Characterization of recombinant and natural forms of the human LIM domain-containing protein FHL2
✍ Scribed by Haquima El Mourabit; Stefan Müller; Lucy Tunggal; Mats Paulsson; Monique Aumailley
- Book ID
- 117702824
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 249 KB
- Volume
- 32
- Category
- Article
- ISSN
- 1046-5928
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📜 SIMILAR VOLUMES
## Abstract Containing four LIM domains and an N‐terminal half LIM domain, FHL2 has been predicted to have an adaptor function in the formation of higher order molecular complexes in the nucleus and the cytoplasm of cells. We expressed recombinant FHL2 in insect cells using the baculovirus system a
In the yeast two-hybrid library screening, the heart-specific FHL2 protein was found to interact with hCDC47. In vitro interaction study between FHL2 protein and hCDC47 was demonstrated. From the results of domain studies by the yeast two-hybrid assay, the second and third LIM domains in conjunction
## Abstract From the publisher: The reproduction quality of Figures 2, 3,and 5 from the above article was subpar and did not accurately capture the fine detail of the author's original prints. The figures and legends are reprinted herein. Originally published in Cell Motility and the Cytoskeleton 4
## Abstract Using a yeast two‐hybrid library screen, we have identified that the heart specific FHL2 protein, four‐and‐a‐half LIM protein 2, interacted with human DNA‐binding nuclear protein, hNP220. Domain studies by the yeast two‐hybrid interaction assay revealed that the second LIM domain togeth