Publications

Milan Mrksich Google Citations

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2024

  1. Megamolecule Self-Assembly Networks: A Combined Computational and Experimental Design Strategy. J. Wu, Z. Gu, J. A. Modica, S. Chen, M. Mrksich and G. A. Voth J. Am. Chem. Soc. 2024, 146, 44, 30553–30564. [PDF]
  2. HaloTag-Modified, Ferrocene Labeled Self-Assembled Monolayers for Protein Sensing. A. B. Brotherton, G. P. Neupane, X. Ji, K. Sullivan, M. D. Bailey E. J. Berns, J. Rivnay, M. Mrksich and T. J. Meade Langmuir, 2024, 40, 43, 22856–22864. [PDF]
  3. Synthesis and Activity of T-Cell Tumor-Directing MegaMolecules. S. Sridhar, J. A. Modica, D. J. Sykora, E. J. Berns and M. Mrksich  J. Am. Chem. Soc., 2024, 146, 26801-26807. [PDF]
  4. Using High-Throughput Experiments to Screen N-Glycosyltransferases with Altered Specificities. L. Lin, W. Knightlinger, K. Warfel, M.C. Jewett and M. Mrksich ACS Syn. Bio., 2024, 13(4), 1290-1302. [PDF]

2022

 
  1. Surface Potential Modulation as a Tool for Mitigating Challenges in SERS-based Microneedle Sensors. V. Brasiliense, J. E. Park, E. J. Berns, R. P. Van Duyne and M. Mrksich  Sci. Rep., 2022, 12, 15929. [PDF]
  2. Tyrosine Phosphatase Activity is Restricted by Basic Charge Substituting Mutation of Substrates. C.-F. Huang, C. J. Gottardi and M. Mrksich  Sci. Rep., 2022, 12, 15095.  [PDF]
  3. Scanning Transmission Electron Microscopy in a Scanning Electron Microscope for the High-Throughput Imaging of Biological Assemblies. K. A. Parker, S, Ribet, B. R. Kimmel, R. dos Reis, M. Mrksich and V. P. Dravid  Biomacromolecules, 2022, 23, 3235-3242. [PDF]
  4. Cell-free prototyping enables implementation of optimized reverse β-oxidation pathways in heterotrophic and autotrophic bacteria.  B. Vögeli, L. Schulz,  S. Garg, K. Tarasava, J. M. Clomburg, S. H. Lee, A. Gonnot, E. Hakim Moully, B. R. Kimmel, L. Tran, H. Zeleznik, S. D. Brown, S. D. Simpson, M. Mrksich, A. S. Karim, R. Gonzalez, M. Köpke and M. C. Jewett  Nat. Commun., 2022, 13, 3058.  [PDF]
  5. High-Throughput Microfluidics Platform for Intracellular Delivery and Sampling of Biomolecules from Live Cells.  C. A. Patino, P. Mukherjee, E. J. Berns, E. Hakim Moully, L. Stan, M. Mrksich and H. D. Espinosa  ACS Nano, 2022, 16, 7937–7946.  [PDF]
  6. Efficient Enzymatic Incorporation of Dehydroalanine Based on SAMDI-Assisted Identification of Optimized Tags for OspF/SpvC.  A. Yang, H. Tao, L. C. Szymczak, L. Lin, J. Song, Y. Wang, S. Bai, J. Modica, S.-Y. Huang, M. Mrksich, and X. Feng  ACS Chem. Biol., 2022, 17, 414–425. [PDF]
  7. Characterizing Enzyme Cooperativity with Imaging SAMDI-MS.  J. Grant, B. R. Kimmel, L. C. Szymczak, J. Roll and M. Mrksich  Chem. Eur. J., 2022, 28, e202103807.  [PDF]

2021

  1. Morphological features of single cells enable accurate automated classification of cancer from non-cancer cell lines. Z. Mousavikhamene, D. Sykora, M. Mrksich and N. Bagheri  Sci. Rep., 2021, 11, 24375 . [PDF]
  2. NADH inhibition of SIRT1 links energy state to transcription during time-restricted feeding.  D. C. Levine, H.-Y. Kuo, H.-K. Hong, J. Cedernaes, C. Hepler, A. G. Wright, M. A. Sommars, Y. Kobayashi, B. Marcheva, P. Gao, O. R. Ilkayeva, C. Omura, K. M. Ramsey, C. B. Newgard, G. D. Barish, C. B. Peek, N. S. Chandel, M. Mrksich and J. Bass  Nat. Metab., 2021, 3, 1621–1632. [PDF]
  3. Storing and Reading Information in Mixtures of Fluorescent Molecules.  A. A. Nagarkar, S. E. Root, M. J. Fink, A. S. Ten, B. J. Cafferty, D. S. Richardson, M. Mrksich, and G. M. Whitesides  ACS Cent. Sci., 2021, 7, 1728–1735.  [PDF]
  4. Development of an Enzyme-Inhibitor Reaction Using Cellular Retinoic Acid Binding Protein II for One-Pot Megamolecule Assembly. B. R. Kimmel and M. Mrksich  Chem. Eur. J. 2021, 27, 17843–17848.  [PDF]
  5. Synthesis, Characterization and Simulation of Four-Armed Megamolecules.  S. Zhou, P. He, S. Dhindwal, V. Grum-Tokars, Y. Li; K. Parker, J. Modica, R. Bleher, R. dos Reis, J. Zuchniarz, V. Dravid, G. Voth; B. Roux, M. Mrksich  Biomacromolecules, 2021, 22, 2363–2372.  [PDF]
  6. Exploring the Ligand Preferences of the PHD1 Domain of Histone Demethylase KDM5A Reveals Tolerance for Modifications of the Q5 Residue of Histone 3.  S. E. Anderson, J. E. Longbotham, P. T. O’Kane, F. S. Ugur, D. G. Fujimori and M. Mrksich  ACS Chem. Biol., 2021, 16, 205-213. [PDF]
  7. Synthetic Tuning of Domain Stoichiometry in Nanobody-Enzyme Megamolecules. K. J. Metcalf, B. R. Kimmel, D. J. Sykora, J. A. Modica, K. A. Parker, E. Berens, R. Dai, V. P. Dravid, Z. Werb and M. Mrksich  Bioconjugate Chem., 2021, 32, 143-152. [PDF]

