2025
Macromolecular crowding-based biofabrication utilizing unmodified extracellular matrix bioinks
Jordan S, Li X, Rossello-Martinez A, Liang Z, Gong X, Xiao H, Mak M. Macromolecular crowding-based biofabrication utilizing unmodified extracellular matrix bioinks. Acta Biomaterialia 2025, 198: 37-48. PMID: 40268621, DOI: 10.1016/j.actbio.2025.02.052.Peer-Reviewed Original ResearchConceptsDecellularized extracellular matrixExtrusion bioprintingComplex 3D structuresLayer-by-layer buildingCell scaffold materialsNatural extracellular matrixBiofabrication applicationsSolubilized extracellular matrixRobust hydrogelsLow printabilityTissue engineeringBioinkFabrication methodPromote biocompatibilityGelation timeBioactive scaffoldsPrintabilityBiofabricationNative tissueOrgan-specific extracellular matrixCrosslinkingExtracellular matrixBiocompatibilityExtrusionRegenerative medicine
2020
Fluorescent stem peptide mimics: In situ probes for peptidoglycan crosslinking
Gautam S, Kim T, Howell R, Spiegel DA. Fluorescent stem peptide mimics: In situ probes for peptidoglycan crosslinking. Methods In Enzymology 2020, 638: 57-67. PMID: 32416921, DOI: 10.1016/bs.mie.2020.02.016.Peer-Reviewed Case Reports and Technical NotesConceptsBacterial cell wall synthesisSynthetic probesPeptide mimicsPeptidoglycan crosslinkingSynthesisSitu probeKey stepCrosslinkingNumerous classesMechanical strengthNew antibioticsProbeCell wall synthesisPeptidoglycan synthesisSuper-resolution microscopyLive bacteriaWall synthesisReactionCell wallDetailed protocolMicroscopyStaphylococcus aureusHuman pathogens
2019
Synthesis and reactivity of precolibactin 886
Healy AR, Wernke KM, Kim CS, Lees NR, Crawford JM, Herzon SB. Synthesis and reactivity of precolibactin 886. Nature Chemistry 2019, 11: 890-898. PMID: 31548676, PMCID: PMC6761996, DOI: 10.1038/s41557-019-0338-2.Peer-Reviewed Original ResearchConceptsStructural assignmentNucleophilic cleavageΑ-ketoiminesSpontaneous cyclizationSynthetic pathwayΑ-dicarbonylsBasic conditionsHPLC purificationBiosynthetic routeBiosynthetic intermediatesBiosynthesis of metabolitesCleavage pathwayBiosynthetic productsGut commensal Escherichia coliClb gene clusterCleavageCyclizationPyridoneAdductsIntermediatesCompoundsDNA crosslinkingSynthesisCrosslinkingMajor biosynthetic route
1988
Photochemical crosslinking of bacteriophage T4 single‐stranded DNA‐binding protein (gp32) to oligo‐p(dT)8: Identification of phenylalanine‐183 as the site of crosslinking
Shamoo Y, Williams K, Konigsberg W. Photochemical crosslinking of bacteriophage T4 single‐stranded DNA‐binding protein (gp32) to oligo‐p(dT)8: Identification of phenylalanine‐183 as the site of crosslinking. Proteins Structure Function And Bioinformatics 1988, 4: 1-6. PMID: 3186689, DOI: 10.1002/prot.340040103.Peer-Reviewed Original ResearchConceptsCovalent bond formationAnion-exchange high-performance liquid chromatographyHigh-performance liquid chromatographyBond formationGas-phase sequencingLiquid chromatographyPhotochemical crosslinkingPhenylthiohydantoin derivativesSer-GlyTryptic peptidesUltraviolet irradiationTyr-AspUltraviolet lightCrosslinkingSer-AsnHigh affinityCleavage productsGln-ValGlu-SerPeptidesPhotolysisTrypsin cleavage productSingle tryptic peptideChromatographyComplexes
1982
Comparative Peptide Mapping by HPLC: Identification of Single Amino Acid Substitutions in Temperature Sensitive Mutants
Williams K, L’Italien J, Guggenheimer R, Sillerud L, Spicer E, Chase J, Konigsberg W. Comparative Peptide Mapping by HPLC: Identification of Single Amino Acid Substitutions in Temperature Sensitive Mutants. Experimental Biology And Medicine 1982, 499-507. DOI: 10.1007/978-1-4612-5832-2_44.Peer-Reviewed Original ResearchPeptide mappingChemical modificationCovalent proteinComparative peptide mappingAmino acid analysisProtein structureParticular amino acid replacementsPrimary structureLac repressor moleculesHuman hemoglobinHPLCAcid analysisSubstitutionStructurePowerful approachSingle amino acid substitutionCrosslinkingMoleculesAmino acid substitutionsSubtitutionAcid substitutionsMutant proteins
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