Modulation of endogenous opioid signaling by inhibitors of puromycin-sensitive aminopeptidase. [PDF]
Singh R +8 more
europepmc +1 more source
Beta-amyloid influences the content and trafficking of beta-amyloid precursor protein via Na,K-ATPase-Src kinase positive feedback loop. [PDF]
Petrushanko IY +6 more
europepmc +1 more source
Optimization of Sequential Enzymatic Hydrolysis in Porcine Blood and the Influence on Peptide Profile and Bioactivity of Prepared Hydrolysates. [PDF]
Moreno-Mariscal C +4 more
europepmc +1 more source
Impact of the diverse cardiotonic steroids on beta-amyloid precursor protein level. [PDF]
Petrushanko IY +7 more
europepmc +1 more source
Combating New Delhi metallo-beta-lactamase-1 (NDM-1): an integrated review of inhibitor development and next-generation therapeutic platforms. [PDF]
Mohanty A, Sahoo RK, Sanket AS, Rout E.
europepmc +1 more source
Harder than Metal: Challenging Antimicrobial Resistance with Metallo-β-lactamase Inhibitors. [PDF]
De Falco A +4 more
europepmc +1 more source
Study of thiorphan degradation
International Journal of Pharmaceutics, 1988Abstract The degradation of the enkephalinase inhibitor thiorphan was studied. Liquid chromatography UV and electrochemical detections and several techniques of spectrometry showed that the degradation was oxidative and generates diastereoisomers of the corresponding disulfide.
E Postaire, P Prognon, F Giménez
exaly +2 more sources
Structures of soluble rabbit neprilysin complexed with phosphoramidon or thiorphan [PDF]
Neutral endopeptidase (neprilysin; NEP) is a proteinase that cleaves a wide variety of peptides and has been implicated in Alzheimer's disease, cardiovascular conditions, arthritis and other inflammatory diseases. The structure of the soluble extracellular domain (residues 55–750) of rabbit neprilysin was solved both in its native form at 2.1 Å ...
Jurgen Sygusch, Pawel Grochulski
exaly +3 more sources
Thiorphan and retro-thiorphan display equivalent interactions when bound to crystalline thermolysin
Biochemistry, 1989The three-dimensional structures of (S)-thiorphan and (R)-retro-thiorphan bound to thermolysin have been determined crystallographically and refined to residuals of 0.183 and 0.187 at 1.7-A resolution. Thiorphan [N-[(S)-2-(mercaptomethyl)-1-oxo-3-phenylpropyl]glycine] [HSCH2CH(CH2C6H5)CONHC-H2COOH] and retro-thiorphan [[[(R)-1-(mercaptomethyl)-2 ...
S L, Roderick +3 more
openaire +3 more sources

