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Targeted Catalytic Inactivation of Angiotensin Converting Enzyme by Lisinopril-Coupled Transition-Metal Chelates

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Cleavage Agents for Soluble Oligomers of Amyloid β Peptides
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Metallotherapeutics: Novel Strategies in Drug Design
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Neuromedin C Binds Cu(II) and Ni(II) via the ATCUN Motif: Implications for the CNS and Cancer Growth
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Peptide-cleaving catalyst selective for melanin-concentrating hormone: oxidative decarboxylation of N-terminal aspartate catalyzed by Co(III)cyclen
inferredcites →https://doi.org/10.1007/s00775-006-0145-2openalex-snapshot
Metallopeptide-promoted inactivation of angiotensin-converting enzyme and endothelin-converting enzyme 1: toward dual-action therapeutics
inferredcites →https://doi.org/10.1007/s00775-007-0221-2openalex-snapshot
Cellular activity of Rev response element RNA targeting metallopeptides
inferredcites →https://doi.org/10.1007/s00775-008-0354-yopenalex-snapshot
Cleavage agents for soluble oligomers of human islet amyloid polypeptide
inferredcites →https://doi.org/10.1007/s00775-010-0750-yopenalex-snapshot
New chelating ligands for Co(III)-based peptide-cleaving catalysts selective for pathogenic proteins of amyloidoses
inferredcites →https://doi.org/10.1016/0006-291x(90)91766-lopenalex-snapshot
A deeply recessed active site in angiotensin-converting enzyme is indicated from the binding characteristics of biotin-spacer-inhibitor reagents
inferredcites →https://doi.org/10.1016/j.ab.2007.07.008openalex-snapshot
Rapid determination of enzyme kinetics from fluorescence: Overcoming the inner filter effect
inferredcites →https://doi.org/10.1016/j.bbrc.2007.04.121openalex-snapshot
Pro-oxidant activity of histatin 5 related Cu(II)-model peptide probed by mass spectrometry
inferredcites →https://doi.org/10.1016/j.bmc.2010.02.045openalex-snapshot
Cu(II) cyclen cleavage agent for human islet amyloid peptide
inferredcites →https://doi.org/10.1016/j.cbpa.2008.01.028openalex-snapshot
Metal complexes as artificial proteases: toward catalytic drugs
inferredcites →https://doi.org/10.1016/j.jmb.2006.01.048openalex-snapshot
Crystal Structure of the N Domain of Human Somatic Angiotensin I-converting Enzyme Provides a Structural Basis for Domain-specific Inhibitor Design
inferredcites →https://doi.org/10.1016/s0014-5793(01)02157-3openalex-snapshot
Zinc and copper bind to unique sites of histatin 5
inferredcites →https://doi.org/10.1016/s0021-9258(17)43139-5openalex-snapshot
Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site.
inferredcites →https://doi.org/10.1016/s0021-9258(18)61817-4openalex-snapshot
Ternary Coordination Complex between Human Serum Albumin, Copper (II), and l-Histidine
inferredcites →https://doi.org/10.1016/s0021-9258(18)63601-4openalex-snapshot
The Amino Acid Sequence of Peptide (1–24) of Rat and Human Serum Albumins
inferredcites →https://doi.org/10.1016/s0021-9258(18)98378-xopenalex-snapshot
Differences in the properties and enzymatic specificities of the two active sites of angiotensin I-converting enzyme (kininase II). Studies with bradykinin and other natural peptides
inferredcites →https://doi.org/10.1016/s0021-9258(20)79900-xopenalex-snapshot
A Peptide Molecule Mimicking the Copper(II) Transport Site of Human Serum Albumin
inferredcites →https://doi.org/10.1021/bi00014a030openalex-snapshot
Highly Specific Oxidative Crosslinking of Proteins Mediated by a Nickel-Peptide Complex
inferredcites →https://doi.org/10.1021/bi00243a012openalex-snapshot
Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes
inferredcites →https://doi.org/10.1021/bi00272a015openalex-snapshot
Potentiometric titrations and oxidation-reduction potentials of several iron superoxide dismutases
inferredcites →https://doi.org/10.1021/bi971565jopenalex-snapshot
Protease Activity of 1,10-Phenanthroline−Copper(I). Targeted Scission of the Catalytic Site of Carbonic Anhydrase
inferredcites →https://doi.org/10.1021/ci800390mopenalex-snapshot
Partial Charge Calculation Method Affects CoMFA QSAR Prediction Accuracy
inferredcites →https://doi.org/10.1021/ic00048a037openalex-snapshot
Redox chemistry of superoxide dismutase. Cyclic voltammetry of wild-type enzymes and mutants on functionally relevant residues
inferredcites →https://doi.org/10.1021/j100308a011openalex-snapshot
Further comments on the redox potentials of tryptophan and tyrosine
inferredcites →https://doi.org/10.1021/ja0503985openalex-snapshot
DNA Cleavage by Copper−ATCUN Complexes. Factors Influencing Cleavage Mechanism and Linearization of dsDNA
inferredcites →https://doi.org/10.1021/ja055272mopenalex-snapshot
