Hana Huang - Academia.edu (original) (raw)
Uploads
Papers by Hana Huang
Proceedings of the …, 2005
Physical review letters, 1997
Magnetic entropy change larger than that of gadolinium has been observed in polycrystalline of La... more Magnetic entropy change larger than that of gadolinium has been observed in polycrystalline of La 1-x Ca x MnO 3 ( x = 0.2 and 0.33) perovskite-type manganese oxide. The large magnetic entropy change produced by the abrupt reduction of magnetization is attributed to the ...
Macromolecules, 1987
ABSTRACT: A new type of hybrid material incorporating poly(dimethylsi1oxane) (PDMS) with tetraeth... more ABSTRACT: A new type of hybrid material incorporating poly(dimethylsi1oxane) (PDMS) with tetraeth-oxysilane (TEOS) has been successfully produced by using a sol-gel process. This material showed good optical transparency and very different mechanical behavior ...
Proceedings of The National Academy of Sciences, 2000
Parkinson's disease is a common neurodegenerative disorder in which familial-linked genes... more Parkinson's disease is a common neurodegenerative disorder in which familial-linked genes have provided novel insights into the pathogenesis of this disorder. Mutations in Parkin, a ring-finger-containing protein of unknown function, are implicated in the pathogenesis of autosomal recessive familial Parkinson's disease. Here, we show that Parkin binds to the E2 ubiquitin-conjugating human enzyme 8 (UbcH8) through its C-terminal ring-finger. Parkin has ubiquitin-protein ligase activity in the presence of UbcH8. Parkin also ubiquitinates itself and promotes its own degradation. We also identify and show that the synaptic vesicle-associated protein, CDCrel-1, interacts with Parkin through its ring-finger domains. Furthermore, Parkin ubiquitinates and promotes the degradation of CDCrel-1. Familial-linked mutations disrupt the ubiquitin-protein ligase function of Parkin and impair Parkin and CDCrel-1 degradation. These results suggest that Parkin functions as an E3 ubiquitin-protein ligase through its ring domains and that it may control protein levels via ubiquitination. The loss of Parkin's ubiquitin-protein ligase function in familial-linked mutations suggests that this may be the cause of familial autosomal recessive Parkinson's disease.
Journal of the American Statistical …, 1999
Proceedings of the …, 2005
Physical review letters, 1997
Magnetic entropy change larger than that of gadolinium has been observed in polycrystalline of La... more Magnetic entropy change larger than that of gadolinium has been observed in polycrystalline of La 1-x Ca x MnO 3 ( x = 0.2 and 0.33) perovskite-type manganese oxide. The large magnetic entropy change produced by the abrupt reduction of magnetization is attributed to the ...
Macromolecules, 1987
ABSTRACT: A new type of hybrid material incorporating poly(dimethylsi1oxane) (PDMS) with tetraeth... more ABSTRACT: A new type of hybrid material incorporating poly(dimethylsi1oxane) (PDMS) with tetraeth-oxysilane (TEOS) has been successfully produced by using a sol-gel process. This material showed good optical transparency and very different mechanical behavior ...
Proceedings of The National Academy of Sciences, 2000
Parkinson's disease is a common neurodegenerative disorder in which familial-linked genes... more Parkinson's disease is a common neurodegenerative disorder in which familial-linked genes have provided novel insights into the pathogenesis of this disorder. Mutations in Parkin, a ring-finger-containing protein of unknown function, are implicated in the pathogenesis of autosomal recessive familial Parkinson's disease. Here, we show that Parkin binds to the E2 ubiquitin-conjugating human enzyme 8 (UbcH8) through its C-terminal ring-finger. Parkin has ubiquitin-protein ligase activity in the presence of UbcH8. Parkin also ubiquitinates itself and promotes its own degradation. We also identify and show that the synaptic vesicle-associated protein, CDCrel-1, interacts with Parkin through its ring-finger domains. Furthermore, Parkin ubiquitinates and promotes the degradation of CDCrel-1. Familial-linked mutations disrupt the ubiquitin-protein ligase function of Parkin and impair Parkin and CDCrel-1 degradation. These results suggest that Parkin functions as an E3 ubiquitin-protein ligase through its ring domains and that it may control protein levels via ubiquitination. The loss of Parkin's ubiquitin-protein ligase function in familial-linked mutations suggests that this may be the cause of familial autosomal recessive Parkinson's disease.
Journal of the American Statistical …, 1999