntington, M. Mrksich and T. Odom. J. Phys. Chem. C. 2013117, 5286-5292. [PDF]
  54. Label-Assisted Mass Spectrometry to Accelerate Reaction Discovery. J.R. Cabrera-Pardo, D.I. Chai, S. Liu, M. Mrksich and S.A. Kozmin. Nat. Chem. 20135, 423-427.[PDF]
  55. Steady-State of an Enzymatic Reaction is Dependent on the Density of Reactant. S. Li, X. Liao, and M. Mrksich. Langmuir 201329, 294-298. [PDF]
  56. Modular Assembly of Protein Building Blocks to Create Precisely-Defined MegaMolecules. J.A. Modica, S. Skarpathiotis and M. Mrksich. ChemBioChem 201213, 2331-2334. [PDF]
  57. The Mechano-Stability of Isolated Focal Adhesions is Strongly Dependent on pH. K.G. Beaumont and M. Mrksich. Chem. & Biol. 201219, 711-720. [PDF]
  58. Cancer Prognostics by Direct Detection of p53-Antibodies on Gold Surfaces by Impedance Measurements. E. Prats-Alfonso, X. Sisquella, N. Zine, G. Gabriel, A. Guimerà, F. Javier del Campo, Rosa Villa, A. H. Eisenberg, M. Mrksich, A. Errachid, J. Aguiló and F Albericio. Small 20128, 1962-1969. [PDF]
  59. Directing Stem Cell Fate by Controlling the Affinity and Density of Ligand-Receptor Interactions at the Biomaterials Interface. K.A. Kilian and M. Mrksich. Ang. Chem. Int. Ed. 201251, 4891-4895. [PDF]
  60. Discovery of Glycosyltransferases Using Carbohydrate Arrays and Mass Spectrometry. L. Ban, N. Pettit, L. Li, A.D. Stuparu, L. Cai, W. Chen, W. Guan, P.W. Wang and M. Mrksich. Nat. Chem. Biol.20128, 769-773. [PDF]
  61. Three-Component Reaction Discovery Enabled by SAMDI Mass Spectrometry. T.J. Montavon, J. Li, J.R. Cabrera-Pardo, M. Mrksich and S.A. Kozmin. Nat. Chem. 20124, 45-51. [PDF]
  62. Stem Cell Differentiation—Multipotency Retained. M. Mrksich. Nat. Mater. 201110, 559-560. [PDF]
  63. Enzymatic Synthesis and Properties of Uridine-5´-O-(2-thiodiphospho)-N-acetylglucosamine. L. Cai, L. Ban, W.Y. Guan, M. Mrksich and P.W. Wang. Carbohydr. Res. 2011, 346, 1576-1580. [PDF]
  64. Combining Carbochips and Mass Spectrometry to Study the Donor Specificity for the Neisseria Meningitidis Beta 1,3-N-Acetylglucosaminyltransferase LgtA. W. Guan, L. Ban, L. Cai, L. Li, W. Chen, X. Liu, M. Mrksich, and P.G. Wang. Bioorg. & Med. Chem. Lett. 201121, 5025-5028. [PDF]
  65. The RGD and FEI Motifs in Nephronectin Bind to Different Sites in Integrin a8ß1. J. Sánchez-Cortés and M. Mrksich. ACS Chem. Biol. 20116, 1078-1086. [PDF]
  66. De Novo Motif for Kinase-Mediated Signaling Across the Cell Membrane. R.T. Petty and M. Mrksich. Integr. Biol. 20113 (8), 816-822.
  67. High-Throughput Screening of Small Molecule Libraries using SAMDI Mass Spectrometry. Z.A. Gurard-Levin, M.D. Scholle, A.H. Eisenberg and M. Mrksich. ACS Comb. Sci. 201113 (4), 347-350. [PDF]
  68. A Spatially Propagating Biochemical Reaction. X. Liao, R.T. Petty and M. Mrksich. Ang. Chem. Int. Ed.201150, 706-708. [PDF]
  69. Micropatterned Dynamically Adhesive Substrates for Cell Migration. S. Raghavan, R.A. Desai, Y. Kwon, M. Mrksich, C. S. Chen. Langmuir 201026, 17733-17738. [PDF]
  70. A Conformation- and Ion-Sensitive Plasmonic Biosensor. W. Hall, J. Modica, J. Anker, Y. Lin, M. Mrksich and R. Van Duyne. Nano Letters 201111, 1098-1105. [PDF]
  71. Rate Acceleration of an Interfacial Biochemical Reaction through Localization of Substrate and Enzyme by an Adaptor Domain. J. Li, S. Nayak and M. Mrksich. J. Phys. Chem. B 2010114, 15113-15118. [PDF]
  72. Non-Peptide Macrocyclic Histone Deacetylase Inhibitors Derived from Tricyclic Ketolide Skeleton. S.C. Mwakwari, W. Guerrant, V. Patil, S.I. Khan, B.L. Tekwani, Z.A. Gurard-Levin, M. Mrksich and A.K. Oyelere. J. Med. Chem. 201053, 6100-6111. [PDF]
  73. Peptide Arrays Identify Isoform-Selective Substrates for Profiling Endogenous Lysine Deacetylase Activity. Z. Gurard-Levin, K. Kilian, J. Kim, K. Bähr and M. Mrksich, Chem. Biol. 20105, 863-873. [PDF]
  74. An Inhibitor of a Cell Adhesion Receptor Stimulates Cell Migration. S. Shabbir, J.L. Eisenberg and M. Mrksich, Angew. Chem. Int. Ed. 201049, 7706 –7709. [PDF]
  75. Using the Angle-Dependent Resonances of Molded Plasmonic Crystals to Improve the Sensitivities of Biosensors. H. Gao, J.-C. Yang, J.Y. Lin, A. Stuparu, M. Hyung Lee, M. Mrksich, and T.W. Odom. NanoLetters 201010, 2549-2554.