2020

  1. High Throughput Screening with SAMDI Mass Spectrometry for Directed Evolution. A. J. Pluchinsky, D. W. Wackelin, X. Huang, F. H. Arnold, M. Mrksich  J. Am. Chem. Soc., 2020, 142, 19804-19808. [PDF]
  2. Computational Planning of the Synthesis of Complex Natural Products. B. Mikulak-Klucznik, P. Gołębiowska, A. Bayly, et al. Nature, 2020, 588, 83-88. [PDF]
  3. Design and Synthesis of Megamolecule Mimics of a Therapeutic Antibody. J. Modica, T. Iderzorig, and M. Mrksich  J. Am. Chem. Soc., 2020, 142, 13657-13661. [PDF]
  4. Outer Membrane Protease (OmpT)-based E. coli Sensing with Anionic Polythiophene and Unlabeled Peptide Substrate. G. Sinsinbar, S. Gudlur, S.E. Wood, G. Ammanath, H.U. Yildiz, P. Alagappan, M. Mrksich, and B. Liedberg  Angew. Chem. Int. Ed., 2020, 59, 2-12 [PDF] 
  5. Role of Lipopolysaccharide in Protecting OmpT from Autoproteolysis during In Vitro Refolding. G. Sinsinbar, S. Gudlur, K. Metcalf, M. Mrksich, M. Nallani, and B. Liedberg   Biomolecules, 2020, 10, 922. [PDF]
  6. A High-Throughput Photocapture Approach for Reaction Discovery.  A. A. Bayly, B. R. McDonald, K. A.  Scheidt and M. Mrksich  PNAS, 2020, 117, 13261-13266. [PDF]
  7. Temporal Sampling of Enzymes from Live Cells by Localized Electroporation and Quantification of Activity by SAMDI Mass Spectrometry.  P. Mukherjee, E. J. Berns, C. A. Patino, E. H. Moully, L. Chang, S. S. P. Nathamgari, J. A. Kessler, M. Mrksich and H. D. Espinosa  Small, 2020, 16, 2000584. [PDF]
  8. Solid-Phase Synthesis of Megamolecules.  B. R. Kimmel, J. A. Modica, K. Parker, V. Dravid and M. Mrksich  J. Am. Chem. Soc., 2020, 142, 4534-4538. [PDF]
  9. A High-Throughput SAMDI-Mass Spectrometry Assay for Isocitrate Dehydrogenase 1.  S. E. Anderson, N. S. Fahey, J. Park, P. T. O’Kane, C. A. Mirkin and M. Mrksich  Analyst, 2020, 145, 3899-3908. [PDF]
  10. Bump-and-Hole Engineering Identifies Specific Substrates of Glycosyltransferases in Living.  B. Schumann, S. Alyse Malaker, S. P. Wisnovsky, M. F. Debets, A. J. Agbay, D. Fernandez, L. J. S. Wagner, L. Lin, Z. Li, J. Choi, D. M. Fox, J. Peh, M. A. Gray, K. Pedram, J. J. Kohler, M. Mrksich and C. R. Bertozzi  Molecular Cell, 2020, 78, 824-834. [PDF]
  11. Sequential Glycosylation of Proteins with Substrate-Specific N-Glycosyltransferases.  L. Lin, W. Kightlinger, S. Prabhu, A. J. Hockenberry, C. Li, L.-X. Wang, M.C. Jewett and M. Mrksich  ACS Central Science, 2020, 6, 144-154. [PDF]
  12. High-Throughput Synthesis and Analysis of Intact Glycoproteins Using SAMDI-MS.  J.-M. Techner, W. Kightlinger, L. Liang, J. Herschewe, A. Ramesh, M. DeLisa, M. Jewett and M. Mrksich  Anal. Chem., 2020, 92, 1963-1971. [PDF]
  13. Using Peptide Arrays to Profile Phosphatase Activity in Cell Lysates. L. C. Szymczak, D. J. Sykora and M. Mrksich  Chem. Eur. J. 2020, 26, 165. [PDF]

