| 2. |
- Linnarsson, Margareta K., et al.
(författare)
-
Sputter profiling of AlGaAs/GaAs superlattice structures using oxygen and argon ions
- 1993
-
Ingår i: Applied Surface Science. - 0169-4332 .- 1873-5584. ; 70-71:1, s. 40-43
-
Tidskriftsartikel (refereegranskat)abstract
- Broadening of Al sputter profiles in AlxGa1-xAs/GaAs structures has been investigated using secondary ion mass spectrometry. The depth profiling was carried out with 32O+2 ions and 40Ar+ ions using net primary energies of 1.8, 2.2, 3.2 and 5.7 keV. The decay lengths of the Al profiles show a pronounced increase with increasing sputtering ion energy caused by ballistic mixing. Moreover, in the O+2 case the λ-values degrade with eroded depth, indicating that beam-induced surface roughening takes place during profiling and in particular, this holds for high x-values. The results are discussed in terms of a semi-empirical model for ion-beam-induced broadening developed by Zalm and Vriezema.
|
|
| 3. |
- Weclewicz, K, et al.
(författare)
-
Microtubule-associated protein 2 appears in axons of cultured dorsal root ganglia and spinal cord neurons after rotavirus infection.
- 1993
-
Ingår i: Journal of neuroscience research. - : Wiley. - 0360-4012 .- 1097-4547. ; 36:2, s. 173-82
-
Tidskriftsartikel (refereegranskat)abstract
- The immunohistochemical distribution of microtubule-associated protein 2 (MAP2), being normally restricted to nerve cell bodies and dendrites, became altered in rat dorsal root ganglia and spinal cord neurons in cultures infected with rhesus rotavirus. MAP2 appeared in axons of both sources of neurons as displayed with monoclonal antibodies to MAP2a + b and MAP2a + b + c at 48 hr post-infection (p.i.). Other cytoskeletal elements, i.e., tau, MAP1, MAP5, neurofilament, actin, and tubulin, did not reveal any alterations in the rotavirus-infected neurons. One of the rotavirus cytosolic proteins, the inner capsid protein vp6, was expressed in axons at 48 hr p.i. simultaneously with the appearance of MAP2, while two other viral proteins, vp4 and NS28, remained in the nerve cell bodies. By quantitative enzyme-linked immunosorbent assay (ELISA) a binding of single-shelled rotaviruses, which express vp6 on their surfaces, to purified MAP2 was found. There was no binding of these viral particles to tau or tubulin proteins. This study indicates that a selective interaction between certain viral and neuronal cytoskeletal proteins can occur and that a non-cytolytic viral infection can cause alterations in the polarized sorting of neuronal proteins.
|
|
