Radiologic seminar CLXXXV: subcapsular hematoma of the liver: A case report.
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Biomedical subjects
Publications and source records attributed to G Warren.
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The transfer defect of some ColE1 mutants is complemented by ColE1 or ColK, but not by ColE2. This implies that at least one ColE1-specified protein or RNA is normally needed for ColE1 conjugal transfer. The gene(s) postulated for this function lies within a region whose length is at most 50% of the genome.
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1-Methyl-3-nitro-1-nitrosoguanidine (NG) was able to inactivate and mutate adsorbed but not free coliphage T2. Coliphage T4 was as sensitive to NG as T2. When treatment was delayed for 5 min or longer after adsorption of T2, the phage became increasingly refractory to NG inactivation.
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In the eukaryotic cell, both secreted and plasma membrane proteins are synthesized at the endoplasmic reticulum, then transported, via the Golgi complex, to the cell surface. Each of the compartments of this transport pathway carries out particular metabolic functions, and therefore presumably contains a distinct complement of membrane proteins. Thus, mechanisms must exist for localizing such proteins to their respective destinations. However, a major obstacle to the study of such mechanisms is that the isolation and detailed analysis of such internal membrane proteins pose formidable technical problems. We have therefore used the E1 glycoprotein from coronavirus MHV-A59 as a viral model for this class of protein. Here we present the primary structure of the protein, determined by analysis of cDNA clones prepared from viral mRNA. In combination with a previous study of its assembly into the endoplasmic reticulum membrane, the sequence reveals several unusual features of the protein which may be related to its intracellular localization.
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