  76. Cell Adhesion to Unnatural Ligands Mediated by a Bifunctional Protein. J. Sánchez-Cortés, K. Bähr, M. Mrksich, J. Am. Chem. Soc2010132, 9733-9737. [PDF]
  77. Geometric Cues for Directing the Differentiation of Mesenchymal Stem Cells. K.A. Kilian, B. Bugarija, B. Lahn and M. Mrksich, Proc. Natl. Acad. Sci. 2010107(11), 4872-4877. [PDF]
  78. Detection of Differentially Expressed Basal Cell Proteins by Mass Spectrometry. V. Todorovic, B.V. Desai, R.A. Eigenheer, T. Yin, E.V. Amargo, M. Mrksich, K.J. Green and M.J. Schroeder Patterson. Mol. & Cell. Proteomics 20109, 351-361.
  79. Using Self-Assembled Monolayers to Model Cell Adhesion to the 9th and 10th Type III Domains of Fibronectin. J.L. Eisenberg, J.L. Piper and M. Mrksich, Langmuir, 2009, 25, 13942-13951. [PDF]
  80. The Platelet Integrin aIIbß3 Binds to the RGD and AGD Motifs in Fibrinogen. J. Sánchez-Cortés and M. Mrksich, Chem. Biol. 200916, 990-1000. [PDF]
  81. An Adapter Domain-Mediated Autocatalytic Interfacial Kinase Reaction. X. Liao, J. Su and M. Mrksich, Chem. Eur. J. 200915, 12303-12309. [PDF]
  82. Profiling the Selectivity of DNA Linases with Mass Spectrometry. J. Kim and M. Mrksich, Nucleic Acis Research. 200938, 1-10. [PDF]
  83. Combining Mass Spectrometry and Peptide Arrays to Profile the Specificities of Histone Deacetylases. Z.A. Gurard-Levin, J. Kim and M. Mrksich, ChemBioChem 200910, 2159-2161. [PDF]
  84. Detection and Identification of Bioanalytes with High Resolution LSPR Spectroscopy and MALDI Mass Spectrometry. J.N. Anker, W.P. Hall, M.P. Lambert, P.T. Velasco, M. Mrksich, W.L. Klein and R.P. Van Duyne, J. Phys. Chem. B 2009113(15), 5891-5894. [PDF]
  85. Using Self-Assembled Monolayers to Model the Extracellular Matrix. M. Mrksich, Acta Biomaterialia20095, 832-841. [PDF]
  86. Biochemical Assays of Immobilized Oligonucleotides with Mass Spectrometry. H. Tsubery and M. Mrksich, Langmuir 200824(10), 5433-5438. [PDF]
  87. A Bio-mechanical Model for Coupling Cell Contractility with Focal Adhesion Formation. V.S. Deshpande, M. Mrksich, R.M. McMeeking and A.G. Evans, J. Mech. Phys. Solids 200856(18), 1484-1510. [PDF]
  88. A Calcium-Modulated Plasmonic Switch. W.P. Hall, J.N. Anker, Y. Lin, J. Modica, M. Mrksich and R. P. Van Dyne, J. Am. Chem. Soc. 2008130(18), 5836-5837. [PDF]
  89. Subcellular Curvature at the Perimeter of Micropatterned Cells Influences Lamellipodial Distribution and Cell Polarity. J. James, E.D. Goluch, H. Hu, C. Liu and M. Mrksich, Cell. Motil. Cyctoskel. 200865, 841-852. [PDF]
  90. Combining Self-Assembled Monolayers and Mass Spectrometry for Applications in Biochips. Z.A. Gurard-Levin and M. Mrksich, Annu. Rev. Anal. Chem. 20081, 767-800. [PDF]
  91. On-Chip Synthesis and Label-Free Assays of Oligosaccharide Arrays. L. Ban and M. Mrksich, Angew. Chem. Int. Ed. 200847(18), 3396-3399. [PDF]
  92. The Activity of HDAC8 Depends on Local and Distal Sequences of Its Peptide Substrates. Z.A. Gurard-Levin and M. Mrksich, Biochemistry 2008, 47(23), 6242-6250. [PDF]
