scholarly article | Q13442814 |
P819 | ADS bibcode | 1979PNAS...76.6216H |
P356 | DOI | 10.1073/PNAS.76.12.6216 |
P953 | full work available at URL | https://europepmc.org/articles/PMC411834 |
https://europepmc.org/articles/PMC411834?pdf=render | ||
https://pnas.org/doi/pdf/10.1073/pnas.76.12.6216 | ||
P932 | PMC publication ID | 411834 |
P698 | PubMed publication ID | 230502 |
P5875 | ResearchGate publication ID | 22905993 |
P2093 | author name string | B. L. Vallee | |
B. Holmquist | |||
P2860 | cites work | Protein measurement with the Folin phenol reagent | Q20900776 |
Electronic properties of sulfhydryl- and imidazole-containing peptide-cobalt(II) complexes: their relationship to cobalt(II)-substituted "blue" copper proteins | Q28326931 | ||
Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids | Q34089278 | ||
Binding of the by-product analog benzylsuccinic acid by carboxypeptidase A | Q34217732 | ||
Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysis | Q34376750 | ||
Transition state analog inhibitors and enzyme catalysis | Q39106066 | ||
Reaction of peptide aldehydes with serine proteases. Implications for the entropy changes associated with enzymic catalysis | Q39653987 | ||
Carboxypeptidase of Streptomyces griseus. Implications of its characteristics | Q39653990 | ||
Metal stoichiometry, coenzyme binding, and zinc and cobalt exchange in highly purified yeast alcohol dehydrogenase | Q40121564 | ||
Cobalt exchange in horse liver alcohol dehydrogenase | Q40169645 | ||
A continuous spectrophotometric assay for angiotensin converting enzyme | Q40235334 | ||
Magnetic circular dichroic spectra of cobalt(II) substituted metalloenzymes | Q40315119 | ||
Characterization of the "microprotease" from Bacillus cereus. A zinc neutral endoprotease | Q41326672 | ||
Design of potent and specific inhibitors of carboxypeptidases A and B | Q41482450 | ||
Purification and crystallization of human carboxypeptidase A | Q41519531 | ||
Inhibition of thermolysin and carboxypeptidase A by phosphoramidates | Q41725271 | ||
Intramolecular and divalent metal ion catalysis. Hydrolytic mechanism of O-phenyl N-(glycyl)phosphoramidate | Q42234393 | ||
Metal cofactor requirements of beta-lactamase II | Q42584980 | ||
Preparation and properties of cobalt(II) rubredoxin | Q43619010 | ||
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Use of peptide aldehydes to generate transition-state analogs of elastase | Q44335259 | ||
Metal Substitutions and Inhibition of Thermolysin: Spectra of the Cobalt Enzyme | Q47851666 | ||
Infrared and visible circular dichroism and magnetic circular dichroism studies on cobalt (II)-substituted blue copper proteins. | Q50955738 | ||
Enzymatic Catalysis and the Transition State Theory of Reaction Rates: Transition State Analogs | Q52995860 | ||
Angiotensin I-converting enzyme of the kidney cortex. | Q54600740 | ||
The structure of carboxypeptidase A. VII. The 2.0-angstrom resolution studies of the enzyme and of its complex with glycyltyrosine, and mechanistic deductions. | Q55062003 | ||
Peptide hydroxamic acids as inhibitors of thermolysin | Q67375686 | ||
Synthetic analogues of the active sites of iron-sulfur proteins. 14. Synthesis, properties, and structures of bis(o-xylyl-alpha,alpha'-dithiolato)ferrate(II, III) anions, analogues of oxidized and reduced rubredoxin sites | Q67537627 | ||
Letter: A thermolysin inhibitor produced by Actinomycetes: phospholamidon | Q69687907 | ||
Spectral properties of cobalt carboxypeptidase. Effects of substrates and inhibitors | Q70729747 | ||
2-phenylethaneboronic acid, a possible transition-state analog for chymotrypsin | Q71790019 | ||
Contamination in trace element analysis and its control | Q74789515 | ||
P433 | issue | 12 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 6216-6220 | |
P577 | publication date | 1979-12-01 | |
P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
P1476 | title | Metal-coordinating substrate analogs as inhibitors of metalloenzymes | |
P478 | volume | 76 |
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