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Human testis angiotensin-converting enzyme: Crystal structure of a glycosylation mutant and investigation of a putative hinge-mechanism by normal mode analysis.Watermeyer, Jean Margaret January 2004 (has links)
Human angiotensin-converting enzyme (ACE) is a key enzyme in the regulation of blood pressure via the renin-angiotensin and kallikrein-kinin systems. A number of orally active drugs have been developed over the years that target somatic ACE, for the treatment of hypertension, myocardial infarction and congestive heart failure. Protein structural information about ACE is an important key for the understanding of the mechanism and substrate-specificity of the enzyme. However, this information has only begun to be elucidated in the past year, with the solution of crystal structures of human testis ACE (tACE), and homologues Drosophila AnCE and human ACE2. tACE is identical to the C-terminal domain of somatic ACE, which consists of two homologous domains, each having a slightly different substrate-specificity. This thesis describes the purification, crystallisation and X-ray crystal structure-determination of a glycosylation-deficient mutant of tACE, tACEG1,3, to 2.9 Å / .
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Human testis angiotensin-converting enzyme: Crystal structure of a glycosylation mutant and investigation of a putative hinge-mechanism by normal mode analysis.Watermeyer, Jean Margaret January 2004 (has links)
Human angiotensin-converting enzyme (ACE) is a key enzyme in the regulation of blood pressure via the renin-angiotensin and kallikrein-kinin systems. A number of orally active drugs have been developed over the years that target somatic ACE, for the treatment of hypertension, myocardial infarction and congestive heart failure. Protein structural information about ACE is an important key for the understanding of the mechanism and substrate-specificity of the enzyme. However, this information has only begun to be elucidated in the past year, with the solution of crystal structures of human testis ACE (tACE), and homologues Drosophila AnCE and human ACE2. tACE is identical to the C-terminal domain of somatic ACE, which consists of two homologous domains, each having a slightly different substrate-specificity. This thesis describes the purification, crystallisation and X-ray crystal structure-determination of a glycosylation-deficient mutant of tACE, tACEG1,3, to 2.9 Å / .
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The mechanism of action of captopril in human renal cell carcinoma /Reid, Janet Louise. January 2003 (has links) (PDF)
Thesis (Ph.D.) - University of Queensland, 2003. / Includes bibliography.
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Human testis angiotensin-converting enzyme: crystal structure of a glycosylation mutant and investigation of a putative hinge-mechanism by normal mode analysisWatermeyer, Jean Margaret January 2004 (has links)
Magister Scientiae - MSc / Human angiotensin-converting enzyme (ACE) is a key enzyme in the
regulation of blood pressure via the renin-angiotensin and kallikrein-kinin
systems. A number of orally active drugs have been developed over the
years that target somatic ACE, for the treatment of hypertension, myocardial
infarction and congestive heart failure. Protein structural information about
ACE is an important key for the understanding of the mechanism and
substrate-specificity of the enzyme. However, this information has only
begun to be elucidated in the past year, with the solution of crystal structures
of human testis ACE (tACE), and homologues Drosophila AnCE and
human ACE2. tACE is identical to the C-terminal domain of somatic ACE,
which consists of two homologous domains, each having a slightly different
substrate-specificity.
This thesis describes the purification, crystallisation and X-ray crystal
structure-determination of a glycosylation-deficient mutant of tACE, tACEG1,3,
to 2.9 Å. The structure of tACE-G1,3 aligns closely with that of
native tACE, indicating that the mutations did not alter the conformation.
The ability to achieve minimal glycosylation of tACE for crystallisation
purposes via mutation, rather than using expensive glycosidase inhibitors,
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should prove advantageous for further structural studies, such as the study of
the binding of novel inhibitors.
In all of the tACE structures thus far observed, the active site is closed off
from the external medium in a deep cleft, so that it is unclear how a large
substrate molecule could gain access. However, a hinge motion that opens
this cleft has been observed in the structures of ACE2. Temperature factor
and sequence comparison between tACE, tACE-G1,3, AnCE and ACE2
suggests the functional conservation of three flexible loop regions, as well as
the sequence conservation of three constrained regions, involved in the
hinge. Normal mode analysis reveals the intrinsic flexibility of tACE, and
further suggests that a putative open form of tACE would behave similarly
to the open form of ACE2. Based on these indications, a conservation of the
ACE2 hinge-bending mechanism is proposed.
