A5051707864- Coagulation, Bradykinin, Polyphosphates, and Angioedema
- Renin-Angiotensin System Studies
- Computational Drug Discovery Methods
- Enzyme function and inhibition
- Receptor Mechanisms and Signaling
- Peptidase Inhibition and Analysis
- 3D Printing in Biomedical Research
- Chemical Synthesis and Analysis
- Monoclonal and Polyclonal Antibodies Research
- Neuropeptides and Animal Physiology
- Digestive system and related health
- Biochemical and Structural Characterization
- Protein Structure and Dynamics
- Bone and Dental Protein Studies
- Angiogenesis and VEGF in Cancer
- SARS-CoV-2 and COVID-19 Research
- Cancer Cells and Metastasis
- Cell Adhesion Molecules Research
- Protease and Inhibitor Mechanisms
- Viral Infectious Diseases and Gene Expression in Insects
- Hormonal Regulation and Hypertension
- Steroid Chemistry and Biochemistry
- Health, Environment, Cognitive Aging
University of Cape Town
2013-2022
Florida College
2022
University of Florida
2022
Uppsala University
2022
University of Houston
2022
Australian Regenerative Medicine Institute
2022
Monash University
2022
Maastricht University
2022
University of Southern Denmark
2022
Charité - Universitätsmedizin Berlin
2022
Angiotensin-1-converting enzyme (ACE) is a key in the renin-angiotensin-aldosterone and kinin systems where it cleaves angiotensin I bradykinin peptides, respectively. However, ACE also participates numerous other physiological functions, can hydrolyse many peptide substrates has various exo- endopeptidase activities. achieves this complexity by containing two homologous catalytic domains (N- C-domains), which exhibit different substrate specificities. Here, we present first open...
ACE (angiotensin-1-converting enzyme) is a zinc metallopeptidase that plays prominent role in blood pressure regulation and electrolyte homeostasis. consists of two homologous domains despite similarities sequence topology display differences substrate processing inhibitor binding. The design inhibitors selectively inhibit the N-domain (N-selective) could be useful treating conditions tissue injury fibrosis due to build-up N-domain-specific Ac-SDKP (N-acetyl-Ser–Asp–Lys–Pro). Using...
Abstract Hypertension (high blood pressure) is a major risk factor for cardiovascular disease, which the leading cause of death worldwide. The somatic isoform angiotensin I‐converting enzyme (sACE) plays critical role in pressure regulation, and ACE inhibitors are thus widely used to treat hypertension disease. Our current understanding sACE structure, dynamics, function, inhibition has been limited because truncated, minimally glycosylated forms typically X‐ray crystallography molecular...
Angiotensin‐1‐converting enzyme ( ACE ) is a zinc metalloprotease that plays major role in blood pressure regulation via the renin–angiotensin–aldosterone system. consists of two domains with differences inhibitor binding affinities despite their 90% active site identity. While C‐domain primarily controls pressure, N‐domain selective for cleavage antifibrotic N ‐acetyl‐Ser–Asp–Lys–Pro. Inhibitors, such as 33 RE , selectively bind to thus show potential treating fibrosis without affecting...
Abstract Angiotensin-converting enzyme (ACE) is a zinc metalloprotease best known for its role in blood pressure regulation. ACE consists of two homologous catalytic domains, the N- and C-domain, that display distinct but overlapping functions vivo owing to subtle differences substrate specificity. While current generation inhibitors target both domain-selective may be clinically advantageous, either reducing side effects or having utility new indications. Here, we used site-directed...
Angiotensin-converting enzyme (ACE) is best known for its formation of the vasopressor angiotensin II that controls blood pressure but also involved in other physiological functions through hydrolysis a variety peptide substrates. The contains two catalytic domains (nACE and cACE) have different affinities ACE substrates inhibitors. We investigated whether nACE inhibitor backbones contain unique property which allows them to take advantage hinging nACE. Kinetic analysis showed mutation...
Angiotensin I-converting enzyme (ACE, CD143) plays a crucial role in blood pressure regulation, vascular remodeling, and immunity. A wide spectrum of mAbs to different epitopes on the N C domains human ACE have been generated used study aspects biology, including establishing novel approach-conformational fingerprinting. Here we characterized set 14 mAbs, developed against seminal fluid ACE. The for these were defined using recombinant constructs with truncated domains, species...
Angiotensin converting enzyme (ACE) is one of the key targets current antihypertensive therapy with ACE inhibitors being four recommended first-line therapies 1 .In some patients, however, trigger adverse effects such as persistent cough (5-20%) 2 or angioedema (0.1-0.7%) 3 .Current non-selectively block both domains and thereby lead to bradykinin accumulation angioedema.The two are catalytically active but differ in physiological function C-and N-terminal respectively responsible for blood...
Objective: Angiotensin-1-converting enzyme (ACE) is a zinc metallopeptidase that well known for its role in cardiovascular physiology. Through cleavage of peptides angiotensin I and bradykinin, ACE involved the renin-angiotensin-aldosterone kinin systems, respectively. However, also catalyses variety substrates, thus participates numerous other physiological functions. The aim this study was to investigate hinging mechanism molecular basis hydolysis wide range substrates with exo-...