about
The Metagenome-Derived Enzymes LipS and LipT Increase the Diversity of Known LipasesStructural basis for the slow dark recovery of a full-length LOV protein from Pseudomonas putidaConservation of dark recovery kinetic parameters and structural features in the pseudomonadaceae "short" light, oxygen, voltage (LOV) protein family: implications for the design of LOV-based optogenetic toolsSignaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR SpectroscopyProbing enzyme promiscuity of SGNH hydrolasesStructure of a LOV protein in apo-state and implications for construction of LOV-based optical tools.Rapid sequence scanning mutagenesis using in silico oligo design and the Megaprimer PCR of whole plasmid method (MegaWHOP).The photophysics of LOV-based fluorescent proteins--new tools for cell biology.Structure and function of a short LOV protein from the marine phototrophic bacterium Dinoroseobacter shibae.LOVely enzymes - towards engineering light-controllable biocatalystsPhotoactivation Reduces Side-Chain Dynamics of a LOV Photoreceptor.A combination of mutational and computational scanning guides the design of an artificial ligand-binding controlled lipase.Catalytically-active inclusion bodies-Carrier-free protein immobilizates for application in biotechnology and biomedicine.Photophysics of the LOV-Based Fluorescent Protein Variant iLOV-Q489K Determined by Simulation and Experiment.Fusion of a flavin-based fluorescent protein to hydroxynitrile lyase from Arabidopsis thaliana improves enzyme stabilitySynthesis of chiral cyanohydrins by recombinant Escherichia coli cells in a micro-aqueous reaction system.Diversity of 'benzenetriol dioxygenase' involved in p-nitrophenol degradation in soil bacteria.Cofactor trapping, a new method to produce flavin mononucleotide.Electron transfer pathways in a light, oxygen, voltage (LOV) protein devoid of the photoactive cysteine.Initial characterization of a blue-light sensing, phototropin-related protein from Pseudomonas putida: a paradigm for an extended LOV construct.Distribution and phylogeny of light-oxygen-voltage-blue-light-signaling proteins in the three kingdoms of life.Interdomain signalling in the blue-light sensing and GTP-binding protein YtvA: a mutagenesis study uncovering the importance of specific protein sites.Special Issue dedicated to Karl-Erich Jaeger on the occasion of his 60th birthday.Reporter proteins for in vivo fluorescence without oxygen.Conformational analysis of the blue-light sensing protein YtvA reveals a competitive interface for LOV-LOV dimerization and interdomain interactions.Purification and simultaneous immobilization of Arabidopsis thaliana hydroxynitrile lyase using a family 2 carbohydrate-binding module.insilico.mutagenesis: a primer selection tool designed for sequence scanning applications used in directed evolution experiments.Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production.Mechanistic Basis of the Fast Dark Recovery of the Short LOV Protein DsLOV from Dinoroseobacter shibaeMutual Exchange of Kinetic Properties by Extended Mutagenesis in Two Short LOV Domain Proteins fromPseudomonas putidaTailoring the properties of (catalytically)-active inclusion bodiesEnlightened enzymes: strategies to create novel photoresponsive proteinsDiscovery of the first light-dependent protochlorophyllide oxidoreductase in anoxygenic phototrophic bacteriaConsensus model of a cyanobacterial light-dependent protochlorophyllide oxidoreductase in its pigment-free apo-form and photoactive ternary complexA Synthetic Reaction Cascade Implemented by Colocalization of Two Proteins within Catalytically Active Inclusion BodiesA thermostable flavin-based fluorescent protein from Chloroflexus aggregans: a framework for ultra-high resolution structural studiesTernary Complex Formation and Photoactivation of a Photoenzyme Results in Altered Protein Dynamics
P50
Q27674858-6B873C33-CE2F-4203-A78A-398E629D8938Q27677220-722DFB8B-4A3E-44B4-BAFD-98C1684471CEQ27684767-A90E2C88-46E6-47B7-8E96-9B8375A8E6CEQ27709854-0A44E5DD-96C4-445D-A47F-B6D42FBF8FF8Q28492669-BAD95865-183E-4D07-91E3-F98798B326B1Q30838981-0025D730-B027-4FCB-86B0-E053441FEE33Q33647031-AD2EBFB4-B284-4CBB-9017-7089423B6367Q34402598-12A15217-86EB-4A28-A5CD-F4E06A5E2DA9Q35607806-761B336F-1C76-4987-A67F-FF828DDB016BQ37831409-D1E322A3-EF44-4167-91F6-D485BEEC545EQ38951149-24118215-72AD-48DC-8DA0-F091CBB4E420Q38952031-873D05B5-1378-4D94-A367-6E6FDD341997Q39279132-9E9F828B-334C-4A0F-A81A-1C5A81C8AF5FQ39932267-C433A1CE-BE52-47EA-AC9C-519E71935F62Q42119355-B887F425-B097-461A-AF47-48B5C9427290Q42133994-B93EAC18-B975-4563-903E-4C341D9C06B5Q42327038-97B5DB91-9CE5-48A0-973B-22603B81ACBEQ42582954-6646F758-1B08-45DF-A47C-874DA9349DD6Q42656935-0BEF6380-CC69-47E4-8C66-CADD1704FA38Q42669241-665989F2-0FAD-4A17-8917-2874F8806277Q42688668-1B461E43-A18E-449E-A380-35C08949C469Q43198094-FDE7DD5C-CBE8-4708-A5FC-E30276977627Q48057715-1ADD1B0C-B251-49E3-AEFB-A24B0BAA5841Q50470989-53EEE317-6EBC-404D-B818-7A4E6CE7AB60Q50472921-89F10143-D402-4CA0-AD4B-6A540C2FE7D3Q51000448-22D202E7-9032-4B4C-B815-077CC17593EEQ51959281-D9446A1F-DB6C-49AA-8832-42B123F2D95BQ52593099-C87DC9C4-68E1-4067-82B1-DC67FF51C01FQ57243783-AF51E0EE-48F6-44CA-9918-867B8C928734Q60921752-C08D3AAD-62FF-48C9-89B3-B4C47DFAAB27Q61797935-CD9E66C5-4E20-4E99-AFEB-CC90B673B368Q83390854-6404BB4E-910B-44B6-A733-44CBD05893F1Q87413843-D1698C24-B5C8-4BE3-93B8-955748359F89Q90471784-5C484585-BE11-45EB-9909-1E873B7DFD34Q90572966-077B5FF3-5446-47A1-99A3-F0026E174D9BQ92212547-747ADC19-735E-406E-9288-B6E9B887FD77Q92411702-FFE3C543-EEE8-49DF-A04F-407E9BB96C31
P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Ulrich Krauss
@ast
Ulrich Krauss
@en
Ulrich Krauss
@es
Ulrich Krauss
@nl
Ulrich Krauss
@sl
type
label
Ulrich Krauss
@ast
Ulrich Krauss
@en
Ulrich Krauss
@es
Ulrich Krauss
@nl
Ulrich Krauss
@sl
prefLabel
Ulrich Krauss
@ast
Ulrich Krauss
@en
Ulrich Krauss
@es
Ulrich Krauss
@nl
Ulrich Krauss
@sl
P106
P21
P31
P496
0000-0003-2219-7388