2019

  1. Profiling Protein Tyrosine Phosphatase Specificity with Self-Assembled Monolayers for Matrix-Assisted Laser Desorption/ Ionization Mass Spectrometry and Peptide Arrays.  C.-F. Huang and M. Mrksich  ACS Comb. Sci., 2019, 21, 760-769. [PDF]
  2. Plasmonic Microneedle Arrays for in Situ Sensing with Surface-Enhanced Raman Spectroscopy (SERS).  J. E. Park, N. Yonet-Tanyeri, E. V. Ende, A.-I. Henry, B. E. Perez, M. Mrksich and R. P. Van Duyne  Nano Letters, 2019, 19, 6862-6868. [PDF]
  3. Label-Free Assay of Protein Tyrosine Phosphatase Activity in Single Cells.  E. H. Moully, E. Berns and M. Mrksich  Anal. Chem., 2019, 91, 13206-13212. [PDF]
  4. Subcellular Control Over Focal Adhesion Anisotropy, Independent of Cell Morphology, Dictates Stem Cell Fate.  M. D. Cabezas, B. Meckles, C. A. Mirkin and M. Mrksich  ACS Nano, 2019, 13, 11144-11152. [PDF]
  5. A Cell-Free Biosynthesis Platform for Modular Construction of Protein Glycosylation Pathways.  W. Kightlinger, K. E. Duncker, A. Ramesh, A. N. Thames, A. Natarajan, L. Lin, J. C. Stark, M. Mrksich, M. P. DeLisa and M. C. Jewett  Nat. Comm., 2019, 10, 5404-5416. [PDF]
  6. Profiling Protease Activity in Laundry Detergents with Peptide Arrays and SAMDI Mass Spectrometry.  R. Dai, A. Ten and M. Mrksich  Ind. & Eng. Chem. Res., 2019, 58, 10692-10697. [PDF]
  7. 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, 2019, 5, 911-916. [PDF] [Cover Photo]
  8. High-Throughput Mapping of CoA Metabolites by SAMDI-MS to Optimize the Cell-Free Biosynthesis of HMG-CoA.  P. O’Kane, Q. Dudley, A. McMillan, M. Jewett and M. Mrksich  Science Advances, 2019, 5, eaaw9180. [PDF]
  9. Sequential Photoactivation of Self-Assembled Monolayers to Direct Cell Adhesion and Migration. P. Bugga and M. Mrksich  Langmuir 2019, 35, 17, 5937-5943. [PDF]
  10. Using Peptide Arrays To Discover the Sequence-Specific Acetylation of the Histidine-Tyrosine Dyad.  L. Szymczak and M. Mrksich  Biochemistry, 2019, 58, 13, 1810-1817 [PDF]
  11. Using Microfluidics and Imaging SAMDI-MS to Characterize Reaction Kinetics. J. Grant, P.T. O’Kane, B.R. Kimmel and M. Mrksich   ACS Central Science, 2019, 5 (3), 486-493 [PDF]
  12. Exploration of the Nanomedicine-Design Space With Highthroughput Screening and Machine Learning.  G. Yamankurt, E. J. Berns, A. Xue, A. Lee, N. Bagheri, M. Mrksich and C. A. Mirkin  Nat. Biomed. Eng., 2019, 3, 318-327. [PDF]

2018

  1. 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]
  2. 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]
  3. High Throughput Enzyme Kinetics with 3D Microfluidics and Imaging SAMDI Mass Spectrometry.  J. Grant, S.H. Goudarzi and M. Mrksich  Anal. Chem., 2018, 90, 13096-13103. [PDF]
  4. Dynamic Substrates for Cell Biology.  P. Bugga and M. Mrksich  Curr. Op. Coll. & Inter. Sci., 2018, 38, 80-87.  [PDF]
  5. An Immobilized Enzyme Reactor for Spatiotemporal Control over Reaction Products. J. Grant, J. A. Modica, J. Roll, P. Perkovich  and M. Mrksich  Small, 2018, 14. [PDF]
  6. 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]
  7. An Unusual Salt Effect in an Interfacial Nucleophilic Substitution Reaction.  S. Li and M. Mrksich  Langmuir, 2018, 34, 6713-6718. [PDF]
  8. Traceless Immobilization of Analytes for High Throughput Experiments with SAMDI Mass Spectrometry.  K. Y. Helal, A. Alamgir, E. J. Berns and M. Mrksich  J. Am. Chem. Soc., 2018, 140, 8060-8063. [PDF] 
  9. Synthesis of Cyclic Megamolecules.  J.A Modica, Y. Lin and M. Mrksich   J. Am. Chem. Soc., 2018, 140, 6391-6399. [PDF]
  10. Potent Laminin-Inspired Antioxidant Regenerative Dressing Accelerates Wound Healing in Diabetes.  Y. X. Zhu, Z. Cankova, M. Iwanaszko, S. Lichtor, M. Mrksich and G. A. Ameer  Proc. Natl. Acad. Sc., USA., 2018, 115, 6816-6821. [PDF]
  11. Combining SAMDI Mass Spectrometry and Peptide Arrays to Profile Phosphatase Activities.  L. C. Szymczak, C.-F. Huang, E. J. Berns and M. Mrksich  Methods in Enzymology, 2018, 607, 389-403. [PDF]
  12. Design of Glycosylation Sites by Rapid Synthesis and Analysis of Glycosyltransferases. W. Kightlinger, L. Lin, M. Rosztoczy, W. Li, M.P. DeLisa, M. Mrksich and M.C. Jewett Nat. Chem. Biol., 2018, 14, 627-635. [PDF]
  13. How Many Human Proteoforms are There? N.L. Kelleher et al., Nat. Chem. Biol., 2018,14, 206-214. [PDF]
  14. Efficient Syntheses of Diverse, Medicinally Relevant Targets Planned by Computer and Executed in the Laboratory. R. Klucznik, B. Mikulak, M. P. McCormack, H. Lima, S. Szymkuc, M. Bhowmick, K. Molga, Y. Zhou, L. Rickershauser, E. P. Gajewska, A. Toutchkine, P. Dittwald, M. P. Startek, G. J. Kirkovits, R. Roszak, A. Adamski, B. Sieredzinska, M. Mrksich, S. L. J. Trice and B. A. Grzybowski  Chem, 2018, 4, 522-532. [PDF]
  15. Peptide Arrays: Development and Application.  L.C. Szymczak, H.-Y. Kuo and M. Mrksich  Anal. Chem., 2018, 90, 266-282 [PDF]

