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Journal Article|Research Support, N.I.H., Extramural |
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11443 |
issn |
0006-2960 1520-4995 |
issueIdentifier |
38 |
pageRange |
11432-11443 |
publicationName |
Biochemistry |
startingPage |
11432 |
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bibliographicCitation |
Vineyard D, Zhang X, Lee I. Transient kinetic experiments demonstrate the existence of a unique catalytic enzyme form in the peptide-stimulated ATPase mechanism of Escherichia coli Lon protease. Biochemistry. 2006 Sep 26;45(38):11432–43. doi: 10.1021/bi060809+. PMID: 16981703. |
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date |
2006-08-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
identifier |
https://doi.org/10.1021/bi060809%2B https://pubmed.ncbi.nlm.nih.gov/16981703 |
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language |
English |
source |
https://pubmed.ncbi.nlm.nih.gov/ https://www.crossref.org/ |
title |
Transient Kinetic Experiments Demonstrate the Existence of a Unique Catalytic Enzyme Form in the Peptide-Stimulated ATPase Mechanism of Escherichia coli Lon Protease |
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