Temperature factor analysis also reveals that subdomain II, containing
bound chloride ions, is more structurally rigid than subdomain I, in all
structures considered.
Based on these results, lines of investigation are suggested that should yield
insight into the mechanisms of action of ACE and its association with
various substrates and inhibitors, ideally aiding in the development of novel
drugs for the treatment of cardiac disease. / South Africa
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The estimation of renin in biological fluidsLee, Michael R. January 1965 (has links)
No description available.
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Formation of drug-protein conjugates from captoprilYeung, J. H. K. January 1984 (has links)
No description available.
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Ligand binding studies of Drosophila angiotensin converting enzymes and mouse major urinary proteinBingham, Richard Jonathan January 2003 (has links)
No description available.
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The interaction of thiopeptides with angiotensin converting enzyme : synthesis, conformation, and enzymologyMaziak, Louise Ann. January 1984 (has links)
No description available.
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Utilization of Angiotensin-Converting-Enzyme Inhibitors in the Treatment of Diabetics Within an Out-Patient Care FacilityTitus, Timothy January 2005 (has links)
Class of 2005 Abstract / Objective: The purpose of this study was to retrospectively determine if individuals within the SAVAHCS home-based patient population with a diagnosis of diabetes mellitus are receiving an angiotensin-converting-enzyme inhibitor (ACE-I) based on recent evidence supporting its use in these patients.
Research Design: A retrospective, chart review of 41 patients with a diagnosis of diabetes mellitus from November 1, 2004 to December 31, 2005.
Methodology: This was a retrospective, chart review of all patients within the SAVAHCS home-based population with an active diagnosis of diabetes mellitus. Once the patients were identified, their clinical profiles were extracted from the VISTA computer system. The patients had data regarding age, gender, diabetes type, diagnoses of heart disease and hypertension, type of ACE- Inhibitor prescribed, blood pressure, HgbA1c, and height and weight in order to calculate body mass index (BMI). The patients were classified as either having or not having ACE-Inhibitor therapy.
Results: The total number of diabetic patients currently receiving an ACE-Inhibitor was 24 (58.5%). This was significantly lower than the value of 80% predetermined (p=0.0352). Thirty-one patients were also found to have a diagnosis of hypertension (75.6%), with 18 of these patients having a prescription for an ACE-Inhibitor (43.9%). Four patients (9.8%) who were not currently on an ACE- Inhibitor had a documented history of cough induced by the use of these drugs.
Clinical Relationships: ACE-Inhibitors are drug agents used to treat hypertension. They have also been shown to be of significant clinical value in diabetic patients, in both renal protective effects as well as to reduce cardiovascular risk, the most common cause of morbidity and mortality in diabetic patients.
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Angiotensin Converting Enzyme Inhibitor Cough: A Review of Characteristics, Frequency, Mechanism, and TreatmentSulzbach, Robert M. January 2008 (has links)
Class of 2008 Abstract / Objectives: : The purpose of this paper is to provide greater understanding of ACE inhibitor cough and appropriate treatment options.
Methods: A Medline search of key terms from 1975-2008 was conducted and all types of published material were included in this review. The articles were evaluated for relevance and appropriateness for inclusion in this review. Subjects considered appropriate included ACE inhibitor cough treatment, mechanism of action, incidence and prevalence, genetics, cough characteristics, onset and resolution of cough, and others. Whenever possible, original studies were obtained but several reviews were also used.
Results: ACE inhibitor cough is typically a dry, non-productive, persistent but benign cough reportedly occurring in anywhere from 0.5%-50% of patients receiving ACE inhibitors, though most studies indicate less than 20%. The mechanism is not completely understood but seems to be related to a complicated mechanism involving pathways caused by ACE inhibition and including bradykinin, C fibers, and prostaglandins. Several treatment options have been successful in resolving or relieving cough, including NSAIDs, baclofen, cromolyn and others. Results, however, are inconsistent. Anti-tussive agents, switching to a different ACE inhibitor, or lowering the dose of the current ACE inhibitor do not seem to be effective.
Conclusions: In spite of its benign nature, ACE inhibitor cough is usually bothersome enough to discontinue the medication and therefore can not be ignored. Several treatments have appeared effective, all of which carry the risk of drug interactions and additional side effects, and alternative therapy such as angiotensin receptor blockers seem to be reasonable in indicated patients.
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