2017

  1. Active Site Metal Identity Alters HDAC8 Substrate Selectivity: A Potential Novel Regulatory Mechanism. C. A. Castaneda, J. E.  Lopez, C. G. Joseph, M. D. Scholle, M. Mrksich and C. A. Fierke  Biochemistry, 2017, 56, 5663-5670. PDF
  2. A Bottom-Up Proteomic Approach to Identify Substrate Specificity of Outer Membrane Protease OmpT.  S. E. Wood, G. Sinsinbar, S. Gudlur, M. Nallani, C.-F. Huang, B. Liedberg and M. Mrksich  Ang. Chem., 2017, 56, 16531-16535. [PDF] [Cover Photo]
  3. Machine Learning on Signal-to-Noise Ratios Improves Peptide Array Design in SAMDI Mass Spectrometry.  A. Xu, L. Szymczak, M. Mrksich and N. Bagheri  Anal. Chem., 2017, 89, 9039-9047. [PDF]
  4. An Assay Based on SAMDI Mass Spectrometry for Profiling Protein Interaction Domains. P. O’Kane and M. Mrksich  J. Am. Chem. Soc., 2017, 139, 10320-10327. [PDF]
  5. Peptide Delivery with Poly(Ethylene Glycol) Diacrylate Microneedles through Swelling Effect. S. Liu, C. Xu, D. C. Yeo, C. Wiraja, H. L. Tey, M. Mrksich and C. Xu   Bioeng. & Trans. Med., 2017, 2, 258-267. [PDF]
  6. Nanopatterned Extracellular Matrices Enable Cell-Based Assays with a Mass Spectrometric Readout.  M. Cabezas, C. M. Mirkin and M. Mrksich  Nano Lett., 2017, 17, 1373-1377. [PDF]
  7. Bifunctional Conjugates with Potent Inhibitory Activity Towards Cyclooxygenase and Histone Deacetylase.  I. Raji; F. Yadudu, E. Janeira, S. Fathi, L. Szymczak, J. Kornacki, M. Mrksich and A. Oyelere Bioorg. & Med. Chem., 2017, 25, 1202-1218. [PDF]

2016

  1. Measuring Drug Metabolism Kinetics and Drug-Drug Interactions with SAMDI Mass Spectrometry.  L. Anderson, E. Berns, P. Bugga, A. George and M. Mrksich   Anal. Chem., 2016, 88, 8604-8609. [PDF]
  2. Toward Design Rules for Enzyme Immobilization in Hierarchical Mesoporous Metal-Organic Frameworks.  L. Peng, J. A. Modica, A. J. Howarth, E. Vargas, P. Z. Moghadam, R. Z. Snurr, M. Mrksich, J. T. Hupp and O. K. Farha   CHEM, 2016, 1, 154-169. [PDF]
  3. Cellular Assays with a Molecular Endpoint Measured by SAMDI Mass Spectrometry.  E. J. Berns, M. D. Cabezas and M. Mrksich Small, 2016, 12, 3811-3818. [PDF] [Cover Photo]
  4. SIRT1 is a Critical Regulator of K562 Cell Growth, Survival, and Differentiation.  M. T. Duncan, T. A. DeLuca, H.-Y. Kuo, M. Yi, M. Mrksich and W. M. Miller  Exp. Cell Res., 2016,  344, 40-52. [PDF]
  5. Micropatterning Facilitates the Long-Term Growth and Analysis of iPSC-Derived Individual Human Neurons and Neuronal Networks. L. F. Burbulla, K. G. Beaumont, M. Mrksich and D. Krainc   Advanced Healthcare Materials,  2016,  5, 1894-1903. [PDF]

2015

  1. SAMDI Mass Spectrometry–Enabled High–Throughput Optimization of a Traceless Petasis Reaction. A. B. Diagne, S. Li, G. A. Perkowski, M. Mrksich and R. J. Thomson  ACS Combinatorial Chemistry, 2015, 17, 658-662.   [PDF]  [Cover Photo]
  2. 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]
  3. 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]
  4. 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,  2015, 52, 385-394. [PDF]
  5. A Structure-Activity Relationship of Non-Peptide Macrocyclic Histone Deacetylase Inhibitors and Their Anti-Proliferative and Anti-Inflammatory Activities. S. Tapadar, S. Fathi, I. Raji, W. Omesiete, J. R. Kornacki, S. C. Mwakwari, M. Miyata, K. Mitsutake, J. D. Li, M. Mrksich and A. K. Oyelere  Bioorg. Med. Chem., 2015, 23, 7543-7564. [PDF]
  6. Acetyltransferase p300/CBP Associated Factor (PCAF) Regulates Crosstalk-Dependent Acetylation of Histone H3 by Distal Site Recognition. J .R. Kornacki, A. D. Stuparu and M. Mrksich  ACS Chemical Biology,  2015,  10, 157-164. [PDF]

2014

  1. 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 One,  2014, 9, e94816. [PDF]
  2. 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 Biology,  2014,  119, 261-276. [PDF]
  3. Self-Assembled Monolayer Facilitates Epithelial-Mesenchymal Interactions Mimicking Odontogenesis.   T. Muni, M. Mrksich and A. George  Connective Tissue Res.,  2014,  55, 26-33. [PDF]
  4. 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]
  5. Geometric Control of Cytoskeletal Elements:   Impact on Vimentin Intermediate Filaments.  S.H. Shabbir, M.M. Cleland, R.D. Goldman and M. Mrksich  Biomaterials,  2014,  35, 1359-1366. [PDF]

2013

  1. 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]
  2. 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]
  3. 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   Science,  2013, 342, 591. [PDF]
  4. 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.,  2013, 126, 3746-3755.  [PDF]  [Cover Photo]
  5. 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., 2013, 2, 1114-1119. [PDF]
  6. 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., 2013, 56, 3492-3506. [PDF]
  7. 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., 2013, 117, 5286-5292. [PDF]
  8. Label-Assisted Mass Spectrometry for the Acceleration of Reaction Discovery and Optimization. J. R. Cabrera-Pardo, D.I. Chai, S. Liu, M. Mrksich and S. A. Kozmin  Nat. Chem.,  2013, 5, 423-427. [PDF]
  9. Steady-State of an Enzymatic Reaction is Dependent on the Density of Reactant. S. Li, X. Liao, and M. Mrksich  Langmuir, 2013, 29, 294-298. [PDF]