  93. Mass Spectroscopy of Self-Assembled Monolayers: A New Tool for Molecular Surface Science. M. Mrksich, ACS Nano 20082(1), 7-18. [PDF]
  94. Functional Assays of Membrane-Bound Proteins with SAMDI-TOF Mass Spectrometry. V.L. Marin, T.H. Bayburt, S.G. Silgar and M. Mrksich, Angew. Chem. Int. Ed. 200746(46), 8796-8798. [PDF]
  95. Rapid Evaluation and Screening of Interfacial Reactions on Self-Assembled Monolayers. J. Li, P.S. Thiara and M. Mrksich, Langmuir 200723(23), 11826-11835. [PDF]
  96. Self-Assembled Monolayers for MALDI-TOF Mass Spectrometry for Immunoassays of Human Protein Antigens. S.M. Patrie and M. Mrksich, Anal. Chem. 200779(15), 5878-5887. [PDF]
  97. Attachement of Cells to Islands Presenting Gradients of Adhesion Ligands. R.T. Petty, H-W. Li, J.H. Maduram, R. Ismagilov and M. Mrksich, J. Am. Chem. Soc. 2007129(29), 8966-8967. [PDF]
  98. Model Systems: Mimics and Probes of Biological Systems. B.R. Peterson and M. Mrksich, Curr. Op. Chem. Bio. 2007, 11, 579-580. [PDF]
  99. Dynamic Hydrogels: Translating a Protein Conformational Change to Macroscopic Motion. W.L. Murphy, W.S. Dillmore, J. Modica and M. Mrksich, Angew. Chem.200746, 3066-3069. [PDF]
  100. Determination of Kinetic Parameters for Interfacial Enzymatic Reactions on Self-Assembled Monolayers. S. Nayak, W.S. Yeo and M. Mrksich, Langmuir 200723(10), 5578-5583. [PDF]
  101. Electroactive Self-Assembled Monolayers that Permit Orthogonal Control over the Adhesion of Cells to Patterned Substrates. W.S. Yeo and M. Mrksich, Langmuir 200622 (25), 10816-10820.[PDF]
  102. Assays of Endogenous Caspase Activities: A Comparison of Mass Spectrometry and Fluorescence Formats. J. Su, T. W. Rajapaksha, M. E. Peter and M. Mrksich, Anal. Chem. 200678 (14), 4945-4951. [PDF]
  103. Identification of Ligands with Bicyclic Scaffolds Provides Insights Into Mechanisms of Estrogen Receptor Subtype Selectivity. R. W. Hsieh, S. S. Rajan, S. K. Sharma, Y. Guo, E. R. DeSombre, M. Mrksich, and G. L. Greene, J. Biol. Chem. 2006281(26), 17909-17919. [PDF]
  104. Engineering a Biospecific Communication Pathway Between Cells and Electrodes. J. H. Collier and M. Mrksich, Proc. Natl. Acad. Sci. USA 2006103(7), 2021-2025. [PDF]
  105. Structural Basis for the Interaction of Bordetella pertussis Adenylyl Cyclase Toxin with Calmodulin. Q. Guo, Y. Shen, Y.S. Lee, C.S. Gibbs, M. Mrksich and W.J. Tang, EMBO J. 200524(18), 3190-3201. [PDF]
  106. Label-Free Detection of Protein-Protein Interactions on Biochips. W. S. Yeo, D. H. Min , R. W. Hsieh, G. L. Greene and M. Mrksich, Angew. Chem. Int. Ed. 200544(34), 5480-5483. [PDF]
  107. Combining Microfluidic Networks and Peptide Arrays for Multi-Enzyme Assays. J. Su, M. R. Bringer, R. F. Ismagilov and M. Mrksich, J. Am. Chem. Soc. 2005127(20), 7280-7281. [PDF]
  108. *Dynamic Substrates for Cell Biology.  M. Mrksich  MRS Bulletin200530, 180-184.
