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A lipoamide dehydrogenase from Neisseria meningitidis has a lipoyl domain
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What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1002/prot.340130406openalex-snapshot
The refined crystal structure of Pseudomonas putida lipoamide dehydrogenase complexed with NAD+ at 2.45 Å resolution
inferredcites →https://doi.org/10.1006/jmbi.1993.1103openalex-snapshot
Three-dimensional Structure of the Lipoyl domain from Bacillus stearothermophilus Pyruvate Dehydrogenase Multienzyme Complex
inferredcites →https://doi.org/10.1006/jmbi.1993.1235openalex-snapshot
Refined Crystal Structure of the Catalytic Domain of Dihydrolipoyl Transacetylase (E2p) from Azotobacter vinelandii at 2·6 Å Resolution
inferredcites →https://doi.org/10.1006/jmbi.1993.1236openalex-snapshot
Three-dimensional Structure of Lipoamide Dehydrogenase from Pseudomonas fluorescens at 2·8 Å Resolution
inferredcites →https://doi.org/10.1016/0003-9861(89)90309-3openalex-snapshot
Dihydrolipoamide dehydrogenase: Functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases
inferredcites →https://doi.org/10.1016/0014-5793(86)80979-6openalex-snapshot
Chain folding in the dihydrolipoyl acyltransferase components of the 2‐oxo‐acid dehydrogenase complexes from Escherichia coli
inferredcites →https://doi.org/10.1016/0022-2836(91)90367-fopenalex-snapshot
Refined crystal structure of lipoamide dehydrogenase from Azotobacter vinelandii at 2.2 Å resolution
inferredcites →https://doi.org/10.1021/bi00128a021openalex-snapshot
Three-dimensional solution structure of the E3-binding domain of the dihydrolipoamide succinyltransferase core from the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli
inferredcites →https://doi.org/10.1021/bi00361a021openalex-snapshot
Dihydrolipoamide dehydrogenase from halophilic archaebacteria: purification and properties of the enzyme from Halobacterium halobium
inferredcites →https://doi.org/10.1042/bj2430661openalex-snapshot
Dihydrolipoamide dehydrogenase from Trypanosoma brucei. Characterization and cellular location
inferredcites →https://doi.org/10.1042/bj2470641openalex-snapshot
Segmental structure and protein domains in the pyruvate dehydrogenase multienzyme complex of Escherichia coli . Genetic reconstruction in vitro and 1H-n.m.r. spectroscopy
inferredcites →https://doi.org/10.1042/bj2880823openalex-snapshot
Purification, characterization and function of dihydrolipoamide dehydrogenase from the cyanobacterium Anabaena sp. strain P.C.C. 7119
inferredcites →https://doi.org/10.1093/nar/10.22.7449openalex-snapshot
Sequence of themalKgene inE.coliK12
inferredcites →https://doi.org/10.1111/j.1432-1033.1983.tb07683.xopenalex-snapshot
Nucleotide sequence of the lipoamide dehydrogenase gene of Escherichia coli K12
inferredcites →https://doi.org/10.1111/j.1432-1033.1986.tb09596.xopenalex-snapshot
Galactose- and maltose-stimulated lipoamide dehydrogenase activities related to the binding-protein-dependent transport of galactose and maltose in toluenized cells of Escherichia coli
inferredcites →https://doi.org/10.1111/j.1574-6941.1980.tb01619.xopenalex-snapshot
IDENTIFICATION OF ANTIGEN 19/27 AS DIHYDROLIPOYL DEHYDROGENASE AND ITS PROBABLE INVOLVEMENT IN UBIQUINONE-MEDIATED NADH-DEPENDENT TRANSPORT PHENOMENA IN MEMBRANE VESICLES OFESCHERICHIA COLI
inferredcites →https://doi.org/10.1128/jb.162.1.286-293.1985openalex-snapshot
Possible involvement of lipoic acid in binding protein-dependent transport systems in Escherichia coli
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/jmr.2924openalex-snapshot
The moonlighting activities of dihydrolipoamide dehydrogenase: Biotechnological and biomedical applications
inferred← citeshttps://doi.org/10.1002/jmr.919openalex-snapshot
The titanium binding protein of Rhodococcus ruber GIN1 (NCIMB 40340) is a cell‐surface homolog of the cytosolic enzyme dihydrolipoamide dehydrogenase
inferred← citeshttps://doi.org/10.1002/pmic.200500100openalex-snapshot
