Abnormal pontine activation in pathological laughing as shown by functional magnetic resonance imaging

To explore the aetiology of pathological laughing, a 65-year-old woman with pathological laughing was examined by 3-T functional magnetic resonance imaging (fMRI) before and after treatment with drugs. Here, we report that the patient consistently showed exaggerated pontine activation during the performance of three tasks before treatment, whereas abnormal pontine activation was no longer found after successful treatment with the selective serotonin reuptake inhibitor, paroxetine. Our findings in this first fMRI study of pathological laughing suggest that serotonergic replacement decreases the aberrant activity in a circuit that involves the pons

2000年代以降の外食産業再編期における飲食店の立地動向に関する研究 : 京阪神大都市圏を中心に

立命館大学博士(文学)doctoral thesi

伝世戦国貨幣調査の意義

2007-03-31departmental bulletin pape

They are Coming

This is the story of a small family in Lobengula township, Bulawayo: a shoemaker, Ngwenya, his wife, MaVundla, and their two children, Ambition and Senzeni, whose lives are turned upside-down when Senzeni joins the local youth militia. Mlalazi captures the texture of everyday life in the township, the humour, warmth, rivalry and fear as neighbours interact with each other or get swept up by events outside their control. Their constant search, however, is for autonomy and independence, for the ability to have control over their own lives. They are Coming provides us with perspectives often hidden from view, in a story where particular events are part of a more complex history

The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog-6

S). Thermal denaturation of ecRBP in the absence (open circle) or presence of 1 mM ribose (black circles). Solid lines in (A) are fit to a two-state model [31, 32] which takes into account the native and denatured baseline slopes. (B) Extrapolated of tteRBP in the absence (open squares) or presence of 1 mM ribose (black squares) obtained from a series of thermal melting curves at different GdCl concentrations. Solid lines represent linear fits to the observations.<p><b>Copyright information:</b></p><p>Taken from "The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog"</p><p>http://www.biomedcentral.com/1472-6807/8/20</p><p>BMC Structural Biology 2008;8():20-20.</p><p>Published online 28 Mar 2008</p><p>PMCID:PMC2315655.</p><p></p

The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog-1

S). Thermal denaturation of ecRBP in the absence (open circle) or presence of 1 mM ribose (black circles). Solid lines in (A) are fit to a two-state model [31, 32] which takes into account the native and denatured baseline slopes. (B) Extrapolated of tteRBP in the absence (open squares) or presence of 1 mM ribose (black squares) obtained from a series of thermal melting curves at different GdCl concentrations. Solid lines represent linear fits to the observations.<p><b>Copyright information:</b></p><p>Taken from "The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog"</p><p>http://www.biomedcentral.com/1472-6807/8/20</p><p>BMC Structural Biology 2008;8():20-20.</p><p>Published online 28 Mar 2008</p><p>PMCID:PMC2315655.</p><p></p

The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog-5

underlined, amino acids that are conserved but not identical are in bold type (charge inversions are scored as non-conservative here). Core, boundary or surface classification of amino acids is shown below the aligned residues.<p><b>Copyright information:</b></p><p>Taken from "The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog"</p><p>http://www.biomedcentral.com/1472-6807/8/20</p><p>BMC Structural Biology 2008;8():20-20.</p><p>Published online 28 Mar 2008</p><p>PMCID:PMC2315655.</p><p></p

The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog-3

S 55–61, 2/residues 117–126, 3/residues 149–156). (B) Close-up view of the polar binding pocket residues in tteRBP (blue) and ecRBP (magenta). Ribose is shown in gray. Critical residues involved in ribose binding are indicated (where the tteRBP and ecRBP numbering are different, the former is given first). (C) Close-up view of the non-polar binding pocket amino acids of tteRBP (blue) and ecRBP (magenta). (D) Structural differences in the Cα positions of the aligned models of ecRBP and tteRBP generated by LSQMAN [60]. Dashed and dotted lines indicate the RMSD of 235/271 and 270/271 of the Cα atoms respectively of the aligned structures. The N- and C- terminal residues are indicated with a solid line. Loops and turns are indicated (asterisk), or loops (underlined asterisk) in the binding pocket region.<p><b>Copyright information:</b></p><p>Taken from "The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog"</p><p>http://www.biomedcentral.com/1472-6807/8/20</p><p>BMC Structural Biology 2008;8():20-20.</p><p>Published online 28 Mar 2008</p><p>PMCID:PMC2315655.</p><p></p

The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog-0

underlined, amino acids that are conserved but not identical are in bold type (charge inversions are scored as non-conservative here). Core, boundary or surface classification of amino acids is shown below the aligned residues.<p><b>Copyright information:</b></p><p>Taken from "The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog"</p><p>http://www.biomedcentral.com/1472-6807/8/20</p><p>BMC Structural Biology 2008;8():20-20.</p><p>Published online 28 Mar 2008</p><p>PMCID:PMC2315655.</p><p></p

The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog-2

Ted.<p><b>Copyright information:</b></p><p>Taken from "The backbone structure of the thermophilic ribose binding protein is essentially identical to its mesophilic homolog"</p><p>http://www.biomedcentral.com/1472-6807/8/20</p><p>BMC Structural Biology 2008;8():20-20.</p><p>Published online 28 Mar 2008</p><p>PMCID:PMC2315655.</p><p></p