  109. A Substituent Effects Study Reveals the Kinetic Pathway for an Interfacial Diels-Alder Reaction. E. S. Gawalt and M. Mrksich, J. Am. Chem. Soc. 2004126(47), 15613-15617. [PDF]
  110. The Synergy Peptide PHSRN and the Adhesion Peptide RGD Mediate Cell Adhesion through a Common Mechanism. Y. Feng and M. Mrksich, Biochemistry 200443(50), 15811-15821. [PDF]
  111. Patterning Multiple Aligned Self-Assembled Monolayers Using Light. D. Ryan, B.A. Parviz, V. Linder, V. Semetey, J. Su, M. Mrksich and G.M. Whitesides, Langmuir 200420(21), 9080-9088. [PDF]
  112. Profiling Kinase Activities by Using a Peptide Chip and Mass Spectrometry. D.-H. Min, J. Su and M. Mrksich, Angew. Chem. Int. Ed. 200443(44), 5973-5977. [PDF]
  113. A Comparative Analysis of Localized and Propagating Surface Plasmon Resonance Sensors: The Binding of Concanavalin A to a Monosaccharide Functionalized Self-Assembled Monolayer. C.R. Yonzon, E. Jeoung, S. Zou, G.C. Schatz, M. Mrksich and R.P. Van Duyne, J. Am. Chem. Soc. 2004126(39), 12669-12676. [PDF]
  114. Peptide Arrays: Towards Routine Implementation. D.H. Min and M. Mrksich, Curr. Op. Chem. Biol.20048(5), 554-558. [PDF]
  115. Antibody Arrays Prepared by Cutinase-Mediated Immobilization on Self-Assembled Monolayers. Y. Kwon, Z. Han, E. Karatan, M. Mrksich and B.K. Kay, Anal. Chem. 200476(19), 5713-5720. [PDF]
  116. An Early Taste of Functional Glycomics. M. Mrksich, Chem. Biol. 200411(6) , 739-740. [PDF]
  117. Discovery of a Small Molecule that Inhibits the Interaction of Anthrax Adenylyl Cyclase Toxin Edema Factor with its Cellular Activator, Calmodulin. Y.-S. Lee, P. Bergson, W.S. He, M. Mrksich and W.-J. Tang, Chem. Biol. 200411, 1139-1146. [PDF]
  118. A Photochemical Method for Patterning the Immobilization of Ligands and Cells to Self-Assembled Monolayers. W. S. Dillmore, M. N. Yousaf and M. Mrksich, Langmuir 200420(17), 7223-7231. [PDF]
  119. Electroactive Substrates that Reveal Aldehyde Groups for Bio-Immobilization. W.S. Yeo and M. Mrksich, Adv. Mater. 200416, 1352-1356. [PDF]
  120. A Method for Connecting Solution Phase Enzyme Activity Assays with Immobilized Format Analysis by Mass Spectrometry. D.-H. Min, W.-S. Yeo and M. Mrksich, Anal. Chem. 200476(14) , 3923-3929. [PDF]
  121. Rewiring Cell Adhesion. M. Kato and M. Mrksich, J. Am. Chem. Soc. 2004126(21) , 6504-6505. [PDF]
  122. Chemical Screening by Mass Spectrometry to Identify Inhibitors of Anthrax Lethal Factor. D.-H. Min, W.-J. Tang and M. Mrksich, Nature Biotechnology 200422, 717-720. [PDF]
  123. Probing Protein-Carbohydrate Interactions with Microarrays of Synthetic Oligosaccharides. D.M. Ratner, E.W. Adams, J. Su, B.R. O’Keefe, M. Mrksich and P.H. Seeberger, ChemBioChem 20045 (3), 379-383. [PDF]
  124. Substrates for Cell Adhesion Prepared via Active Site-directed Immobilization of a Protein Domain. W. L. Murphy, K.O. Mercurius, S. Koide, M. Mrksich, Langmuir 200420 (4), 1026-1030. [PDF]
  125. Dynamic Interfaces Between Cells and Surfaces: Electroactive Substrates that Sequentially Release and Attach Cells. W.S. Yeo, M.N. Yousaf, M. Mrksich, J. Am. Chem. Soc. 2003125(49), 14994-14995. [PDF]
  126. Using Model Substrates To Study the Dependence of Focal Adhesion Formation on the Affinity of Integrin-Ligand Complexes . M. Kato, M. Mrksich, Biochemistry 200443(10), 2699 – 2707. [PDF]
  127. Using MALDI-TOF Mass Spectrometry to Characterize Interfacial Reactions on Self-Assembled Monolayers. J. Su and M. Mrksich, Langmuir 200319(12), 4867-4870. [PDF]
  128. Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough. S. Soelaiman, B.Q. Wei, P. Bergson, Y.S. Lee, Y. Shen, M. Mrksich, B.K. Shoichet, W.J. Tang, J. Biol. Chem. 2003278(28), 25990-25997. [PDF]
  129. Self-Assembled Monolayers That Transduce Enzymatic Activities to Electrical Signals. W.S. Yeo and M. Mrksich, Angew. Chem. Int. Ed. 200342(27), 3121-3124. [PDF]