Targeted Cleavage of HIV Rev Response Element RNA by Metallopeptide Complexes
inferredcites →https://doi.org/10.1021/ja0778038openalex-snapshot
Catalytic Inactivation of Human Carbonic Anhydrase I by a Metallopeptide−Sulfonamide Conjugate is Mediated by Oxidation of Active Site Residues
inferredcites →https://doi.org/10.1021/ja203057zopenalex-snapshot
Targeted Cleavage of HIV RRE RNA by Rev-Coupled Transition Metal Chelates
inferredcites →https://doi.org/10.1021/ja2052599openalex-snapshot
Factors Influencing the DNA Nuclease Activity of Iron, Cobalt, Nickel, and Copper Chelates
inferredcites →https://doi.org/10.1038/nature01370openalex-snapshot
Crystal structure of the human angiotensin-converting enzyme–lisinopril complex
inferredcites →https://doi.org/10.1038/nchembio.333openalex-snapshot
Potent and selective photo-inactivation of proteins with peptoid-ruthenium conjugates
inferredcites →https://doi.org/10.1039/a803477jopenalex-snapshot
Reduction potential of histidine free radicals: a pulse radiolysis study
inferredcites →https://doi.org/10.1039/b813568aopenalex-snapshot
Targeting proteins with metal complexes
inferredcites →https://doi.org/10.1042/bj20040634openalex-snapshot
Evaluation of angiotensin-converting enzyme (ACE), its homologue ACE2 and neprilysin in angiotensin peptide metabolism
inferredcites →https://doi.org/10.1042/bj20050187openalex-snapshot
The N domain of somatic angiotensin-converting enzyme negatively regulates ectodomain shedding and catalytic activity
inferredcites →https://doi.org/10.1042/bj2530287openalex-snapshot
The potential diagram for oxygen at pH 7
inferredcites →https://doi.org/10.1042/bst0361317openalex-snapshot
Albumin as a zinc carrier: properties of its high-affinity zinc-binding site
inferredcites →https://doi.org/10.1073/pnas.19.9.875openalex-snapshot
Oxidation-Reduction Potential of Ascorbic Acid (Vitamin C)
inferredcites →https://doi.org/10.1073/pnas.91.16.7807openalex-snapshot
Naturally occurring active N-domain of human angiotensin I-converting enzyme.
inferredcites →https://doi.org/10.1093/oxfordjournals.jbchem.a134951openalex-snapshot
DNA-Scission Activities of Ascorbate in the Presence of Metal Chelates1
inferredcites →https://doi.org/10.1097/00005344-198600101-00007openalex-snapshot
The Catalytic Mechanism of Angiotensin Converting Enzyme and Related Zinc Enzymes
inferredcites →https://doi.org/10.1124/mol.51.6.1070openalex-snapshot
Substrate Dependence of Angiotensin I-Converting Enzyme Inhibition: Captopril Displays a Partial Selectivity for Inhibition ofN-Acetyl-Seryl-Aspartyl-Lysyl-Proline Hydrolysis Compared with That of Angiotensin I·
inferredcites →https://doi.org/10.1139/v76-185openalex-snapshot
Molecular design to mimic the copper(II) transport site of human albumin. The crystal and molecular structure of copper(II) – glycylglycyl- L -histidine-N-methyl amide monoaquo complex
inferredcites →https://doi.org/10.1146/annurev.bi.62.070193.004053openalex-snapshot
OXIDATION OF FREE AMINO ACIDS AND AMINO ACID RESIDUES IN PROTEINS BY RADIOLYSIS AND BY METAL-CATALYZED REACTIONS
inferredcites →https://doi.org/10.1161/01.cir.90.4.2056openalex-snapshot
Emerging role of angiotensin-converting enzyme inhibitors in cardiac and vascular protection.
inferredcites →https://doi.org/10.1161/01.cir.97.14.1411openalex-snapshot
Angiotensin-Converting Enzyme Inhibitors
inferredcites →https://doi.org/10.1161/01.cir.99.25.3234openalex-snapshot
Long-Term Ascorbic Acid Administration Reverses Endothelial Vasomotor Dysfunction in Patients With Coronary Artery Disease
inferredcites →https://doi.org/10.1161/01.hyp.31.1.362openalex-snapshot
Metabolism of Angiotensin-(1–7) by Angiotensin-Converting Enzyme
inferredcites →https://doi.org/10.1161/01.hyp.31.4.912openalex-snapshot
N-Domain–Specific Substrate and C-Domain Inhibitors of Angiotensin-Converting Enzyme
inferredcites →https://doi.org/10.1161/01.hyp.35.4.936openalex-snapshot
Pharmacological Concentrations of Ascorbic Acid Are Required for the Beneficial Effect on Endothelial Vasomotor Function in Hypertension
inferredcites →https://doi.org/10.1161/01.res.0000081593.33848.fcopenalex-snapshot
Roles of the Two Active Sites of Somatic Angiotensin-Converting Enzyme in the Cleavage of Angiotensin I and Bradykinin
inferredcites →https://doi.org/10.1351/pac200880081799openalex-snapshot
Catalytic metallodrugs
inferredcites →https://doi.org/10.2307/3579271openalex-snapshot
Catalytic Metals, Ascorbate and Free Radicals: Combinations to Avoid

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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N- versus C-Domain Selectivity of Catalytic Inactivation of Human Angiotensin Converting Enzyme by Lisinopril-Coupled Transition Metal Chelates
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