Proteomic analysis of Candida albicans yeast and hyphal cell wall and associated proteins
inferred← citeshttps://doi.org/10.1006/jmbi.1997.1009openalex-snapshot
Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis
inferred← citeshttps://doi.org/10.1006/jsbi.1997.3846openalex-snapshot
Folding and Assembly of Hepatitis B Virus Core Protein: A New Model Proposal
inferred← citeshttps://doi.org/10.1007/s00216-021-03569-0openalex-snapshot
Synthesis, LC-MS/MS analysis, and biological evaluation of two vaccine candidates against ticks based on the antigenic P0 peptide from R. sanguineus linked to the p64K carrier protein from Neisseria meningitidis
inferred← citeshttps://doi.org/10.1016/j.biochi.2009.04.007openalex-snapshot
Moonlighting protein in Starkeyomyces koorchalomoides: Characterization of dihydrolipoamide dehydrogenase as a protein acetyltransferase utilizing acetoxycoumarin as the acetyl group donor
inferred← citeshttps://doi.org/10.1016/j.ejbt.2018.03.004openalex-snapshot
Scaling-up fermentation of Escherichia coli for production of recombinant P64k protein from Neisseria meningitidis
inferred← citeshttps://doi.org/10.1016/j.jpba.2011.01.041openalex-snapshot
Novel and sensitive ELISA for the rapid quantification of recombinant p64K protein
inferred← citeshttps://doi.org/10.1016/j.microc.2024.111025openalex-snapshot
On the utility of the extracted ion chromatograms for assigning the conjugation sites and side reactions in bioconjugates synthesized by the maleimide-thiol chemistry
inferred← citeshttps://doi.org/10.1016/s0079-6603(04)78003-4openalex-snapshot
Flavoprotein Disulfide Reductases: Advances in Chemistry and Function
inferred← citeshttps://doi.org/10.1016/s0378-1097(99)00140-8openalex-snapshot
Characterisation of the lpdA gene from Neisseria meningitidis by polymerase chain reaction, restriction fragment length polymorphism and sequencing
inferred← citeshttps://doi.org/10.1042/ba19990115openalex-snapshot
B‐cell epitope mapping of theNeisseria meningitidisP64k protein using overlapping peptides
inferred← citeshttps://doi.org/10.1042/ba20010029openalex-snapshot
Safety and preliminary immunogenicity of the recombinant outer membrane protein P64k of Neisseria meningitidis in human volunteers
inferred← citeshttps://doi.org/10.1046/j.0014-2956.2001.02422.xopenalex-snapshot
Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis
inferred← citeshttps://doi.org/10.1073/pnas.1105429108openalex-snapshot
Repurposing lipoic acid changes electron flow in two important metabolic pathways of Escherichia coli
inferred← citeshttps://doi.org/10.1074/jbc.m703144200openalex-snapshot
Enzymatic Characterization of Dihydrolipoamide Dehydrogenase from Streptococcus pneumoniae Harboring Its Own Substrate
inferred← citeshttps://doi.org/10.1080/08982100801893887openalex-snapshot
Humoral Immune Response Against Epidermal Growth Factor Encapsulated in Dehydration Rehydration Vesicles of Different Phospholipid Composition
inferred← citeshttps://doi.org/10.1111/j.1470-8744.1998.tb00494.xopenalex-snapshot
Expression in Escherichia coli of the lpdA gene, protein sequence analysis and immunological characterization of the P64k protein from Neisseria meningitidis
inferred← citeshttps://doi.org/10.1111/j.1470-8744.1999.tb00540.xopenalex-snapshot
Preformulation study of the vaccine candidate P64k against Neisseria meningitidis
inferred← citeshttps://doi.org/10.1111/j.1574-695x.2006.00047.xopenalex-snapshot
Safety and preliminary immunogenicity of MenC/P64k, a meningococcal serogroup C conjugate vaccine with a new recombinant carrier
inferred← citeshttps://doi.org/10.1128/mmbr.00008-10openalex-snapshot
Lipoic Acid Metabolism in Microbial Pathogens
inferred← citeshttps://doi.org/10.1139/w00-133openalex-snapshot
Mapping of monoclonal antibodies specific to P64k: A common antigen of several isolates of Neisseria meningitidis
inferred← citeshttps://doi.org/10.3389/fmicb.2020.631433openalex-snapshot
A Novel Lipoate-Protein Ligase, Mhp-LplJ, Is Required for Lipoic Acid Metabolism in Mycoplasma hyopneumoniae
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