  130. Nanopatterning the Chemospecific Immobilization of Cowpea Mosaic Virus Capsid. J. C. Smith, K.-B. Lee, Q. Wang, M. G. Finn, J. E. Johnson, M. Mrksich and C. A. Mirkin, Nano Lett. 20033(7), 883-886. [PDF]
  131. Electrochemical Desorption of Self-Assembled Monolayers Non-Invasively Releases Patterned Cells from Geometrical Confinements. X. Jiang, R. Ferrigno, M. Mrksich and G. M. Whitesides, J. Am. Chem. Soc. 2003125(9), 2366-2367. [PDF]
  132. Adsorption of Proteins to Hydrophobic Sites on Mixed Self-Assembled Monolayers. E. Ostuni, B. A. Grzybowski, M. Mrksich, C. S. Roberts and G. M. Whitesides, Langmuir 200319, 1861-1872. [PDF]
  133. Physiological calcium concentrations regulate calmodulin binding and catalysis of adenylyl cyclase exotoxins. Y .Shen, Y.S. Lee, S. Soelaiman, P. Bergson, D. Lu, A. Chen, K. Beckingham, Z. Grabarek, M. Mrksich, W.J. Tang, EMBO J. 200221(24), 6721-6732. [PDF]
  134. Maleimide-Functionalized Self-Assembled Monolayers for the Preparation of Peptide and Carbohydrate Biochips. B. T. Houseman, E. S. Gawalt and M. Mrksich, Langmuir 200319(5), 1522-1531. [PDF]
  135. Protein Chips: From Concept to Practice. Y.-S. Lee and M. Mrksich, Trends Biotechnol. 200220, S14-S18. [PDF]
  136. What Can Surface Chemistry do for Cell Biology?. M. Mrksich, Curr. Op. Chem. Biol. 20026, 794-797. [PDF]
  137. Using Mass Spectrometry to Characterize Self-Assembled Monolayers Presenting Peptides, Proteins and Carbohydrates. J. Su and M. Mrksich, Angew. Chem. Int. Ed. 200241, 4715-4718. [PDF]
  138. Selective Immobilization of Protein to Self-Assembled Monolayers Presenting Active Site Directed Capture Ligands. C. D. Hodneland, Y.-S. Lee, D.-H. Min and M. Mrksich, Proc. Natl. Acad. Sci. USA200299, 5048-5052. [PDF]
  139. Protein Nanoarrays Generated by Dip-Pen Nanolithography. K.-B. Lee, S.-J. Park, C. A. Mirkin, J. C. Smith and M. Mrksich, Science 2002295, 1702-1705. [PDF]
  140. Carbohydrate Arrays for the Evaluation of Protein Binding and Enzyme Activity. B. T. Houseman and M. Mrksich, Chem. Biol. 20029, 443-454. [PDF]
  141. Toward Quantitative Assays with Peptide Chips: A Surface Engineering Approach. B. T. Houseman and M. Mrksich, Trends Biotech. 2002, 20 (7), 279-281. [PDF]
  142. Dependence of the Rate of an Interfacial Diels-Alder Reaction on the Steric Environment of the Immobilized Dienophile: An Example of Enthalpy-Entropy Compensation. Y. Kwon and M. Mrksich, J. Am. Chem. Soc. 2002124, 806-812. [PDF]
  143. Peptide Chips for the Evaluation of Protein Kinase Activity. B. T. Houseman, J. H. Huh, S. J. Kron and M. Mrksich, Nature Biotech. 200220, 270-274. [PDF]
  144. Surface Molecular Recognition. N. S. Sampson, M. Mrksich and C. R. Bertozzi, Proc. Natl. Acad. Sci. USA 200198, 12870-12871. [PDF]
  145. Direct Cell Adhesion to the Angiopoietins Mediated by Integrins. T. R. Carlson, Y. Feng, P. C. Maisonpierre, G. D. Yancopoulos, M. Mrksich and A. O. Morla, J. Biol. Chem. 2001276, 26516-26525. [PDF]
  146. Using Electroactive Substrates to Pattern the Attachment of Two Different Cell Types. M. N. Yousaf, B. T. Houseman and M. Mrksich, Proc. Natl. Acad. Sci. USA 200198, 5992-5996. [PDF]
  147. Electroactive Monolayer Substrates that Selectively Release Adherent Cells. W.-S. Yeo, C. D. Hodneland and M. Mrksich, ChemBioChem 20017/8, 590-593. [PDF]
  148. Model Systems for Studying Polyvalent Carbohydrate Binding Interactions. B. T. Houseman and M. Mrksich in Host-Guest Chemistry, Topics in Current Chemistry 2002218, 1-44. [PDF]
  149. Streamlining the Drug Discovery Process by Integrating Miniaturization, High Throughput Screening, High Content Screening, and Automation on the CellChip^TM System. R. Kapur, K. A. Giuliano, M. Campana, T. Adams, K. Olson, D. Jung, M. Mrksich, C. Vasudevan and D. L. Taylor, Biomedical Microdevices 19992, 99-109. [PDF]
  150. Dynamic Substrates: Modulating the Behaviors of Attached Cells. M. N. Yousaf and M. Mrksich In New Technologies for Life Sciences: A Trends Guide, (Wilson, E. et al., eds: Elsevier), pp 28-35.