2012

  1. Modular Assembly of Protein Building Blocks to Create Precisely-Defined MegaMolecules. J. A. Modica, S. Skarpathiotis and M. Mrksich  ChemBioChem,  2012, 13, 2331-2334. [PDF]
  2. The Mechano-Stability of Isolated Focal Adhesions is Strongly Dependent on pH. K. G. Beaumont and M. Mrksic.  Chem. & Biol.,  2012, 19, 711-720. [PDF]
  3. Cancer Prognostics by Direct Detection of p53-Antibodies on Gold Surfaces by Impedance Measurements. E. Prats-Alfonso, X. Sisquella, N. Zine, G. Gabriel, A. Guimer, F. Javier del Campo, Rosa Villa, A. H. Eisenberg, M. Mrksich, A. Errachid, J. Aguiló and F Albericio  Small,  2012,  8, 1962-1969. [PDF] [Cover Photo]
  4. 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.,  2012,  51, 4891-4895. [PDF]
  5. 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.,  2012,  8, 769-773. [PDF]
  6. Three-Component Reaction Discovery Enabled by Mass Spectrometry of Self-Assembled Monolayers. T.J. Montavon, J. Li, J.R. Cabrera-Pardo, M. Mrksich and S.A. Kozmin.  Nat. Chem., 2012,  4, 45-51. [PDF]

2011

  1. Stem Cell Differentiation-Multipotency Retained. M. Mrksich  Nat. Mater.,  2011,  10, 559-560. [PDF]
  2. 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]
  3. 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.,  2011,  21, 5025-5028. [PDF]
  4. Using Self-Assembled Monolayers To Understand α8β1-Mediated Cell Adhesion to RGD and FEI Motifs in Nephronectin.   J. Sánchez-Cortés and M. Mrksich  ACS Chem. Biol., 2011, 6, 1078-1086. [PDF]
  5. De Novo Motif for Kinase-Mediated Signaling Across the Cell Membrane. R.T. Petty and M. Mrksich  Integr. Biol.,  2011, 3 (8), 816-822.  [PDF] [Cover Photo]
  6. 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.,  2011, 13 (4), 347-350. [PDF]
  7. A Spatially Propagating Biochemical Reaction. X. Liao, R.T. Petty and M. Mrksich  Ang. Chem. Int. Ed., 2011,  50, 706-708. [PDF]
  8. A Conformation- and Ion-Sensitive Plasmonic Biosensor. W. Hall, J. Modica, J. Anker, Y. Lin, M. Mrksich and R. Van Duyne  Nano Letters,  2011, 11, 1098-1105. [PDF]

2010

  1.   Profiling the Selectivity of DNA Ligases in an Array Format with Mass Spectrometry.   J. Kim and M. Mrksich  Nucleic Acids Research,  2010, 38, e2.  [PDF]
  2. Rate Enhancement 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., 2010, 114, 15113-15118.  [PDF]
  3. 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.,  2010,  53, 6100-6111.  [PDF]
  4. 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.,  2010, 5, 863-873.  [PDF]
  5. An Inhibitor of a Cell Adhesion Receptor Stimulates Cell Migration. S. Shabbir, J.L. Eisenberg and M. Mrksich  Angew. Chem. Int. Ed.,  2010, 49, 7706-7709.  [PDF]
  6. 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,  2010, 10, 2549-2554.  [PDF]
  7. Cell Adhesion to Unnatural Ligands Mediated by a Bifunctional Protein. J. Sánchez-Cortés, K. Bähr, M. Mrksich  J. Am. Chem. Soc., 2010, 132, 9733-9737.  [PDF]
  8. Geometric Cues for Directing the Differentiation of Mesenchymal Stem Cells. K.A. Kilian, B. Bugarija, B. Lahn and M. Mrksich Proc. Natl. Acad. Sci., 2010, 107(11), 4872-4877. [PDF]
  9. 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,  2010, 9, 351-361. [PDF]
  10. Micropatterned Dynamically Adhesive Substrates for Cell Migration. S. Raghavan, R.A. Desai, Y. Kwon, M. Mrksich, C. S. Chen Langmuir, 2010, 26, 17733-17738. [PDF]

2009

  1. 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]
  2. The Platelet Integrin αIIbβ3 Binds to the RGD and AGD Motifs in Fibrinogen. J. Sánchez-Cortés and M. Mrksich,  Chem. Biol.  2009,  16, 990-1000.  [PDF]
  3. An Adapter Domain-Mediated Autocatalytic Interfacial Kinase Reaction. X. Liao, J. Su and M. Mrksich,  Chem. Eur. J.  2009,  15, 12303-12309.  [PDF]
  4. Combining Mass Spectrometry and Peptide Arrays to Profile the Specificities of the Histone Deacetylases. Z.A. Gurard-Levin, J. Kim and M. Mrksich,  ChemBioChem  2009,  10, 2159-2161.  [PDF]
  5. 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  2009,  113(15), 5891-5894.  [PDF]
  6. Using Self-Assembled Monolayers to Model the Extracellular Matrix. M. Mrksich,  Acta Biomaterialia 2009,  5, 832-841.  [PDF]

