about
Environmental changes bridge evolutionary valleysIn vitro recombination of non-homologous genes can result in gene fusions that confer a switching phenotype to cellsStructure prediction of domain insertion proteins from structures of individual domains.Shifting Fitness and Epistatic Landscapes Reflect Trade-offs along an Evolutionary Pathway.Synthetic gene libraries: in search of the optimal diversity.Rapid generation of incremental truncation libraries for protein engineering using alpha-phosphothioate nucleotides.Creation of an allosteric enzyme by domain insertion.Theoretical distribution of truncation lengths in incremental truncation libraries.Mathematical expressions useful in the construction, description and evaluation of protein libraries.Directed evolution of protein switches and their application to the creation of ligand-binding proteins.Beyond cataloging the Library of Babel.Sites in the AAV5 capsid tolerant to deletions and tandem duplications.A comprehensive, high-resolution map of a gene's fitness landscapeHeterodimeric DNA methyltransferases as a platform for creating designer zinc finger methyltransferases for targeted DNA methylation in cells.Design and synthesis of a beta-lactamase activated 5-fluorouracil prodrug.Protein switch engineering by domain insertion.Circular permutation in the Ω-loop of TEM-1 β-lactamase results in improved activity and altered substrate specificityPFunkel: efficient, expansive, user-defined mutagenesis.Directed evolution of improved zinc finger methyltransferases.A protein therapeutic modality founded on molecular regulation.Advancements in the development of HIF-1α-activated protein switches for use in enzyme prodrug therapy.Rational design of a fusion protein to exhibit disulfide-mediated logic gate behavior.A hot-spot motif characterizes the interface between a designed ankyrin-repeat protein and its target ligand.Insertion of a xylanase in xylose binding protein results in a xylose-stimulated xylanase.A xylose-stimulated xylanase-xylose binding protein chimera created by random nonhomologous recombination.A Positive Selection for Nucleoside Kinases in E. coliInsightful directed evolution of Escherichia coli quorum sensing promoter region of the lsrACDBFG operon: a tool for synthetic biology systems and protein expressionDevelopment of a cancer-marker activated enzymatic switch from the herpes simplex virus thymidine kinase.Construction of Protein Switches by Domain Insertion and Directed Evolution.Design of protein switches based on an ensemble model of allosteryElectrochemical activation of engineered protein switches.An externally tunable bacterial band-pass filter.Modulation of effector affinity by hinge region mutations also modulates switching activity in an engineered allosteric TEM1 beta-lactamase switch.The interplay between effector binding and allostery in an engineered protein switch.Targeted DNA methylation in human cells using engineered dCas9-methyltransferases.Enzymatic protein switches built from paralogous input domains.Characterization of monobody scaffold interactions with ligand via force spectroscopy and steered molecular dynamics.An engineered split M.HhaI-zinc finger fusion lacks the intended methyltransferase specificity.The thymidylate kinase genes from Mycobacterium tuberculosis and methicillin-resistant Staphylococcus aureus confer 3'-azido-3'-deoxythymidine resistance to Escherichia coli.NMR characterization of an engineered domain fusion between maltose binding protein and TEM1 beta-lactamase provides insight into its structure and allosteric mechanism.
P50
Q28272911-C20E3F70-6146-4EE7-BC80-96F373E8666CQ28742847-16478C60-4287-4080-9D90-33BE393A66EDQ30368737-D5CFEB6D-C2B1-48E5-A99B-F9A3FF9058BCQ30388039-7366ACE9-7177-4546-9A64-DA7264F0D925Q30943778-2458A13C-ECF2-4C66-8C2F-24E408B86686Q30978579-C32FD5AD-5228-4E1A-A3DA-784DADA6603DQ31037438-3D18C71B-4CC9-40A0-BD8D-B9A90BA6DAFDQ31136043-26D1612A-BFB7-424B-BC34-3AE21EBAB362Q33214478-C9E45F71-9E50-4A51-95B1-C62B0356FC22Q33220847-7A3C07EB-C703-4315-A849-4BF4B4E4E926Q33279696-DE4FB944-05BC-419D-8592-E99BB66A038CQ33526697-B1A6285E-8581-499B-96C7-3CCB3259EBAEQ33654337-F5A62563-E0CE-4032-94BA-067A2C0A1C83Q33719384-3AC8F225-43A9-4894-824D-F2101E17DC49Q33726983-4EB2CF01-8140-4C3E-AD52-40E6F2B594AEQ33753116-5EB7B38D-D880-425F-A6CB-9969934DCCFEQ34247553-9D7E0111-A18A-41FA-B685-D9190C39FC6DQ34532804-D6C55FA6-48AC-4065-B042-C4FCCF630D91Q35165535-646D2DED-351D-46BC-978D-C6D4F51DEA2EQ35239717-F1245F3D-EB7C-4EC7-B090-B7DCD26F3830Q35451950-1AE4D4B9-410C-44F8-9AD0-20C4E0C9E003Q35541987-268E332C-A78C-48F1-8F3C-DAAC573F361BQ35743283-42127563-B139-470E-B193-3130CAD05B34Q35747587-17EC7796-01BF-49CA-BFDA-F2FB7A9C2217Q36044450-4B160431-7291-452B-AE68-8BD855AE3428Q36146148-2326E2B3-F7C6-4C4E-9E25-4C3D16DBB04DQ36212767-6AD7DD0C-5C58-447D-B9C3-BE5F486632CBQ36227090-773BE96E-F486-40DC-8C41-7D5DD0F360B6Q36308146-3D457DCD-D100-4095-BCEB-50C3B1740244Q36438734-1E521838-B515-4CDD-8B15-3AC83AD091E5Q36486885-D57AE1F5-92FD-4423-98F9-0666597BDDB6Q37238770-07DDAA25-209F-4C17-87F1-7A0A77C06FAEQ38317254-6401BC79-1B43-435B-A74B-03B66A73B88FQ39703543-FF6368CD-9DAD-431E-A492-0A69A4FEB860Q40104894-A3D0E82D-EC71-4DF3-8D6D-A6215CC80B28Q40438592-33F3EB7F-E436-4724-9DF5-6067F7B9A259Q41481730-6B800CB2-0947-4170-BB4C-2AB38FAEBF3EQ41660887-CFBAFE0F-8EDE-4271-8E76-73FC0ABE34EDQ41703445-A1CD6702-0892-4041-A0CC-ED4A799E0D4BQ43208254-3F2E7FD0-8EA5-4AD3-9FDD-B4D457C9F466
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Marc Ostermeier
@ast
Marc Ostermeier
@en
Marc Ostermeier
@es
Marc Ostermeier
@nl
type
label
Marc Ostermeier
@ast
Marc Ostermeier
@en
Marc Ostermeier
@es
Marc Ostermeier
@nl
prefLabel
Marc Ostermeier
@ast
Marc Ostermeier
@en
Marc Ostermeier
@es
Marc Ostermeier
@nl
P108
P106
P21
P31
P496
0000-0003-0900-3665