  151. Self-Assembled Monolayers of Alkanethiolates Presenting Mannitol Groups are Inert to Protein Adsorption and Cell Attachment. Y.-Y. Luk, M. Kato and M. Mrksich, Langmuir 200016, 9604-9608. [PDF]
  152. Turning on Cell Migration with Electroactive Substrates. M. N. Yousaf, B. T. Houseman and M. Mrksich, Angew. Chem. Int. Ed. 200140, 1093-1096. [PDF]
  153. Using Selective Withdrawal to Coat Micro Particles. I. Cohen, H. Li, J. L. Hougland, M. Mrksich and S. R. Nagel, Science 2001292, 265-267. [PDF]
  154. The Microenvironment of Immobilized Arg-Gly-Asp Peptides is an Important Determinant of Cell Adhesion. B. T. Houseman and M. Mrksich, Biomaterials 200122, 943-955. [PDF]
  155. Biomolecular Surfaces that Release Ligands Under Electrochemical Control. C. D. Hodneland and M. Mrksich, J. Am. Chem. Soc. 2000122, 4235-4236. [PDF]
  156. A Surface Chemistry Approach to Studying Cell Adhesion. M. Mrksich, Chem. Soc. Rev. 200029, 267-273. [PDF]
  157. Understanding the Role of Adsorption in the Reaction of Cyclopentadiene with an Immobilized Dienophile. E. W. L. Chan, M. N. Yousaf and M. Mrksich, J. Phys. Chem. A 2000104, 9315-9320. [PDF]
  158. Towards a Fibrous Composite with Dynamically Controlled Stiffness:  Lessons from Echinoderms.  J. A. Trotter, J. Tipper, G. Lyons-Levy, K. Chino, A. H. Heuer, Z. Liu, M. Mrksich, C. Hodneland, W. S. Dillmore, T. J. Koob, M. M. Koob-Emunds, K. Kadler and D. Holmes  Biotechnology of Extracellular Matrix,  200028, 357-362.
  159. The Kinetic Order of an Interfacial Diels-Alder Reaction Depends on the Microenvironment of an Immobilized Dienophile. M. N. Yousaf, E. W. L. Chan and M. Mrksich, Angew. Chem. Int. Ed. 200039, 1943-1946. [PDF]
  160. Geometric Control of Switching Between Growth, Apoptosis, and Differentiation During Angiogenesis Using Micropatterned Substrates. L. E. Dike, C. S. Chen, M. Mrksich, J. Tien, G. M. Whitesides and D. E. Ingber, In Vitro Cellular & Developmental Biology 199935, 441-448. [PDF]
  161. Catalytic Asymmetric Dihydroxylation by Gold Colloids Functionalized with Self-Assembled Monolayers. H. Li, Y.-Y. Luk and M. Mrksich, Langmuir 199915, 4957-4959. [PDF]
  162. Diels Alder Reaction for the Selective Immobilization of Protein to Electroactive Self-Assembled Monolayers. M. N. Yousaf and M. Mrksich, J. Am. Chem. Soc. 1999121, 4286-4287. [PDF]
  163. NMR Characterization of the Aliphatic b/b Pairing for Recognition of AT/TA Base Pairs in the Minor Groove of DNA. R. P. L. Clairac, C. J. Seel, B. H. Geierstanger, M. Mrksich, E. E. Baird, P. B. Dervan and D. E. Wemmer, J. Am. Chem. Soc. 1999121, 2956-2964. [PDF]
  164. The Role of Ligand Density in the Enzymatic Glycosylation of Carbohydrates Presented on Self-Assembled Monolayers of Alkanethiolates on Gold. B. T. Houseman and M. Mrksich, Angew. Chem. Int. Ed. 199938, 782-785. [PDF]
  165. An Efficient Solid-Phase Synthesis of Peptide-Substituted Alkanethiols for the Preparation of Substrates that Support Cell Adhesion. B. T. Houseman and M. Mrksich, J. Org. Chem. 1998, 63, 7552-7555. [PDF]
  166. The Effect of Surface Wettability on the Adsorption of Proteins and Detergents. G. S. Sigal, M. Mrksich and G. M. Whitesides, J. Am. Chem. Soc. 1998120, 3464-3473. [PDF]
  167. Micropatterned Surfaces for Control of Cell Shape, Position, and Function. C. S. Chen, M. Mrksich, S. Huang, G. M. Whitesides and D. E. Ingber, Biotech. Prog. 199814, 356-363. [PDF]
  168. Tailored Substrates for Studies of Attached Cell Culture. M. Mrksich, Cell. Mol. Life Sciences 199854, 653-662. [PDF]
  169. Using Mixed Self-Assembled Monolayers Presenting GRGD and (EG)3OH Groups to Characterize the Long-term Attachment of Bovine Capillary Endothelial Cells to Surfaces. C. Roberts, C. S. Chen, M. Mrksich, V. Martichonok, D. E. Ingber and G. M. Whitesides, J. Am. Chem. Soc. 1998120, 6548-6555. [PDF]
  170. Design of Self-Assembled Monolayers that Release Groups Using Applied Electrical Potentials. C. D. Hodneland and M. Mrksich, Langmuir 1997, 13, 6001-6003. [PDF]
  171. Using Self-Assembled Monolayers to Study the Interactions of Man-Made Materials with Proteins. M. V. Merritt, M. Mrksich and G. M. Whitesides Principles of Tissue Engineering, Edited by R. P. Lanza, R. Langer and W. Chick, R. G. Landes Company, Austin, 1997, 211-223.
