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Crystal structure of the human angiotensin-converting enzyme–lisinopril complex
27/27 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
3 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 27 checked references that resolve
resolves10.1021/bi00644a014
Design of potent competitive inhibitors of angiotensin-converting enzyme. Carboxyalkanoyl and mercaptoalkanoyl amino acids
resolves10.1073/pnas.051633198
Structure of neurolysin reveals a deep channel that limits substrate access
resolves10.1016/S0969-2126(02)00698-6
Crystal Structure of a Novel Carboxypeptidase from the Hyperthermophilic Archaeon Pyrococcus furiosus
resolves10.1073/pnas.85.24.9386
Two putative active centers in human angiotensin I-converting enzyme revealed by molecular cloning.
resolves10.1016/S0021-9258(18)43897-5
Identification of two active site residues in human angiotensin I-converting enzyme.
resolves10.1016/S0021-9258(18)42224-7
The two homologous domains of human angiotensin I-converting enzyme interact differently with competitive inhibitors.
resolves10.1172/JCI119419
The critical role of tissue angiotensin-converting enzyme as revealed by gene targeting in mice.
resolves10.1073/pnas.86.20.7741
Molecular cloning of human testicular angiotensin-converting enzyme: the testis isozyme is identical to the C-terminal half of endothelial angiotensin-converting enzyme.
resolves10.1074/jbc.272.6.3511
Identification of N-Linked Glycosylation Sites in Human Testis Angiotensin-converting Enzyme and Expression of an Active Deglycosylated Form
resolves10.1016/S0006-291X(02)02324-0
Defining the boundaries of the testis angiotensin I-converting enzyme ectodomain
resolves10.1021/bi00243a012
Angiotensin-converting enzyme: zinc- and inhibitor-binding stoichiometries of the somatic and testis isozymes
resolves10.1021/bi00285a021
Anion activation of angiotensin converting enzyme: dependence on nature of substrate
resolves10.1016/S0021-9258(18)98378-X
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
resolves10.1074/jbc.M101495200
Arg1098 Is Critical for the Chloride Dependence of Human Angiotensin I-converting Enzyme C-domain Catalytic Activity
resolves10.1016/0196-9781(84)90020-2
Hydrolysis of substance P and neurotensin by converting enzyme and neutral endopeptidase
resolves10.1016/0006-291X(90)91766-L
A deeply recessed active site in angiotensin-converting enzyme is indicated from the binding characteristics of biotin-spacer-inhibitor reagents
resolves10.1016/0006-291X(78)91382-7
Functional residues at the active site of angiotensin converting enzyme
resolves10.1016/S0076-6879(97)76066-X
[20] Processing of X-ray diffraction data collected in oscillation mode
resolves10.1016/S0076-6879(97)76073-7
[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
resolves10.1107/S0907444995008754
Methods used in the structure determination of bovine mitochondrial F1 ATPase
resolves10.1107/S0907444998003254
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
resolves10.1002/prot.340110407
Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
The 3 references without a DOI — listed, not checked
no DOI — not checkedJunot, C. et al. RXP 407, a selective inhibitor of the N-domain of angiotensin I-converting enzyme, blocks in vivo the degradation of hemoregulatory peptide acetyl-Ser-Asp-Lys-Pro with no effect on angiotensin I hydrolysis. J. Pharmacol. Exp. Ther. 297, 606–611 (2001)
no DOI — not checkedCorvol, P. & Williams, T. A. in Handbook of Proteolytic Enzymes (eds Barrett, A. J., Rawlings, N. D. & Woessner, J. F.) 1066–1076 (Academic, London, 1998)
no DOI — not checkedPatchett, A. A. & Cordes, E. H. The design and properties of N-carboxyalkyldipeptide inhibitors of angiotensin converting enzyme. Adv. Enzymol. 57, 1–84 (1985)
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