2008

  1. Biochemical Assays of Immobilized Oligonucleotides with Mass Spectrometry. H. Tsubery and M. Mrksich, Langmuir 2008, 24(10), 5433-5438. [PDF]
  2. 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 2008, 56(18), 1484-1510. [PDF]
  3. 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. 2008, 130(18), 5836-5837. [PDF]
  4. 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. 2008, 65, 841-852. [PDF]
  5. Combining Self-Assembled Monolayers and Mass Spectrometry for Applications in Biochips. Z.A. Gurard-Levin and M. Mrksich, Annu. Rev. Anal. Chem. 2008, 1, 767-800. [PDF]
  6. On-Chip Synthesis and Label-Free Assays of Oligosaccharide Arrays. L. Ban and M. Mrksich, Angew. Chem. Int. Ed. 2008, 47(18), 3396-3399. [PDF]
  7. 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]
  8. Mass Spectroscopy of Self-Assembled Monolayers: A New Tool for Molecular Surface Science. M. Mrksich, ACS Nano 2008, 2(1), 7-18. [PDF]

2007

  1. 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.  2007,  46(46), 8796-8798.  [PDF]
  2. Rapid Evaluation and Screening of Interfacial Reactions on Self-Assembled Monolayers. J. Li, P.S. Thiara and M. Mrksich,  Langmuir  2007,  23(23), 11826-11835.  [PDF]
  3. Self-Assembled Monolayers for MALDI-TOF Mass Spectrometry for Immunoassays of Human Protein Antigens. S.M. Patrie and M. Mrksich,  Anal. Chem.  2007,  79(15), 5878-5887.  [PDF]
  4. Attachment 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.  2007,  129, 8966-8967. [PDF]
  5. Model Systems: Mimics and Probes of Biological Systems. B.R. Peterson and M. Mrksich,  Curr. Op. Chem. Bio.  2007, 11, 579-580.  [PDF]
  6. Dynamic Hydrogels: Translating a Protein Conformational Change to Macroscopic Motion. W.L. Murphy, W.S. Dillmore, J. Modica and M. Mrksich,  Angew. Chem.,  2007,  46, 3066-3069.  [PDF]
  7. Determination of Kinetic Parameters for Interfacial Enzymatic Reactions on Self-Assembled Monolayers. S. Nayak, W.S. Yeo and M. Mrksich,  Langmuir  2007,  23(10), 5578-5583.  [PDF]

2006

  1. Electroactive Self-Assembled Monolayers that Permit Orthogonal Control over the Adhesion of Cells to Patterned Substrates. W.S. Yeo and M. Mrksich,  Langmuir  2006,  22 (25), 10816-10820.  [PDF]
  2. 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.  2006,  78 (14), 4945-4951.  [PDF]
  3. 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.  2006,  281(26), 17909-17919.    [PDF]
  4. Engineering a Biospecific Communication Pathway Between Cells and Electrodes. J. H. Collier and M. Mrksich,  Proc. Natl. Acad. Sci. USA  2006,  103(7), 2021-2025.  [PDF]

2005

  1. 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. 2005, 24(18), 3190-3201.  [PDF]
  2. 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.  2005,  44(34), 5480-5483.  [PDF]
  3. 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.  2005,  127(20), 7280-7281.  [PDF]
  4. Dynamic Substrates for Cell Biology.  M. Mrksich  MRS Bulletin, 2005, 30, 180-184.  [PDF]

2004

  1. Using Model Substrates To Study the Dependence of Focal Adhesion Formation on the Affinity of Integrin-Ligand Complexes . M. Kato, M. Mrksich,  Biochemistry  2004,  43(10), 2699-2707.  [PDF]
  2. A Substituent Effects Study Reveals the Kinetic Pathway for an Interfacial Reaction. E. S. Gawalt and M. Mrksich,  J. Am. Chem. Soc.  2004,  126(47), 15613-15617.  [PDF]
  3. The Synergy Peptide PHSRN and the Adhesion Peptide RGD Mediate Cell Adhesion through a Common Mechanism. Y. Feng and M. Mrksich,  Biochemistry  2004,  43(50), 15811-15821.  [PDF]
  4. 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  2004,  20(21), 9080-9088.  [PDF]
  5. Profiling Kinase Activities by Using a Peptide Chip and Mass Spectrometry. D.-H. Min, J. Su and M. Mrksich,  Angew. Chem. Int. Ed.  2004,  43(44), 5973-5977.  [PDF]
  6. 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.  2004,  126(39), 12669-12676.  [PDF]
  7. Peptide Arrays: Towards Routine Implementation. D.H. Min and M. Mrksich,  Curr. Op. Chem. Biol.2004,  8(5), 554-558.  [PDF]
  8. 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.  2004,  76(19), 5713-5720.  [PDF]
  9. An Early Taste of Functional Glycomics. M. Mrksich,  Chem. Biol.  2004,  11(6)  , 739-740.  [PDF]
  10. 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.  2004,  11, 1139-1146.  [PDF]
  11. 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  2004,  20(17), 7223-7231.  [PDF]
  12. Electroactive Substrates that Reveal Aldehyde Groups for Bio-Immobilization. W.S. Yeo and M. Mrksich,  Adv. Mater.  2004,  16, 1352-1356.  [PDF]
  13. 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.  2004,  76(14), 3923-3929.  [PDF]
  14. Rewiring Cell Adhesion. M. Kato and M. Mrksich,  J. Am. Chem. Soc.  2004,  126(21), 6504-6505.  [PDF]
  15. Chemical Screening by Mass Spectrometry to Identify Inhibitors of Anthrax Lethal Factor. D.-H. Min, W.-J. Tang and M. Mrksich,  Nature Biotechnology  2004,  22, 717-720.  [PDF]
  16. 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  2004, 5, 379-383.  [PDF]
  17. 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  2004,  20 (4), 1026-1030.  [PDF]

