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Adriana K. Carmona | doi.page

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Adriana K. Carmona

Universidade Federal de São Paulo(BR)

Publications by Year

Research Areas

Peptidase Inhibition and Analysis, Coagulation, Bradykinin, Polyphosphates, and Angioedema, Protease and Inhibitor Mechanisms, Renin-Angiotensin System Studies, Protein Hydrolysis and Bioactive Peptides

Most-Cited Works

→ Aerobic Exercise Training–Induced Left Ventricular Hypertrophy Involves Regulatory MicroRNAs, Decreased Angiotensin-Converting Enzyme-Angiotensin II, and Synergistic Regulation of Angiotensin-Converting Enzyme 2-Angiotensin (1-7)(2011)251 cited
→ Chlorhexidine Inhibits the Activity of Dental Cysteine Cathepsins(2012)233 cited
→ Peptidase Specificity Characterization of C- and N-Terminal Catalytic Sites of Angiotensin I-Converting Enzyme(2000)159 cited
→ Proteolytic processing of osteopontin by PHEX and accumulation of osteopontin fragments in Hyp mouse bone, the murine model of X-linked hypophosphatemia(2012)142 cited
→ Sex Hormones Promote Opposite Effects on ACE and ACE2 Activity, Hypertrophy and Cardiac Contractility in Spontaneously Hypertensive Rats(2015)136 cited
→ ACE2–angiotensin-(1–7)–Mas axis in renal ischaemia/reperfusion injury in rats(2010)113 cited

→ A continuous fluorescence resonance energy transfer angiotensin I-converting enzyme assay(2006)

100 cited

→ Human recombinant endopeptidase PHEX has a strict S1' specificity for acidic residues and cleaves peptides derived from fibroblast growth factor-23 and matrix extracellular phosphoglycoprotein(2003)98 cited

→ Positional-scanning combinatorial libraries of fluorescence resonance energy transfer peptides to define substrate specificity of carboxydipeptidases: assays with human cathepsin B(2004)91 cited

→ Biochemical characterization of human cathepsin X revealed that the enzyme is an exopeptidase, acting as carboxymonopeptidase or carboxydipeptidase(2000)89 cited