Research graph
References from Biochemical Investigation of PumG, a Key Pyridoxal 5′-Phosphate (PLP)-Dependent Aminotransferase Involved in Pseudouridimycin Biosynthesis. Local targets link to admitted publications; unresolved targets remain external evidence.
Pseudouridine-Modifying Enzymes SapB and SapH Control Entry into the Pseudouridimycin Biosynthetic Pathway
10.1021/acschembio.2c00826 · 2023 · External reference
Analysis of the Pseudouridimycin Biosynthetic Pathway Provides Insights into the Formation of C-Nucleoside Antibiotics
10.1016/j.chembiol.2018.02.008 · 2018 · External reference
Discovery, Properties, and Biosynthesis of Pseudouridimycin, an Antibacterial Nucleoside Analog Inhibitor of Bacterial RNA Polymerase
10.1007/s10295-018-2109-2 · 2019 · External reference
Blocks in the Pseudouridimycin Pathway Unlock Hidden Metabolites in the Streptomyces Producer Strain
10.1038/s41598-021-84833-2 · 2021 · External reference
Structural Mechanism for Rifampicin Inhibition of Bacterial RNA Polymerase
10.1016/s0092-8674(01)00286-0 · 2001 · External reference
New Target for Inhibition of Bacterial RNA Polymerase: ‘Switch Region’
10.1016/j.mib.2011.07.030 · 2011 · External reference
Antibacterial Nucleoside-Analog Inhibitor of Bacterial RNA Polymerase
10.1016/j.cell.2017.05.042 · 2017 · External reference
Characterization of C-Nucleoside Antimicrobials from Streptomyces Albus DSM 40763: Strepturidin Is Pseudouridimycin
10.1038/s41598-019-45375-w · 2019 · External reference
Pseudouridimycin Biosynthesis: Biochemical Characterization of the Glucose–Methanol–Choline (GMC) Family Oxidoreductase
10.1021/acs.biochem.5c00177 · 2025 · External reference
Evolutionary Origin and Functional Diversification of Aminotransferases
10.1016/j.jbc.2022.102122 · 2022 · External reference
Recent Advances in Protein Engineering and Synthetic Applications of Amino Acid Transaminases
10.1002/cctc.202401952 · 2025 · External reference
Biogenesis of the Unique 4′,5′-Dehydronucleoside of the Uridyl Peptide Antibiotic Pacidamycin
10.1021/ja206163j · 2011 · External reference
SsaA, a Member of a Novel Class of Transcriptional Regulators, Controls Sansanmycin Production in Streptomyces Sp. Strain SS through a Feedback Mechanism
10.1128/jb.00054-13 · 2013 · External reference
LIPOSIDOMYCINS: NOVEL NUCLEOSIDE ANTIBIOTICS WHICH INHIBIT BACTERIAL PEPTIDOGLYCAN SYNTHESIS
10.7164/antibiotics.38.1617 · 1985 · External reference
Caprazamycins, Novel Lipo-Nucleoside Antibiotics, from Streptomyces Sp
10.1038/ja.2005.41 · 2005 · External reference
Identification of the Genecluster Involved in Muraymycin Biosynthesis from Streptomyces Sp. NRRL 30471†
10.1039/c0mb00237b · 2011 · External reference
The Muraminomicin Biosynthetic Gene Cluster and Enzymatic Formation of the 2-Deoxyaminoribosyl Appendage
10.1039/c2md20245j · 2012 · External reference
Structure-Based Gene Targeting Discovery of Sphaerimicin, a Bacterial Translocase I Inhibitor
10.1002/anie.201305546 · 2013 · External reference
Recent Advances in the Biosynthesis of Nucleoside Antibiotics
10.1038/s41429-019-0236-2 · 2019 · External reference
Nucleoside Antibiotics: Biosynthesis, Regulation, and Biotechnology
10.1016/j.tim.2014.10.007 · 2015 · External reference
Natural and Engineered Biosynthesis of Nucleoside Antibiotics in Actinomycetes
10.1007/s10295-015-1636-3 · 2016 · External reference
Cryptic Phosphorylation-Mediated Divergent Biosynthesis of High-Carbon Sugar Nucleoside Antifungals
10.1021/acschembio.1c00971 · 2022 · External reference
