Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P50583 (asymmetrical)
 12,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Corticotropin-releasing factor (CRF) and dopamine (DA) are important integrators of the endocrine and autonomic response to stress. CRF neurons in the anterior portions of the periventricular nucleus (PV) and parvocellular paraventricular nucleus (pvPVN) occur close to A14 DA neurons in these same locations. Since CRF has been shown to act as an excitatory neurotransmitter, possible CRF interactions with the DA system were investigated using double-label immunocytochemistry. Coronal vibratome sections through the PV and pvPVN were obtained from colchicine-treated and nontreated juvenile female cynomolgus macaques. They were sequentially immunostained for tyrosine hydroxylase (TH) (to identify DA neurons) with PAP and DAB, and for CRF using 15 nm colloidal gold. By light microscopy, areas of coincidence of TH- and CRF-immunoreactive cell bodies in the PV and pvPVN were obvious, but double-stained elements were not observed. By electron microscopy, asymmetrical synapses frequently occurred between CRF axons and TH dendrites or somata. Symmetrical axosomatic synapses sometimes appeared adjacent to these CRF/TH synapses, while symmetrical axoaxonic synapses were rare. We conclude that CRF neuronal efferents synaptically activate A14 DA neurons in the primate PV and pvPVN. Parallel CRF/DA symmetrical synapses also suggest coexistence of a companion transmitter within some of these same CRF neurons. Our own previous work and recent independent studies indicate that this transmitter is probably GABA. Thus the CRF neuronal system, which is known to alter secretion of several pituitary hormones, may also act through hypothalamic periventricular DA neurons to mediate other responses to stress.
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PMID:Corticotropin-releasing factor neurons innervate dopamine neurons in the periventricular hypothalamus of juvenile macaques. Synaptic evidence for a possible companion neurotransmitter. 257 55

The structure of a 23 nt RNA sequence, rGGACCCGGGCUCAACCUGGGUCC, was elucidated using homonuclear NMR, distance geometry and restrained molecular dynamics. This RNA is analogous to residues 612-628 of the Escherichia coli 16S rRNA. The structure of the RNA reveals the presence of a pentaloop closed by a duplex stem in typical A-form conformation. The loop does not form a U-turn motif, as previously predicted. A non-planar A.C.A triple base interaction (hydrogen bonds A13 NH6-C10 O2 and C10 N3-A14 NH6) stabilizing the loop structure is inferred from structure calculations. The CUCAA loop structure is asymmetrical, characterized by a reversal of the phosphodiester backbone at the UC step (hydrogen bond C12 NH4-C10 O2') and 3'-stacking within the CAA segment. Loop base U11 is oriented towards the major groove and the consecutive adenosines on the 3'-end of the loop are well stacked, exposing their reactive functional groups in the minor groove defined by the duplex stem. The solution structure of the loop resembles that seen in the 3.3 A X-ray structure of the entire 30S subunit, where the analogous loop interacts with a ribosomal protein and a receptor RNA helix.
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PMID:NMR structure of a ribosomal RNA hairpin containing a conserved CUCAA pentaloop. 1181 46