Search results for "ALPHAS"

showing 3 items of 23 documents

"Table 8" of "Measurement of electroweak parameters from Z decays into Fermion pairs"

1990

No description provided.

SINTW88.227E+ E- --> Z0E+ E- ScatteringGAALPHASExclusiveE+ E- --> LEPTON+ LEPTON-GV
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A previously unreported numph cocoon of Alphasida puncticollis on the islet of Lampione (Sicilian Channel) (Coleoptera Tenebrionidae).

2010

In this paper we present an unusual case of cocoons produced by larvae of Tenebrionid Alphasida (Glabrasida) puncticollis (Solier, 1836), which has been observed on the islet of Lampione (Sicilian Channel). Pupal cocoons have never been recorded for species belonging to this genus, and their occurrence results rarely documented within the family Tenebrionidae. Some ecological implications are discussed.

Settore AGR/11 - Entomologia Generale E Applicatapupal biology nymph cocoon Alphasida puncticollis Coleoptera Tenebrionidae Pelagie Islands
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Formation of covalent di-tyrosine dimers in recombinant α-synuclein

2015

Parkinson's disease is associated with fibril deposition in the diseased brain. Misfolding events of the intrinsically disordered synaptic protein α-synuclein are suggested to lead to the formation of transient oligomeric and cytotoxic species. The etiology of Parkinson's disease is further associated with mitochondrial dysfunction and formation of reactive oxygen species. Oxidative stress causes chemical modification of native α-synuclein, plausibly further influencing misfolding events. Here, we present evidence for the spontaneous formation of covalent di-tyrosine α-synuclein dimers in standard recombinant protein preparations, induced without extrinsic oxidative or nitrative agents. The…

chemistry.chemical_classificationReactive oxygen speciesParkinson's diseasealphasynucleinamyloids di-tyrosine dimers EOM Parkinson’s disease SAXSSAXSOxidative phosphorylationFibrilmedicine.disease_causeIndustrial and Manufacturing Engineeringchemistry.chemical_compoundα-synucleinMonomerchemistryBiochemistryCovalent bondmedicinedi-tyrosine dimersamyloidsTyrosineProtein secondary structureEOMOxidative stressResearch PaperIntrinsically Disordered Proteins
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