A Common Structural Basis for pH- and Calmodulin-Mediated Regulation in Plant Glutamate Decarboxylase
10.1016/j.jmb.2009.06.080 · 2009 · External reference
Functional Characterization and Structure-Guided Mutational Analysis of the Transsulfuration Enzyme Cystathionine γ-Lyase from Toxoplasma Gondii
10.3390/ijms19072111 · 2018 · External reference
Unresolved reference
External reference
Pyridoxal 5′-Phosphate Is a Slow Tight Binding Inhibitor of E
10.1371/journal.pone.0041680 · 2012 · External reference
Pac13 Is a Small, Monomeric Dehydratase That Mediates the Formation of the 3′-Deoxy Nucleoside of Pacidamycins
10.1002/anie.201705639 · 2017 · External reference
Comparative Protein Structure Modeling Using MODELLER
10.1002/cpbi.3 · 2016 · External reference
Comparative Protein Modelling by Satisfaction of Spatial Restraints
10.1006/jmbi.1993.1626 · 1993 · External reference
Modeling of Loops in Protein Structures
10.1110/ps.9.9.1753 · 2000 · External reference
AutoDock4 and AutoDockTools4: Automated Docking with Selective Receptor Flexibility
10.1002/jcc.21256 · 2009 · External reference
Avogadro: An Advanced Semantic Chemical Editor, Visualization, and Analysis Platform
10.1186/1758-2946-4-17 · 2012 · External reference
Automated Docking Using a Lamarckian Genetic Algorithm and an Empirical Binding Free Energy Function
10.1002/(sici)1096-987x(19981115)19:14%3c1639::aid-jcc10%3e3.0.co;2-b · 1998 · External reference
CHARMM: The Biomolecular Simulation Program
10.1002/jcc.21287 · 2009 · External reference
CHARMM-GUI Input Generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM/OpenMM Simulations Using the CHARMM36 Additive Force Field
10.1021/acs.jctc.5b00935 · 2016 · External reference
CHARMM-GUI: A Web-Based Graphical User Interface for CHARMM
10.1002/jcc.20945 · 2008 · External reference
AmberTools
10.1021/acs.jcim.3c01153 · 2023 · External reference
CHARMM-GUI Ligand Reader and Modeler for CHARMM Force Field Generation of Small Molecules
10.1002/jcc.24829 · 2017 · External reference
PDB2PQR: An Automated Pipeline for the Setup of Poisson–Boltzmann Electrostatics Calculations
10.1093/nar/gkh381 · 2004 · External reference
PDB2PQR: Expanding and Upgrading Automated Preparation of Biomolecular Structures for Molecular Simulations
10.1093/nar/gkm276 · 2007 · External reference
Web Servers and Services for Electrostatics Calculations with APBS and PDB2PQR
10.1002/jcc.21720 · 2011 · External reference
Improvements to the APBS Biomolecular Solvation Software Suite
10.1002/pro.3280 · 2018 · External reference
CHARMM36m: An Improved Force Field for Folded and Intrinsically Disordered Proteins
10.1038/nmeth.4067 · 2017 · External reference
Solvent-Induced Forces between Two Hydrophilic Groups
10.1021/j100059a038 · 1994 · External reference
Comparison of Simple Potential Functions for Simulating Liquid Water
10.1063/1.445869 · 1983 · External reference
CHARMM General Force Field: A Force Field for Drug-like Molecules Compatible with the CHARMM All-Atom Additive Biological Force Fields
10.1002/jcc.21367 · 2010 · External reference
Molecular Dynamics Simulation for Polymers in the Presence of a Heat Bath
10.1103/physreva.33.3628 · 1986 · External reference
Molecular Dynamics Simulations of Water and Biomolecules with a Monte Carlo Constant Pressure Algorithm
10.1016/j.cplett.2003.12.039 · 2004 · External reference
Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n-Alkanes
10.1016/0021-9991(77)90098-5 · 1977 · External reference
