Publications by authors named "M Golinelli"

We describe a case of Horner syndrome occurring secondary only to the high insertion of a chest tube after video-thoracoscopic apicectomy for spontaneous pneumothorax. Because all other causes could be ruled out, the Authors assume that the lesion to the sympathetic nerve fibres was caused by pressure exerted by the tip of the chest tube. Horner syndrome due to this cause can easily be avoided.

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Background: Intracranial haemorrhage (ICH) is the type of stroke associated with the highest death rate, and about 30% of ICH occurs in patients on antithrombotic treatment. This study relates clinical presentations and outcome of ICH patients on oral anticoagulant (OA) or antiplatelet (AP) therapy admitted to 33 Italian emergency departments (ED).

Methods: Consecutive patients were enrolled after cranial computed tomography (CT).

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We studied the effects of human immunodeficiency virus type 1 (HIV-1) nucleocapsid (NC) protein on the kinetics of annealing of nucleic acids using model substrates derived from the 3' end of the HIV-1 minus-strand strong-stop DNA (-sssDNA). We used HIV-1 reverse transcriptase (RT) to monitor the annealing reaction. Using several different DNA primers and acceptor oligonucleotides, we found that the rate of annealing increased with the size of the complementary region of the primer and the acceptor strands and decreased when secondary structures could be formed in either the primer or the acceptor strands.

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We studied the kinetics of nontemplated nucleotide addition by the reverse transcriptase (RT) of human immunodeficiency virus type 1 (HIV-1) using model substrates derived from the 3' end of HIV-1 minus-strand strong-stop DNA. The addition of a nontemplated nucleotide was highly dependent on the nature of the base (fastest addition with dATP), type of nucleoside, and pH of the reaction buffer. The salt concentration, presence or absence of nucleocapsid protein, and nature of the blunt-ended duplex (DNA/DNA versus RNA/DNA) had only limited effects.

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The Escherichia coli DNA repair enzyme MutY plays an important role in the recognition and repair of 7,8-dihydro-8-oxo-2'-deoxyguanosine-2'-deoxyadenosine (OG*A) mismatches in DNA. MutY prevents DNA mutations caused by the misincorporation of A opposite OG by catalyzing the deglycosylation of the aberrant adenine. MutY is representative of a unique subfamily of DNA repair enzymes that also contain a [4Fe-4S]2+ cluster, which has been implicated in substrate recognition.

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