Milan Mrksich
Northwestern University
Substrate (chemistry)BiophysicsSelf-assembled monolayerAdsorptionMass spectrometryNanotechnologyOrganic chemistryEnzymeChemistryExtracellular matrixMaterials scienceCombinatorial chemistryEthylene glycolPeptideDNABiochemistryMonolayerStereochemistryAdhesionCell adhesionBiologyCell biology
278Publications
92H-index
26.6kCitations
Publications 267
Newest
#1Shengwang Zhou (Jiangsu University)H-Index: 1
#2Peng He (U of C: University of Chicago)H-Index: 11
Last. Milan Mrksich (NU: Northwestern University)H-Index: 92
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This paper describes the synthesis, characterization, and modeling of a series of molecules having four protein domains attached to a central core. The molecules were assembled with the "megamolecule" strategy, wherein enzymes react with their covalent inhibitors that are substituted on a linker. Three linkers were synthesized, where each had four oligo(ethylene glycol)-based arms terminated in a para-nitrophenyl phosphonate group that is a covalent inhibitor for cutinase. This enzyme is a serin...
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#1Kevin J. Metcalf (NU: Northwestern University)H-Index: 5
#2Blaise R. Kimmel (NU: Northwestern University)H-Index: 1
Last. Milan Mrksich (NU: Northwestern University)H-Index: 92
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This paper presents a method to synthetically tune atomically precise megamolecule nanobody-enzyme conjugates for prodrug cancer therapy. Previous efforts to create heterobifunctional protein conjugates suffered from heterogeneity in domain stoichiometry, which in part led to the failure of antibody-enzyme conjugates in clinical trials. We used the megamolecule approach to synthesize anti-HER2 nanobody-cytosine deaminase conjugates with tunable numbers of nanobody and enzyme domains in a single,...
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#1Sarah Anderson (NU: Northwestern University)H-Index: 2
#2James E. Longbotham (UCSF: University of California, San Francisco)H-Index: 4
Last. Milan Mrksich (NU: Northwestern University)H-Index: 92
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Understanding the ligand preferences of epigenetic reader domains enables identification of modification states of chromatin with which these domains associate and can yield insight into recruitment and catalysis of chromatin-acting complexes. However, thorough exploration of the ligand preferences of reader domains is hindered by the limitations of traditional protein-ligand binding assays. Here, we evaluate the binding preferences of the PHD1 domain of histone demethylase KDM5A using the prote...
2 CitationsSource
#1Adam J. PluchinskyH-Index: 1
#2Daniel J. Wackelin (California Institute of Technology)H-Index: 1
Last. Milan MrksichH-Index: 92
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Advances in directed evolution have led to an exploration of new and important chemical transformations; however, many of these efforts still rely on the use of low-throughput chromatography-based screening methods. We present a high-throughput strategy for screening libraries of enzyme variants for improved activity. Unpurified reaction products are immobilized to a self-assembled monolayer and analyzed by mass spectrometry, allowing for direct evaluation of thousands of variants in under an ho...
1 CitationsSource
#1Barbara Mikulak-Klucznik (PAN: Polish Academy of Sciences)H-Index: 4
#2Patrycja Gołębiowska (PAN: Polish Academy of Sciences)H-Index: 1
Last. Bartosz A. Grzybowski (PAN: Polish Academy of Sciences)H-Index: 79
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Teaching computers to plan multistep organic syntheses has been a challenge for over 50 years1-7. Since early pioneering contributions, including programs such as LHASA1,7 (with reaction choices at each step made by human operator), the field has progressed greatly and there are now multiple software platforms6,8-13 capable of completely autonomous planning. Still, these programs 'think' only one step at a time and have so far been limited to relatively simple targets whose syntheses could, argu...
8 CitationsSource
#1Gaurav Sinsinbar (NTU: Nanyang Technological University)H-Index: 3
#2Sushanth Gudlur (NTU: Nanyang Technological University)H-Index: 2
Last. Bo Liedberg (NTU: Nanyang Technological University)H-Index: 71
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E. coli and Salmonella are two of the most common bacterial pathogens involved in food and water borne related deaths. Hence, it is critical to develop rapid and sensitive detection strategies for near outbreak applications. We report a simple and specific assay to detect as low as 1 CFU/mL of E. coli in water within 6 hours by targeting the bacteria's surface protease activity. The assay relies on polythiophene acetic acid (PTAA) as optical reporter and a short unlabeled peptide (LL37 FRRV ) pr...
1 CitationsSource
#1Justin A. Modica (NU: Northwestern University)H-Index: 6
#2Tsatsral Iderzorig (NU: Northwestern University)H-Index: 1
Last. Milan Mrksich (NU: Northwestern University)H-Index: 92
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This communication describes the design, synthesis and biological activity of a megamolecule mimic of an anti-HER2 antibody. The antibody mimic was prepared by linking two Fabs from the therapeutic...
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#1Kelly Parker (NU: Northwestern University)H-Index: 3
#2Shengwang Zhou (NU: Northwestern University)H-Index: 1
Last. Vinayak P. DravidH-Index: 107
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#1Prithvijit Mukherjee (NU: Northwestern University)H-Index: 2
#2Eric J. Berns (NU: Northwestern University)H-Index: 10
Last. Horacio D. Espinosa (NU: Northwestern University)H-Index: 75
view all 9 authors...
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#1Gaurav Sinsinbar (NTU: Nanyang Technological University)H-Index: 3
#2Sushanth Gudlur (NTU: Nanyang Technological University)H-Index: 2
Last. Bo Liedberg (NTU: Nanyang Technological University)H-Index: 71
view all 6 authors...
Outer membrane protease (OmpT) is a 33.5 kDa aspartyl protease that cleaves at dibasic sites and is thought to function as a defense mechanism for E. coli against cationic antimicrobial peptides secreted by the host immune system. Despite carrying three dibasic sites in its own sequence, there is no report of OmpT autoproteolysis in vivo. However, recombinant OmpT expressed in vitro as inclusion bodies has been reported to undergo autoproteolysis during the refolding step, thus resulting in an i...
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