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pro vyhledávání: '"Ingo Gestmann"'
Publikováno v:
Materials Science and Engineering: C. 33:4274-4279
The development of scaffolds and templates is an essential aspect of tissue engineering. We show that thick (> 0.5 mm) vertically aligned carbon nanotube films, made by chemical vapour deposition, can be used as biocompatible substrates for the direc
Autor:
Richard J. Young, Trevor Dingle, Laurent Roussel, Sander Henstra, Gerard Nicolaas Anne van Veen, Todd Templeton, Ingo Gestmann
Publikováno v:
Microscopy Today. 16:24-29
“Extreme high-resolution” (XHR) scanning electron microscopy (SEM) has the potential to change the way we look at SEM. Anyone in the SEM world knows that you don't do high-resolution SEM at low accelerating voltages because of chromatic aberratio
Autor:
Trevor Dingle, Ingo Gestmann, Albert Mangnus, Jarda Chmelik, Richard J. Young, Gerard Nicolaas Anne van Veen, Sander Henstra
Publikováno v:
Scanning Microscopy 2009.
The low voltage scanning electron microscope (SEM) is widely used in many industrial and research applications due to its ability to image surface details and to minimize charging and beam damage effects on sensitive samples. However, fundamental lim
Publikováno v:
Scanning Microscopy 2009.
For decades, high resolution scanning electron microscopes (SEM) have strived to offer improved performance in the high and low energy regimes. High energies have always been attractive, because they lead to sub-nanometer resolution without complex e
Publisher Summary Thyroglobulin is the macromolecular precursor of thyroid hormones. Its storage is an important prerequisite to retain iodide in an organified fashion and to provide a reservoir that guarantees constant levels of thyroid hormones in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5092d3c889fc244afe3a405539623872
https://doi.org/10.1016/s0076-6879(02)48649-1
https://doi.org/10.1016/s0076-6879(02)48649-1
Publikováno v:
Biological Chemistry. 381
Multimerization of thyroglobulin (TG) takes place extracellularly in the thyroid follicle lumen and is regarded as a mechanism to store TG at high concentrations. Human thyroglobulin (hTG) has been shown to multimerize mainly by intermolecular disulf