Results 121 to 130 of about 4,495 (158)
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Seventh Conference Real Time '91 on Computer Applications in Nuclear, Particle and Plasma Physics Conference Record, 2005
The author recals the earliest days of CAMAC development. He notes that in 5 years CAMAC was fully designed and had become a European and American Standard and was later recommended for world-wide use by the International Electrotechnical Commission.
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The author recals the earliest days of CAMAC development. He notes that in 5 years CAMAC was fully designed and had become a European and American Standard and was later recommended for world-wide use by the International Electrotechnical Commission.
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Primary structure and evolution of calcium-activated neutral protease (CANP)
Journal of Protein Chemistry, 1987The amino acid sequences of two subunits (80K and 30K) of calcium-activated neutral protease (CANP) were examined to clarify the structure-function relationship of CANP. The 80K subunit is composed of four clear domains (I–IV from the N-terminus). Domain II is a cysteine proteinase domain homologous to cathepsins B, L, and H.
K. Suzuki +4 more
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Ending remarks from the CANPS chair
2010 17th IEEE-NPSS Real Time Conference, 2010The 17th IEEE Real Time Conference (RT10) took place on May 23–28 at the heart of Lisbon, Portugal, in the Instituto Superior Tecnico in Lisbon. It was organized by the Instituto de Plasmas e Fusoo Nuclear (IPFN) together with the Laboratorio de Instrumentacoo e Fisica Experimental de Particulas (LIP).
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Investigations on spectroscopic and elasticity studies of Nd2O3 doped CANP phosphate glasses
Journal of Alloys and Compounds, 2017Quaternary phosphate glasses CoO - Al2O3 - Na2O - P2O5 (CANP) doped with – different concentrations of Nd2O3 had prepared and studied by FTIR, ultrasonic parameters and UV–Vis–NIR techniques. The Judd-Ofelt theory has applied to describe the absorption and luminescence spectra of Nd3+ ions in these glasses.
Yasser B. Saddeek +4 more
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Limited Autolysis of Ca2+-Activated Neutral Protease (CANP) Changes Its Sensitivity to Ca2+ Ions
The Journal of Biochemistry, 1981Ca2+-activated neutral protease (CANP) usually requires mM Ca2+ for activation. The sensitivity of CANP to Ca2+ is greatly enhanced by passing it through a casein-Sepharose column in the presence of Ca2+ ions. This conversion is ascribed to autolysis of CANP. The converted enzyme required 40 microM Ca2+ for 50% activation.
K, Suzuki +4 more
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Journal of Comparative Neurology, 1990
AbstractIntracellular accumulation of Ca2+ after brain ischemia is regarded as one of the principal causes of neuronal death, but details of the intracellular events occurring after Ca2+ accumulation have not yet been described. We propose that a calcium‐activated neutral proteinase which can degrade neuronal cytoskeletal proteins might link Ca2 ...
T, Fukuda +4 more
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AbstractIntracellular accumulation of Ca2+ after brain ischemia is regarded as one of the principal causes of neuronal death, but details of the intracellular events occurring after Ca2+ accumulation have not yet been described. We propose that a calcium‐activated neutral proteinase which can degrade neuronal cytoskeletal proteins might link Ca2 ...
T, Fukuda +4 more
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Calcium-Activated Neutral Protease (CANP) and its Biological and Medical Implications
1987Calcium activated neutral protease (CANP) apparently participates in a variety of cellular functions mediated by Ca2 +. The primary, structure of CANP reveals a novel domain structure comprising domains highly homologous to papain-like cysteine proteinases and calmodulin-like Ca2+ binding proteins, and a glycine-rich hydrophobic domain that interacts ...
Koichi Suzuki +4 more
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Neurochemical Research, 1988
A calcium-activated neutral proteinase was purified from myelin of bovine brain white matter. Myelin purified in the presence of EDTA (2 mM) was homogenized in 50 mM Trisacetate buffer at pH 7.5, containing 4 mM EDTA, 1 mM NaN3, 5 mM beta-mercaptoethanol and 0.1% Triton X-100 for two hours.
A K, Chakrabarti, N L, Banik
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A calcium-activated neutral proteinase was purified from myelin of bovine brain white matter. Myelin purified in the presence of EDTA (2 mM) was homogenized in 50 mM Trisacetate buffer at pH 7.5, containing 4 mM EDTA, 1 mM NaN3, 5 mM beta-mercaptoethanol and 0.1% Triton X-100 for two hours.
A K, Chakrabarti, N L, Banik
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Biochemical and Biophysical Research Communications, 1988
Kyotorphin (Tyr-Arg) accumulation in the dialysed synaptosol from the rat brain in the presence of an inhibitor of kyotorphin-degrading enzyme, was maximal at neutral pH. This accumulation was activated by calcium ions, but was inhibited by leupeptin and SH-blocking agents, a finding which suggests the involvement of calcium-activated neutral protease (
Y, Yoshihara +4 more
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Kyotorphin (Tyr-Arg) accumulation in the dialysed synaptosol from the rat brain in the presence of an inhibitor of kyotorphin-degrading enzyme, was maximal at neutral pH. This accumulation was activated by calcium ions, but was inhibited by leupeptin and SH-blocking agents, a finding which suggests the involvement of calcium-activated neutral protease (
Y, Yoshihara +4 more
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