Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0033036 (APC)
 10,214 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The rates of colour change reactions of metallochromic indicators such as XO, PAN, PAC and TAC at the equivalence point were measured in the chelatometric titration of copper, nickel, zinc or cobalt. Hexamine buffer has strong disturbing effects on the rate of colour change of the copper or nickel XO chelate. The effects of various auxiliary complex-forming agents were also examined. Bathophenanthroline, 2,2'-bipyridyl, 8-hydroxyquinoline, TPTZ, ethylenediamine, iminodiacetic acid, acetylacetone, 1,10-phenanthroline and glycine improve the colour change of the XO and PAN chelates of copper. Some titration methods for copper or nickel with XO or PAN as indicator are proposed.
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PMID:Effects of auxiliary complex-forming agents on the rate of metallochromic indicator colour change. 1896 52

Transcription and replication of the negative-sense single-stranded influenza A virus genomic viral RNA are catalyzed by the viral RNA polymerase, which is a trimeric complex encoded by the three largest segments of the influenza virus genome: PB1, PB2, and PA. Numerous studies of the trimeric polymerase complex assembly have substantially contributed to current understanding of influenza virus replication. However, the dynamics of spatial and temporal macromolecular interactions involving virus and host proteins during the formation of the trimeric polymerase complex (PA-PB1-PB2) are still not completely understood. In this study, bimolecular fluorescence complementation (BiFC) and Raster image correlation spectroscopy (RICS) were applied to monitor the interactions between PB1, PB2, and PA. The BiFC probes of PA-PB1 and PB1-PB2 could monitor the trimeric polymerase complex as well as the binary complex. Furthermore, the C-terminal domain of PA (PAC) promoted interaction between PB1 and PB2 in the cytoplasm and that the N-terminal domain of PA (PAN) inhibited the aberrant trimeric complex formation and assembly of higher-order oligomers induced by PAC in the cytoplasm. Taken together, these results revealed a novel function of PAN in the formation of the trimeric polymerase complexes of influenza A virus.
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PMID:A novel function of the N-terminal domain of PA in assembly of influenza A virus RNA polymerase. 2200 19