2003

  1. 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.  2003,  125(49), 14994-14995.  [PDF]
  2. Using MALDI-TOF Mass Spectrometry to Characterize Interfacial Reactions on Self-Assembled Monolayers. J. Su and M. Mrksich,  Langmuir  2003,  19(12), 4867-4870.  [PDF]
  3. 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.  2003,  278(28), 25990-25997.  [PDF]
  4. Self-Assembled Monolayers That Transduce Enzymatic Activities to Electrical Signals. W.S. Yeo and M. Mrksich,  Angew. Chem. Int. Ed.  2003,  42(27), 3121-3124.  [PDF]
  5. 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.  2003,  3(7), 883-886.  [PDF]
  6. 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.  2003,  125(9), 2366-2367.  [PDF]
  7. 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  2003,  19, 1861-1872.  [PDF]
  8. Maleimide-Functionalized Self-Assembled Monolayers for the Preparation of Peptide and Carbohydrate Biochips. B. T. Houseman, E. S. Gawalt and M. Mrksich,  Langmuir  2003,  19(5), 1522-1531.  [PDF]

2002

  1. Protein Chips: From Concept to Practice. Y.-S. Lee and M. Mrksich,  Trends Biotechnol.  2002,  20, S14-S18.  [PDF]
  2. What Can Surface Chemistry do for Cell Biology? M. Mrksich,  Curr. Op. Chem. Biol.  2002,  6, 794-797.  [PDF]
  3. Using Mass Spectrometry to Characterize Self-Assembled Monolayers Presenting Peptides, Proteins and Carbohydrates. J. Su and M. Mrksich,  Angew. Chem. Int. Ed.  2002,  41, 4715-4718.  [PDF]
  4. 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. USA,  2002,  99, 5048-5052.  [PDF]
  5. Protein Nanoarrays Generated by Dip-Pen Nanolithography. K.-B. Lee, S.-J. Park, C. A. Mirkin, J. C. Smith and M. Mrksich,  Science  2002,  295, 1702-1705.  [PDF]
  6. Carbohydrate Arrays for the Evaluation of Protein Binding and Enzyme Activity. B. T. Houseman and M. Mrksich,  Chem. Biol.  2002,  9, 443-454.  [PDF]
  7. Toward Quantitative Assays with Peptide Chips: A Surface Engineering Approach. B. T. Houseman and M. Mrksich,  Trends Biotech.  2002,  20 (7), 279-281.  [PDF]
  8. 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.  2002,  124, 806-812.  [PDF]
  9. Peptide Chips for the Evaluation of Protein Kinase Activity. B. T. Houseman, J. H. Huh, S. J. Kron and M. Mrksich,  Nature Biotech.  2002,  20, 270-274.  [PDF]
  10. Model Systems for Studying Polyvalent Carbohydrate Binding Interactions. B. T. Houseman and M. Mrksich in Host-Guest Chemistry, Topics in Current Chemistry  2002,  218, 1-44.  [PDF]
  11. 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.  2002,  21(24), 6721-6732.  [PDF]

2001

  1. Surface Molecular Recognition. N. S. Sampson, M. Mrksich and C. R. Bertozzi,  Proc. Natl. Acad. Sci. USA  2001,  98, 12870-12871.  [PDF]
  2. 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.  2001,  276, 26516-26525.  [PDF]
  3. Using Electroactive Substrates to Pattern the Attachment of Two Different Cell Populations. M. N. Yousaf, B. T. Houseman and M. Mrksich,  Proc. Natl. Acad. Sci. USA  2001,  98, 5992-5996.  [PDF]
  4. Electroactive Monolayer Substrates that Selectively Release Adherent Cells. W.-S. Yeo, C. D. Hodneland and M. Mrksich,  ChemBioChem  2001,  7/8, 590-593.  [PDF]
  5. Turning on Cell Migration with Electroactive Substrates. M. N. Yousaf, B. T. Houseman and M. Mrksich,  Angew. Chem. Int. Ed.  2001,  40, 1093-1096.  [PDF]
  6. Using Selective Withdrawal to Coat Micro Particles. I. Cohen, H. Li, J. L. Hougland, M. Mrksich and S. R. Nagel,  Science  2001,  292, 265-267.  [PDF]
  7. The Microenvironment of Immobilized Arg-Gly-Asp Peptides is an Important Determinant of Cell Adhesion.   B. T. Houseman and M. Mrksich  Biomaterials,  2001,  22, 943-955.  [PDF]

2000

  1. 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),  2000,  pp 28-35.  [PDF]
  2. 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  2000,  16, 9604-9608.  [PDF]
  3. Biomolecular Surfaces that Release Ligands Under Electrochemical Control. C. D. Hodneland and M. Mrksich,  J. Am. Chem. Soc.  2000,  122, 4235-4236.  [PDF]
  4. A Surface Chemistry Approach to Studying Cell Adhesion.   M. Mrksich    Chem. Soc. Rev.,  2000,  29, 267-273.  [PDF]
  5. 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  2000,  104, 9315-9320.  [PDF]
  6. 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,    2000,  28, 357-362.    [PDF]
  7. 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.  2000,  39, 1943-1946.  [PDF]

1999

  1. 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,  1999, 35, 441-448.  [PDF]
  2. Catalytic Asymmetric Dihydroxylation by Gold Colloids Functionalized with Self-Assembled Monolayers. H. Li, Y.-Y. Luk and M. Mrksich  Langmuir,  1999, 15, 4957-4959.  [PDF]
  3. Diels Alder Reaction for the Selective Immobilization of Protein to Electroactive Self-Assembled Monolayers. M. N. Yousaf and M. Mrksich  J. Am. Chem. Soc.,  1999, 121, 4286-4287.  [PDF]
  4. 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., 1999, 121, 2956-2964.  [PDF]
  5. 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.,  1999,  38, 782-785.  [PDF]
  6. Streamlining the Drug Discovery Process by Integrating Miniaturization, High Throughput Screening, High Content Screening, and Automation on the CellChip™ System. R. Kapur, K. A. Giuliano, M. Campana, T. Adams, K. Olson, D. Jung, M. Mrksich, C. Vasudevan and D. L. Taylor  Biomedical Microdevices, 1999,  2, 99-109. [PDF]