Comparison of the Absorbance Spectra and Fluorescence Behavior of Phosphorylase b with That of Model Pyridoxal Phosphate Derivatives in Various Solvents
10.1016/s0021-9258(19)45615-9 · 1972 · External reference
L-Threonine Transaldolase Activity Is Enabled by a Persistent Catalytic Intermediate
10.1021/acschembio.0c00753 · 2021 · External reference
Controlling Reaction Specificity in Pyridoxal Phosphate Enzymes
10.1016/j.bbapap.2011.05.019 · 2011 · External reference
Cyclic Di-GMP Acts as a Cell Cycle Oscillator to Drive Chromosome Replication
10.1038/nature14473 · 2015 · External reference
10.1385/0-89603-234-5:305
10.1385/0-89603-234-5:305 · 1993 · External reference
Identification of the Genecluster Involved in Muraymycin Biosynthesis from Streptomyces Sp. NRRL 30471
10.1039/c0mb00237b · 2011 · External reference
Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations
10.1146/annurev.biochem.73.011303.074021 · 2004 · External reference
VMD: Visual Molecular Dynamics
10.1016/0263-7855(96)00018-5 · 1996 · External reference
Aspartate Aminotransferase: An Old Dog Teaches New Tricks
10.1016/j.abb.2013.10.002 · 2014 · External reference
Molecular Defects of the Glycine 41 Variants of Alanine Glyoxylate Aminotransferase Associated with Primary Hyperoxaluria Type I
10.1073/pnas.0908565107 · 2010 · External reference
Designing Heterodimeric Two-Stranded α-Helical Coiled-Coils: Effects of hydrophobicity and alpha-helical propensity on protein folding, stability, and specificity
10.1074/jbc.m204257200 · 2002 · External reference
Crystal Structures of the Chromobacterium Violaceumω-Transaminase Reveal Major Structural Rearrangements upon Binding of Coenzyme PLP
10.1111/j.1742-4658.2012.08468.x · 2012 · External reference
Automated Docking Using a Lamarckian Genetic Algorithm and an Empirical Binding Free Energy Function
10.1002/(sici)1096-987x(19981115)19:14%3c1639::aid-jcc10%3e3.0.co;2-b · ExternalCitation · doi-reference
Structure-Based Gene Targeting Discovery of Sphaerimicin, a Bacterial Translocase I Inhibitor
10.1002/anie.201305546 · ExternalCitation · doi-reference
Pac13 Is a Small, Monomeric Dehydratase That Mediates the Formation of the 3′-Deoxy Nucleoside of Pacidamycins
10.1002/anie.201705639 · ExternalCitation · doi-reference
Recent Advances in Protein Engineering and Synthetic Applications of Amino Acid Transaminases
10.1002/cctc.202401952 · ExternalCitation · doi-reference
Comparative Protein Structure Modeling Using MODELLER
10.1002/cpbi.3 · ExternalCitation · doi-reference
CHARMM-GUI: A Web-Based Graphical User Interface for CHARMM
10.1002/jcc.20945 · ExternalCitation · doi-reference
AutoDock4 and AutoDockTools4: Automated Docking with Selective Receptor Flexibility
10.1002/jcc.21256 · ExternalCitation · doi-reference
CHARMM: The Biomolecular Simulation Program
10.1002/jcc.21287 · ExternalCitation · doi-reference
CHARMM General Force Field: A Force Field for Drug-like Molecules Compatible with the CHARMM All-Atom Additive Biological Force Fields
10.1002/jcc.21367 · ExternalCitation · doi-reference
Web Servers and Services for Electrostatics Calculations with APBS and PDB2PQR
10.1002/jcc.21720 · ExternalCitation · doi-reference
CHARMM-GUI Ligand Reader and Modeler for CHARMM Force Field Generation of Small Molecules
10.1002/jcc.24829 · ExternalCitation · doi-reference
Improvements to the APBS Biomolecular Solvation Software Suite
10.1002/pro.3280 · ExternalCitation · doi-reference
Comparative Protein Modelling by Satisfaction of Spatial Restraints
