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1.
Nano Lett ; 13(12): 5797-802, 2013.
Article En | MEDLINE | ID: mdl-24228733

The recent focus on topological insulators is due to the scientific interest in the new state of quantum matter as well as the technology potential for a new generation of THz optoelectronics, spintronics and quantum computations. It is important to elucidate the dynamics of the Dirac fermions in the topologically protected surface state. Hence we utilized a novel ultrafast optical pump mid-infrared probe to explore the dynamics of Dirac fermions near the Dirac point. The femtosecond snapshots of the relaxation process were revealed by the ultrafast optics. Specifically, the Dirac fermion-phonon coupling strength in the Dirac cone was found to increase from 0.08 to 0.19 while Dirac fermions were away from the Dirac point into higher energy states. Further, the energy-resolved transient reflectivity spectra disclosed the energy loss rate of Dirac fermions at room temperature was about 1 meV/ps. These results are crucial to the design of Dirac fermion devices.


Nanostructures/chemistry , Nanotechnology , Optics and Photonics , Quantum Theory , Semiconductors , Spectrophotometry, Infrared
2.
Osteoarthritis Cartilage ; 15(12): 1357-66, 2007 Dec.
Article En | MEDLINE | ID: mdl-17590359

OBJECTIVE: To determine whether an intra-articular injection of recombinant human bone morphogenetic protein-2 (rhBMP-2) alleviates cartilage degradation in a rat model of osteoarthritis (OA) of the lumbar facet joint. METHOD: The right-side facet joint OA model was created by an intra-articular injection of collagenase (type II) 2 weeks before treatment. The OA rats were divided into four groups: (1) no treatment, or intra-articular injection of either (2) saline, (3) rhBMP-2 10 ng, or (4) rhBMP-2 100 ng. The left-side facet joint served as the normal control. At 3 and 6 weeks after treatment, histological analyses were performed on the cartilage, synovium, subchondral bone and bone marrow. The cartilage and synovium were graded using a modified Mankin score and a synovium score system. Extracellular type II collagen was evaluated by immunohistochemistry. RESULTS: Intra-articular injection of collagenase causes OA-like changes in the facet joint. OA rats treated with rhBMP-2 at both dosages tested showed reduced severity of their cartilage lesions compared with untreated and saline-treated groups. There was a statistically significant difference in the modified Mankin score compared to the untreated and saline-treated groups. However, some rhBMP-2-treated rats at the higher dose (100 ng) showed, as a side effect, joint space obliteration caused by cartilage overgrowth. Also OA rats treated with 100 ng of rhBMP-2 displayed a significant synovium reaction at 3 weeks compared with that in other groups. Immunohistochemical analysis showed that treatment with rhBMP-2 significantly increased the content of type II collagen. CONCLUSION: This study demonstrates the potential efficacy of rhBMP-2 in the alleviation of arthritic changes in a rat model of OA of the lumbar facet joint. However, treatment with a high dosage of rhBMP-2 caused adverse side effects in some animals.


Bone Morphogenetic Proteins/therapeutic use , Matrix Metalloproteinase 8/adverse effects , Osteoarthritis/drug therapy , Recombinant Proteins/therapeutic use , Transforming Growth Factor beta/therapeutic use , Zygapophyseal Joint/metabolism , Zygapophyseal Joint/pathology , Animals , Bone Morphogenetic Protein 2 , Bone Morphogenetic Proteins/pharmacology , Cartilage, Articular/drug effects , Cartilage, Articular/metabolism , Collagen Type II/metabolism , Disease Models, Animal , Dose-Response Relationship, Drug , Matrix Metalloproteinase 8/administration & dosage , Osteoarthritis/chemically induced , Osteoarthritis/metabolism , Random Allocation , Rats , Rats, Sprague-Dawley , Recombinant Proteins/pharmacology , Staining and Labeling , Synovial Membrane/drug effects , Synovial Membrane/metabolism , Transforming Growth Factor beta/pharmacology , Zygapophyseal Joint/drug effects
3.
J Virol Methods ; 33(1-2): 115-25, 1991 Jun.
Article En | MEDLINE | ID: mdl-1658026

Viral proteins of two strains of infectious bronchitis virus (IBV), which have different tissue trophism and serology, were separated on the basis of their isoelectric points (pI). The viruses have four structural proteins; the protein of greatest serological importance is found at the peplomer tip. The viral structural proteins separated by isoelectric focusing were identified by comparison to SDS-PAGE separations. Three protein bands were identical in pI and one protein band showed a difference in pI between strains. When the renatured viral proteins were Western blotted and reacted with strain-specific antiserum, antigen-antibody complexing was seen only at points corresponding to the strain-specific variant bands. For IBV strain Mass-41, antigen-antibody complexing occurred at a pI of 6.8, and, for IBV strain Ark-99, at 7.2. No cross reaction of antisera was observed for either strain. Since tissue affinities are a function of the viral peplomer-mediated attachment of virus to cells and are often directly related to pathogenicity, it appears that altered pathogenicity of strains of IBV may be detected by alteration of pI of the proteins. Classification by pI of proteins of at least the smaller viruses allows untypeable, highly pathogenic or persistent strains of these viruses to be characterized on the basis of variant proteins.


Infectious bronchitis virus/chemistry , Viral Structural Proteins/isolation & purification , Antibodies, Viral , Infectious bronchitis virus/classification , Infectious bronchitis virus/immunology , Isoelectric Point , Species Specificity , Viral Structural Proteins/chemistry , Viral Structural Proteins/immunology , Virology/methods
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