1998

  1. An Efficient Solid-Phase Synthesis of Peptide-Substituted Alkanethiols for the Preparation of Substrates that Support Adhesion of Cells.   B. T. Houseman and M. Mrksich  J. Org. Chem.,  1998,  63, 7552-7555.  [PDF]
  2. 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.,  1998,  120, 3464-3473.  [PDF]
  3. 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.,  1998,  14, 356-363.  [PDF]
  4. Tailored Substrates for Studies of Attached Cell Culture. M. Mrksich  Cell. Mol. Life Sciences,  1998,  54, 653-662.  [PDF]
  5. 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.,  1998,  120, 6548-6555.  [PDF]

1997

  1. Design of Self-Assembled Monolayers that Release Groups Using Applied Electrical Potentials. C. D. Hodneland and M. Mrksich  Langmuir,  1997,  13, 6001-6003.  [PDF]
  2. Using Self-Assembled Monolayers to Understand the Interactions of Man-Made Materials with Proteins. M. V. Merritt, M. Mrksich and G. M. Whitesides  Principles of Tissue Engineering, 1997, 2, 211-223.  [PDF]
  3. 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.,  1997,  119, 7909-7916.  [PDF]
  4. 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.,  1997,  69, 3321-3328.  [PDF]
  5. Geometric Control of Cell Life and Death. C. S. Chen, M. Mrksich, S. Huang, G. M. Whitesides and D. E. Ingber  Science,  1997,  276, 1345-1347.  [PDF]
  6. 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,  1997,  13, 2749-2755.  [PDF]
  7. 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.,  1997,  235, 305-313.  [PDF]
  8. 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,  1997,  680, 361-373.  [PDF]
  9. Using Self-Assembled Monolayers to Understand the Biomaterials Interface. M. Mrksich  Curr. Op. Coll. & Interface Sci.,  1997,  2, 83-88.  [PDF]

1996

  1. 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.,  1996,  118, 6160-6166.  [PDF]
  2. 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,  1996,  93, 10775-10778.  [PDF]
  3. 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.,  1996,  118, 5136-5137.  [PDF]
  4. Affinity Capillary Electrophoresis: Using Capillary Electrophoresis to Study the Interactions of Proteins with Ligands. J. Gao, M. Mrksich, M. Mammen and G. M. Whitesides  High Performance Capillary Electrophoresis: Theory, Techniques, and Applications, 1998, 146,  947-972.  [PDF]
  5. Microcontact Printing of Alkanethiols on Copper and Its Application in Microfabrication. Y. Xia, E. Kim, M. Mrksich and G. M. Whitesides  Chem. Mater.,  1996,  8, 601-603.  [PDF]
  6. 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.,  1996,  3, 321-324.  [PDF]
  7. 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.,  1996,  25, 55-78.  [PDF]

1995

  1. 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.,  1995,  117, 12009-12010.  [PDF]
  2. 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,  1995,  11, 4383-4385.  [PDF]
  3. 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.,  1995,  67, 3093-3100.  [PDF]
  4. 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,  1995,  11, 3024-3026.  [PDF]
  5. Patterning Self-Assembled Monolayers Using Microcontact Printing: A New Technology for Biosensors? M. Mrksich and G. M. Whitesides  Trends in Biotechnology,  1995,  13, 228-235.  [PDF]
  6. Microcontact Printing of Octadecylsiloxane on the Surface of Silicon Dioxide and Its Application in Microfabrication.  Y. Xia, M. Mrksich, E. Kim and G. M. Whitesides  J. Am. Chem. Soc.,  1995,  117, 9576-9577.  [PDF]
  7. Recognition in the Minor Groove of DNA at 5′-(A,T)GCGC(A,T)-3′ by a Four Ring Tripeptide Dimer. Reversal of the Specificity of the Natural Product Distamycin.   M. Mrksich and P. B. Dervan  J. Am. Chem. Soc.,  1995,  117, 3325-3332.  [PDF]

1994

  1. Design of a G•C-Specific DNA Minor Groove-Binding Peptide.   B. H. Geierstanger, M. Mrksich, P. B. Dervan and D. E. Wemmer    Science,  1994,  266, 646-650.  [PDF]
  2. Hairpin Peptide Motif. A New Class of Oligopeptides for Sequence-Specific Recognition in the Minor Groove of Double-Helical DNA.   M. Mrksich, M. E. Parks and P. B. Dervan  J. Am. Chem. Soc.,  1994,  116, 7983-7988.  [PDF]
  3. 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.,  1994,  116, 3663-3664.  [PDF]
  4. 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, 1994,  33, 3055-3062.  [PDF]

1993

  1. 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,  1993,  32, 11385-11389.  [PDF]
  2. 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.,  1993,  115, 9900-9906.  [PDF]
  3. 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.,  1993,  115, 9892-9899.  [PDF]
  4. 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.,  1993,  115, 2572-2576.  [PDF]

1992

  1. 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,  1992,  31, 10969-10975.  [PDF]
  2. 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.,  1992,  114, 8783-8794.  [PDF]
  3. 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,  1992,  89, 7586-7590.  [PDF]

1989

  1. Highly Efficient Complexation of a Π-Acceptor by a Molecular Tweezer Containing Two Π-Donors: The Role of Preorganization. S. C. Zimmerman, M. Mrksich and M. Baloga  J. Am. Chem. Soc.,  1989, 111, 8528-8530. [PDF]