10.1006/jmbi.1993.1626 · ExternalCitation · doi-reference
Natural and Engineered Biosynthesis of Nucleoside Antibiotics in Actinomycetes
10.1007/s10295-015-1636-3 · ExternalCitation · doi-reference
Discovery, Properties, and Biosynthesis of Pseudouridimycin, an Antibacterial Nucleoside Analog Inhibitor of Bacterial RNA Polymerase
10.1007/s10295-018-2109-2 · ExternalCitation · doi-reference
Numerical Integration of the Cartesian Equations of Motion of a System with Constraints: Molecular Dynamics of n-Alkanes
10.1016/0021-9991(77)90098-5 · ExternalCitation · doi-reference
VMD: Visual Molecular Dynamics
10.1016/0263-7855(96)00018-5 · ExternalCitation · doi-reference
Aspartate Aminotransferase: An Old Dog Teaches New Tricks
10.1016/j.abb.2013.10.002 · ExternalCitation · doi-reference
Controlling Reaction Specificity in Pyridoxal Phosphate Enzymes
10.1016/j.bbapap.2011.05.019 · ExternalCitation · doi-reference
Antibacterial Nucleoside-Analog Inhibitor of Bacterial RNA Polymerase
10.1016/j.cell.2017.05.042 · ExternalCitation · doi-reference
Analysis of the Pseudouridimycin Biosynthetic Pathway Provides Insights into the Formation of C-Nucleoside Antibiotics
10.1016/j.chembiol.2018.02.008 · ExternalCitation · doi-reference
Molecular Dynamics Simulations of Water and Biomolecules with a Monte Carlo Constant Pressure Algorithm
10.1016/j.cplett.2003.12.039 · ExternalCitation · doi-reference
Evolutionary Origin and Functional Diversification of Aminotransferases
10.1016/j.jbc.2022.102122 · ExternalCitation · doi-reference
A Common Structural Basis for pH- and Calmodulin-Mediated Regulation in Plant Glutamate Decarboxylase
10.1016/j.jmb.2009.06.080 · ExternalCitation · doi-reference
New Target for Inhibition of Bacterial RNA Polymerase: ‘Switch Region’
10.1016/j.mib.2011.07.030 · ExternalCitation · doi-reference
Nucleoside Antibiotics: Biosynthesis, Regulation, and Biotechnology
10.1016/j.tim.2014.10.007 · ExternalCitation · doi-reference
Comparison of the Absorbance Spectra and Fluorescence Behavior of Phosphorylase b with That of Model Pyridoxal Phosphate Derivatives in Various Solvents
10.1016/s0021-9258(19)45615-9 · ExternalCitation · doi-reference
Structural Mechanism for Rifampicin Inhibition of Bacterial RNA Polymerase
10.1016/s0092-8674(01)00286-0 · ExternalCitation · doi-reference
Pseudouridimycin Biosynthesis: Biochemical Characterization of the Glucose–Methanol–Choline (GMC) Family Oxidoreductase
10.1021/acs.biochem.5c00177 · ExternalCitation · doi-reference
AmberTools
10.1021/acs.jcim.3c01153 · ExternalCitation · doi-reference
CHARMM-GUI Input Generator for NAMD, GROMACS, AMBER, OpenMM, and CHARMM/OpenMM Simulations Using the CHARMM36 Additive Force Field
10.1021/acs.jctc.5b00935 · ExternalCitation · doi-reference
L-Threonine Transaldolase Activity Is Enabled by a Persistent Catalytic Intermediate
10.1021/acschembio.0c00753 · ExternalCitation · doi-reference
Cryptic Phosphorylation-Mediated Divergent Biosynthesis of High-Carbon Sugar Nucleoside Antifungals
10.1021/acschembio.1c00971 · ExternalCitation · doi-reference
Pseudouridine-Modifying Enzymes SapB and SapH Control Entry into the Pseudouridimycin Biosynthetic Pathway
10.1021/acschembio.2c00826 · ExternalCitation · doi-reference
Solvent-Induced Forces between Two Hydrophilic Groups
10.1021/j100059a038 · ExternalCitation · doi-reference
Biogenesis of the Unique 4′,5′-Dehydronucleoside of the Uridyl Peptide Antibiotic Pacidamycin
10.1021/ja206163j · ExternalCitation · doi-reference
