Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:2.7.7.48 (transcriptase)
9,479 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Nonstructural proteins of plum pox potyvirus were partially purified following a procedure described for the isolation of tobacco etch virus nuclear inclusion proteins. Plum pox virus proteins with electrophoretic mobilities corresponding to 49, 59 and 68 kDa reacted with antibodies against the 49 kDa and 54 kDa components of the nuclear inclusions and the 70 kDa component of the cylindrical inclusions of tobacco etch virus, respectively. Further purification by size exclusion high performance liquid chromatography or SDS-polyacrylamide gel electrophoresis, and amino terminal amino acid sequencing permitted the location in the plum pox virus polyprotein of the cleavage sites from which the 49 kDa (NIa-type, protease), 59 kDa (NIb-type, putative RNA replicase), and 68 kDa (CI-type) proteins originate. A 110 kDa protein which copurified with the plum pox virus inclusion proteins reacted with both anti-NIa and anti-NIb sera and had the same amino terminus as the plum pox virus 49 kDa protein, indicating that it is a non-processed 49-59 kDa polypeptide.
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PMID:Determination of polyprotein processing sites by amino terminal sequencing of nonstructural proteins encoded by plum pox potyvirus. 213 35

The N-methyl-D-aspartate receptor (NMDAR) is involved in a number of physiological and pathophysiological processes in vertebrates, but there have been few studies examining the role of invertebrate NMDA receptors. In the leech, pharmacological evidence suggests that NMDARs contribute to synaptic plasticity, but there has been no molecular identification of NMDA receptors. In this report, a partial cDNA encoding the leech NR1 subunit of the NMDA receptor (HirNR1) is presented. Reverse transcriptase-polymerase chain reaction from single neurons of the leech central nervous system confirms HirNR1 expression in the Retzius (R), Anterior Pagoda (AP), Pressure (P), and Touch (T) neurons. Immunoblotting with an anti-NR1 antibody yielded a approximately 110 kDa protein, similar to the expected weight of the NR1 subunit (approximately 116 kDa). Finally, pairing pre- and postsynaptic activity elicited long-term potentiation in synapses between neurons expressing NR1 mRNA (P-to-AP synapse) and this potentiation was blocked by the NMDAR antagonist AP5.
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PMID:Molecular identification and expression of the NMDA receptor NR1 subunit in the leech. 1914 76