  172. NMR Characterization of Hairpin Polyamide Complexes with the Minor Groove of DNA. R. P. L. de Clairac, B. H. Geierstanger, M. Mrksich, P. B. Dervan and D. E. Wemmer, J. Am. Chem. Soc. 1997119, 7909-7916. [PDF]
  173. On-Line Detection of Nonspecific Protein Adsorption at Artificial Surfaces. R. R. Seigel, P. Harder, R. Dahint, M. Grunze, F. Josse, M. Mrksich and G. M. Whitesides, Anal. Chem. 199769, 3321-3328. [PDF]
  174. Geometric Control of Cell Life and Death. C. S. Chen, M. Mrksich, S. Huang, G. M. Whitesides and D. E. Ingber, Science 1997276, 1345-1347. [PDF]
  175. Using Surface Plasmon Resonance Spectroscopy to Measure the Association of Detergents with Self-Assembled Monolayers of Hexadecanethiolate on Gold. G. B. Sigal, M. Mrksich and G. M. Whitesides, Langmuir 199713, 2749-2755. [PDF]
  176. Using Microcontact Printing to Pattern the Attachment of Mammalian Cells to Self-Assembled Monolayers of Alkanethiolates on Transparent Films of Gold and Silver. M. Mrksich, L. E. Dike, J. Y. Tien, D. E. Ingber and G. M. Whitesides, Exp. Cell Res. 1997235, 305-313. [PDF]
  177. Using Self-Assembled Monolayers that Present Oligo(ethylene glycol) Groups to Control the Interactions of Proteins with Surfaces. M. Mrksich and G. M. Whitesides. American Chemical Society Symposium Series on Chemistry and Biological Applications of Polyethylene Glycol 1997680, 361-373.
  178. Using Self-Assembled Monolayers to Understand the Biomaterials Interface. M. Mrksich, Curr. Op. Coll. & Interface Sci. 19972, 83-88. [PDF]
  179. Extension of Sequence-Specific Recognition in the Minor Groove of DNA by Pyrrole-Imidazole Polyamides to 9-13 Base Pairs. J. W. Trauger, E. E. Baird, M. Mrksich and P. B. Dervan, J. Am. Chem. Soc. 1996118, 6160-6166. [PDF]
  180. Controlling Cell Attachment on Contoured Surfaces with Self-Assembled Monolayers of Alkanethiolates on Gold. M. Mrksich, C. S. Chen, Y. Xia, L. E. Dike, D. E. Ingber and G. M. Whitesides, Proc. Natl. Acad. Sci. USA 199693, 10775-10778. [PDF]
  181. Self-Assembled Monolayers of Alkanethiolates Presenting Tri(propylenesulfoxide) Groups Resist the Adsorption of Protein. L. Deng, M. Mrksich and G. M. Whitesides, J. Am. Chem. Soc. 1996118, 5136-5137. [PDF]
  182. Affinity Capillary Electrophoresis: Using Capillary Electrophoresis to Study the Interactions of Proteins with Ligands. J. Gao, M. Mrksich, M. Mammen and G. M. in High Performance Capillary Electrophoresis: Theory, Techniques, and Applications, 146, Khaledi, M. G., Ed.; John Wiley & Sons, Inc., New York, 1998, 947-972.
  183. Microcontact Printing of Alkanethiols on Copper and Its Application in Microfabrication. Y. Xia, E. Kim, M. Mrksich and G. M. Whitesides, Chem. Mater. 19968, 601-603. [PDF]
  184. Extending the Recognition Site of Designed Minor Groove Binding Molecules. B. H. Geierstanger, M. Mrksich, P. B. Dervan and D. E. Wemmer, Nature Struct. Biol. 19963, 321-324. [PDF]
  185. Bio-Specific Adsorption of Carbonic Anhydrase to Self-Assembled Monolayers of Alkanethiolates That Present Benzenesulfonamide Groups on Gold. M. Mrksich, J. R. Grunwell and G. M. Whitesides, J. Am. Chem. Soc. 1995117, 12009-12010. [PDF]
  186. Using Self-Assembled Monolayers to Understand the Interactions of Man-Made Surfaces with Proteins and Cells. M. Mrksich and G. M. Whitesides, Ann. Rev. Biophys. Biomol. Struct. 199625, 55-78. [PDF]
  187. Surface Plasmon Resonance Permits In Situ Measurement of Protein Adsorption on Self-Assembled Monolayers of Alkanethiolates on Gold. M. Mrksich, G. S. Sigal and G. M. Whitesides, Langmuir 199511, 4383-4385. [PDF]
  188. Using Capillary Electrophoresis to Follow the Acetylation of the Amino Groups of Insulin and to Estimate their Basicities. J. Gao, M. Mrksich, F. A. Gomez and G. M. Whitesides, Anal. Chem. 199567, 3093-3100. [PDF]
  189. Patterned Self-Assembled Monolayers Formed by Microcontact Printing Direct Selective Metallization by Chemical Vapor Deposition on Planar and Non-Planar Substrates. N. L. Jeon, R. G. Nuzzo, Y. Xia, M. Mrksich and G. M. Whitesides, Langmuir 199511, 3024-3026. [PDF]
  190. Patterning Self-Assembled Monolayers Using Microcontact Printing: A New Technology for Biosensors? M. Mrksich and G. M. Whitesides, Trends in Biotechnology 199513, 228-235. [PDF]
  191. Patterning Siloxane Monolayers on the Surfaces of Silicon Dioxide with Microcontact Printing. Y. Xia, M. Mrksich, E. Kim and G. M. Whitesides, J. Am. Chem. Soc. 1995117, 9576-9577. [PDF]
  192. Design of a G•C-Specific DNA Minor Groove-Binding Peptide. B. H. Geierstanger, M. Mrksich, P. B. Dervan and D. E. Wemmer, Science 1994266, 646-650.
