Results 311 to 320 of about 26,327 (353)
Some of the next articles are maybe not open access.

Tat peptides inhibit neprilysin

Journal of Neurovirology, 2006
Dementia associated with human immunodeficiency virus (HIV) infection occurs commonly in the aging population and amyloid depositions are noted in the brains of patients with HIV infection in younger age groups. This suggests a dysregulation of amyloid processing in the setting of HIV infection.
Abigail Daily   +2 more
openaire   +3 more sources

Neprilysin: Indications, Expectations, and Challenges

Revista Española de Cardiología (English Edition), 2016
La neprilisina ha pasado a ser uno de los centros de interes en cardiologia, debido a los impresionantes beneficios que se han demostrado con la combinacion de una inhibicion de la neprilisina y un antagonismo de los receptores de la angiotensina en el reciente ensayo clinico PARADIGM-HF, en el que se evaluo el empleo de LCZ696 (denominado ahora ...
Antoni Bayes-Genis, Josep Lupón
openaire   +3 more sources

Neuroendocrine Differentiation, Neuropeptides, and Neprilysin

American Journal of Respiratory Cell and Molecular Biology, 1999
Pulmonary neuroendocrine cells exhibit highly specialized differentiation with a neurosecretory phenotype and significant bioactive peptide hormone content. In addition to these functions, pulmonary neuroendocrine cells have been demonstrated to act as chemoreceptors for hypoxia (1).
Andrea J. Cohen, York E. Miller
openaire   +3 more sources

Neprilysin Inhibitors in Cardiovascular Disease

Current Cardiology Reports, 2017
Mortality from heart failure remains high despite advances in medical therapy over the last three decades. Angiotensin receptor-neprilysin inhibitor (ARNI) combinations are the latest addition to the heart failure medical armamentarium, which is built on the cornerstone regimen of beta blockers, angiotensin converting enzyme (ACE) inhibitors ...
Dipanjan Banerjee, Guson Kang
openaire   +3 more sources

The Neprilysin Family in Health and Disease

2006
The mammalian neprilysin (NEP) family comprises at least seven members: NEP itself, Kell blood group antigen (KELL), the endothelin-converting enzymes (ECE-1 and ECE-2), the enzyme PEX, associated with X-linked hypophosphataemia, "X-converting enzyme" (XCE) a CNS-expressed orphan peptidase and a soluble, secreted endopeptidase (SEP).
Carolyn D. Brown   +3 more
openaire   +3 more sources

Cell-specific activity of neprilysin 2 isoforms and enzymic specificity compared with neprilysin

Biochemical Journal, 2002
Neprilysin (NEP) 2 is a recently cloned glycoprotein displaying a high degree of sequence identity with neprilysin (EC 3.4.24.11), the prototypical member of the M13 subfamily of metalloproteases. Whereas NEP is involved in the metabolism of several bioactive peptides by plasma membranes of various cells, the enzymic properties and physiological ...
Jean-Charles Schwartz   +4 more
openaire   +2 more sources

Degradation of tropoelastin and skin elastin by neprilysin

Biochimie, 2018
Neprilysin is also known as skin fibroblast-derived elastase, and its up-regulation during aging is associated with impairments of the elastic fiber network, loss of skin elasticity and wrinkle formation. However, information on its elastase activity is still limited. The aim of this study was to investigate the degradation of fibrillar skin elastin by
Chiara Luise   +7 more
openaire   +4 more sources

Neprilysin activity and expression are controlled by nicastrin

Journal of Neurochemistry, 2006
AbstractWe recently demonstrated that the presenilin‐dependent γ‐secretase complex regulates the expression and activity of neprilysin, one of the main enzymes that degrade the amyloid β‐peptide (Aβ) which accumulates in Alzheimer's disease. Here, we examined the influence of endogenous nicastrin (NCT), a member of the γ‐secretase complex, on ...
P. St. George-Hyslop   +5 more
openaire   +3 more sources

Neprilysin and Amyloid Beta Peptide Degradation

Current Alzheimer Research, 2008
Neprilysin is a zinc metalloendopeptidase with relatively broad substrate specificity. The enzyme is localized to the plasma membrane of cells where it can function to degrade extracellular peptides. Structural studies show that neprilysin preferentially cleaves peptides on the amino side of hydrophobic amino acids.
Louis B. Hersh, David W. Rodgers
openaire   +3 more sources

Endopeptidase-24.11 (Neprilysin) and Relatives [PDF]

open access: possible, 1996
The renal and intestinal brush border membranes are an abundant source of peptidase and proteinase activities, most of which are zinc metalloenzymes (see e.g. Kenny et al., 1987). These membranes have proved valuable as starting material for purification of these enzymes as well as for investigating their likely physiological functions.
Leonard J. Murphy   +3 more
openaire   +1 more source

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