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- 저자 : Munehito (검색결과 5 건)
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A New Electrophysiological Method for the Diagnosis of Extraforaminal Stenosis at L5–S1
Hiroshi Iwasaki,Munehito Yoshida,Hiroshi Yamada,Hiroshi Hashizume,Akihito Minamide,Yukihiro Nakagawa,Masaki Kawai,Shunji Tsutsui 대한척추외과학회 2014 Asian Spine Journal Vol.8 No.2
Study Design: A retrospective study. Purpose: To examine the effectiveness of using an electrodiagnostic technique as a new approach in the clinical diagnosis of extraforaminal stenosis at L5–S1. Overview of Literature: We introduced a new effective approach to the diagnosis of extraforaminal stenosis at the lumbosacral junction using the existing electrophysiological evaluation technique. Methods: A consecutive series of 124 patients with fifth lumbar radiculopathy were enrolled, comprising a group of 74 patients with spinal canal stenosis and a second group of 50 patients with extraforaminal stenosis at L5–S1. The technique involved inserting a pair of needle electrodes into the foraminal exit zone of the fifth lumbar spinal nerves, which were used to provide electrical stimulation. The compound muscle action potentials from each of the tibialis anterior muscles were recorded. Results: The distal motor latency (DML) of the potentials ranged from 11.2 to 24.6 milliseconds in patients with extraforaminal stenosis. In contrast, the DML in patients with spinal canal stenosis ranged from 10.0 to 17.2 milliseconds. After comparing the DML of each of the 2 groups and at the same time comparing the differences in DML between the affected and unaffected side of each patient, we concluded there were statistically significant differences (p <0.01) between the 2 groups. Using receiver operating characteristic curve analysis, the cutoff values were calculated to be 15.2 milliseconds and 1.1 milliseconds, respectively. Conclusions: This approach using a means of DML measurement enables us to identify and localize lesions, which offers an advantage in diagnosing extraforaminal stenosis at L5–S1.
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Kunihiro Kuwajima,Tomonao Inobe,Munehito Arai 한국고분자학회 2006 Macromolecular Research Vol.14 No.2
This is a short review article of our recent studies on the ATP-induced, allosteric conformational transition of the chaperonin GroEL complex by solution X-ray scattering. We used synchrotron X-ray scattering with a two-dimensional, charge-coupled, device-based X-ray detector to study (1) the specificity of the chaperonin GroEL for its ligand that induced the allosteric transition, and (2) the identification of the allosteric transition of GroEL in its complicated kinetics induced by ATP. Due to the dramatically increased sensitivity of the X-ray scattering technique based on the use of the two dimensional X-ray detector and synchrotron radiation, different allosteric conformational states of GroEL populated under different conditions were clearly distinguished from each other. It was concluded that solution X-ray scattering is an extremely powerful tool for investigating the equilibrium and kinetics of coop erative conformational transitions of oligomeric protein complex, especially when combined with other spectro scopic techniques such as fluorescence spectroscopy.
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Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2.
Ferreon, Josephine C,Lee, Chul Won,Arai, Munehito,Martinez-Yamout, Maria A,Dyson, H Jane,Wright, Peter E National Academy of Sciences 2009 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.106 No.16
<P>The tumor suppressor activity of p53 is regulated by interactions with the ubiquitin ligase HDM2 and the general transcriptional coactivators CBP and p300. Using NMR spectroscopy and isothermal titration calorimetry, we have dissected the binding interactions between the N-terminal transactivation domain (TAD) of p53, the TAZ1, TAZ2, KIX, and nuclear receptor coactivator binding domains of CBP, and the p53-binding domain of HDM2. The p53 TAD contains amphipathic binding motifs within the AD1 and AD2 regions that mediate interactions with CBP and HDM2. Binding of the p53 TAD to CBP domains is dominated by interactions with AD2, although the affinity is enhanced by additional interactions with AD1. In contrast, binding of p53 TAD to HDM2 is mediated primarily by AD1. The p53 TAD can bind simultaneously to HDM2 (through AD1) and to any one of the CBP domains (through AD2) to form a ternary complex. Phosphorylation of p53 at T18 impairs binding to HDM2 and enhances affinity for the CBP KIX domain. Multisite phosphorylation of the p53 TAD at S15, T18, and S20 leads to increased affinity for the TAZ1 and KIX domains of CBP. These observations suggest a mechanism whereby HDM2 and CBP/p300 function synergistically to regulate the p53 response. In unstressed cells, CBP/p300, HDM2 and p53 form a ternary complex that promotes polyubiquitination and degradation of p53. After cellular stress and DNA damage, p53 becomes phosphorylated at T18 and other residues in the AD1 region, releases HDM2 and binds preferentially to CBP/p300, leading to stabilization and activation of p53.</P>
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Kuwajima Kunihiro,Inobe Tomonao,Arai Munehito The Polymer Society of Korea 2006 Macromolecular Research Vol.14 No.2
This is a short review article of our recent studies on the ATP-induced, allosteric conformational transition of the chaperonin GroEL complex by solution X-ray scattering. We used synchrotron X-ray scattering with a two-dimensional, charge-coupled, device-based X-ray detector to study (1) the specificity of the chaperonin GroEL for its ligand that induced the allosteric transition, and (2) the identification of the allosteric transition of GroEL in its complicated kinetics induced by ATP. Due to the dramatically increased sensitivity of the X-ray scattering technique based on the use of the two dimensional X-ray detector and synchrotron radiation, different allosteric conformational states of GroEL populated under different conditions were clearly distinguished from each other. It was concluded that solution X-ray scattering is an extremely powerful tool for investigating the equilibrium and kinetics of cooperative conformational transitions of oligomeric protein complex, especially when combined with other spectroscopic techniques such as fluorescence spectroscopy.
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