  193. Reversal of the Specificity of the Natural Product Distamycin By Designed Peptides. Recognition in the Minor Groove of DNA at 5′-(A,T)GCGC(A,T)-3′ Sites By ImPImP. M. Mrksich and P. B. Dervan, J. Am. Chem. Soc. 1995117, 3325-3332. [PDF]
  194. Hairpin Peptide-Turn-Peptide Motif. A New Class of Hexapeptides for Sequence-Specific Recognition in the Minor Groove of DNA. M. Mrksich, M. E. Parks and P. B. Dervan, J. Am. Chem. Soc. 1994116, 7983-7988. [PDF]
  195. Design of a Covalent Peptide Heterodimer for Sequence-Specific Recognition in the Minor Groove of Double-Helical DNA. M. Mrksich and P. B. Dervan, J. Am. Chem. Soc. 1994116, 3663-3664. [PDF]
  196. Structural and Dynamic Characterization of Heterodimeric and Homodimeric Complexes of Distamycin and 1-Methylimidazole-2-carboxamide-netropsin Bound to the Minor Groove. B. H. Geierstanger, J. P. Jacobsen, M. Mrksich, P. B. Dervan and D. E. Wemmer, Biochemistry 199433, 3055-3062. [PDF]
  197. Binding Affinities of Synthetic Peptides, Pyridine-2-carboxamide-netropsin and 1-Methylimidazole-2-carboxamide-netropsin, that Form 2:1 Complexes in the Minor Groove of Double-Helical DNA. W. S. Wade, M. Mrksich and P. B. Dervan, Biochemistry 199332, 11385-11389. [PDF]
  198. Structural Analysis of Covalent Peptide Dimers, Bis(Pyridine-2-carboxamide-netropsin)(CH2)3-6, in Complex with 5’-TGACT-3’ Sites by Two-Dimensional NMR. T. J. Dwyer, B. H. Geierstanger, M. Mrksich, P. B. Dervan and D. E. Wemmer, J. Am. Chem. Soc. 1993115, 9900-9906. [PDF]
  199. Enhanced Sequence-Specific Recognition in the Minor Groove of DNA by Covalent Peptide Dimers: Bis(Pyridine-2-carboxamide-netropsin)(CH2)3-6. M. Mrksich and P. B. Dervan, J. Am. Chem. Soc. 1993115, 9892-9899. [PDF]
  200. Antiparallel Side-by-Side Heterodimer for Sequence Specific Recognition in the Minor Groove of DNA by a Distamycin / 1-Methylimidazole-2-carboxamide-netropsin Pair. M. Mrksich and P. B. Dervan, J. Am. Chem. Soc. 1993115, 2572-2576. [PDF]
  201. Evidence That a Minor Groove-Binding Peptide and a Major Groove-Binding Protein Can Simultaneously Occupy a Common Site on DNA. M. G. Oakley, M. Mrksich and P. B. Dervan, Biochemistry 199231, 10969-10975. [PDF]
  202. Design of Peptides That Bind in the Minor Groove of DNA at 5′-(A,T)G(A,T)C(A,T)-3′ Sequences by a Dimeric Side-by-Side Motif. W. S. Wade, M. Mrksich and P. B. Dervan, J. Am. Chem. Soc. 1992114, 8783-8794. [PDF]
  203. Antiparallel Side-by-Side Dimeric Motif for Sequence-Specific Recognition in the Minor Groove of DNA by the Designed Peptide 1-Methylimidazole-2-carboxamide-netropsin. M. Mrksich, W. S. Wade, T. J. Dwyer, B. H. Geierstanger, D. E. Wemmer and P. B. Dervan, Proc. Natl. Acad. Sci. USA 199289, 7586-7590. [PDF]
  204. Highly Efficient Complexation of a p-Acceptor by a Molecular Tweezer Containing Two p-Donors: The Role of Preorganization. S. C. Zimmerman, M. Mrksich and M. Baloga, J. Am. Chem. Soc. 1989111, 8528-8530. [PDF]