Caprazamycins, Novel Lipo-Nucleoside Antibiotics, from Streptomyces Sp
10.1038/ja.2005.41 · ExternalCitation · doi-reference
Cyclic Di-GMP Acts as a Cell Cycle Oscillator to Drive Chromosome Replication
10.1038/nature14473 · ExternalCitation · doi-reference
CHARMM36m: An Improved Force Field for Folded and Intrinsically Disordered Proteins
10.1038/nmeth.4067 · ExternalCitation · doi-reference
Recent Advances in the Biosynthesis of Nucleoside Antibiotics
10.1038/s41429-019-0236-2 · ExternalCitation · doi-reference
Characterization of C-Nucleoside Antimicrobials from Streptomyces Albus DSM 40763: Strepturidin Is Pseudouridimycin
10.1038/s41598-019-45375-w · ExternalCitation · doi-reference
Blocks in the Pseudouridimycin Pathway Unlock Hidden Metabolites in the Streptomyces Producer Strain
10.1038/s41598-021-84833-2 · ExternalCitation · doi-reference
Identification of the Genecluster Involved in Muraymycin Biosynthesis from Streptomyces Sp. NRRL 30471
10.1039/c0mb00237b · ExternalCitation · doi-reference
The Muraminomicin Biosynthetic Gene Cluster and Enzymatic Formation of the 2-Deoxyaminoribosyl Appendage
10.1039/c2md20245j · ExternalCitation · doi-reference
Comparison of Simple Potential Functions for Simulating Liquid Water
10.1063/1.445869 · ExternalCitation · doi-reference
Molecular Defects of the Glycine 41 Variants of Alanine Glyoxylate Aminotransferase Associated with Primary Hyperoxaluria Type I
10.1073/pnas.0908565107 · ExternalCitation · doi-reference
Designing Heterodimeric Two-Stranded α-Helical Coiled-Coils: Effects of hydrophobicity and alpha-helical propensity on protein folding, stability, and specificity
10.1074/jbc.m204257200 · ExternalCitation · doi-reference
PDB2PQR: An Automated Pipeline for the Setup of Poisson–Boltzmann Electrostatics Calculations
10.1093/nar/gkh381 · ExternalCitation · doi-reference
PDB2PQR: Expanding and Upgrading Automated Preparation of Biomolecular Structures for Molecular Simulations
10.1093/nar/gkm276 · ExternalCitation · doi-reference
Molecular Dynamics Simulation for Polymers in the Presence of a Heat Bath
10.1103/physreva.33.3628 · ExternalCitation · doi-reference
Modeling of Loops in Protein Structures
10.1110/ps.9.9.1753 · ExternalCitation · doi-reference
Crystal Structures of the Chromobacterium Violaceumω-Transaminase Reveal Major Structural Rearrangements upon Binding of Coenzyme PLP
10.1111/j.1742-4658.2012.08468.x · ExternalCitation · doi-reference
SsaA, a Member of a Novel Class of Transcriptional Regulators, Controls Sansanmycin Production in Streptomyces Sp. Strain SS through a Feedback Mechanism
10.1128/jb.00054-13 · ExternalCitation · doi-reference
Pyridoxal Phosphate Enzymes: Mechanistic, Structural, and Evolutionary Considerations
10.1146/annurev.biochem.73.011303.074021 · ExternalCitation · doi-reference
Avogadro: An Advanced Semantic Chemical Editor, Visualization, and Analysis Platform
10.1186/1758-2946-4-17 · ExternalCitation · doi-reference
Pyridoxal 5′-Phosphate Is a Slow Tight Binding Inhibitor of E
10.1371/journal.pone.0041680 · ExternalCitation · doi-reference
10.1385/0-89603-234-5:305
10.1385/0-89603-234-5:305 · ExternalCitation · doi-reference
Functional Characterization and Structure-Guided Mutational Analysis of the Transsulfuration Enzyme Cystathionine γ-Lyase from Toxoplasma Gondii
10.3390/ijms19072111 · ExternalCitation · doi-reference
LIPOSIDOMYCINS: NOVEL NUCLEOSIDE ANTIBIOTICS WHICH INHIBIT BACTERIAL PEPTIDOGLYCAN SYNTHESIS
10.7164/antibiotics.38.1617 · ExternalCitation · doi-reference
