S
Steen H. Hansen
Researcher at Boston Children's Hospital
Publications - 46
Citations - 5009
Steen H. Hansen is an academic researcher from Boston Children's Hospital. The author has contributed to research in topics: Endocytosis & Endosome. The author has an hindex of 29, co-authored 46 publications receiving 4752 citations. Previous affiliations of Steen H. Hansen include Harvard University & Finsen Laboratory.
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Journal ArticleDOI
Evidence for a Regulated Interaction between Heterotrimeric G Proteins and Caveolin
Shengwen Li,Takashi Okamoto,Miyoung Chun,Massimo Sargiacomo,James E. Casanova,Steen H. Hansen,Ikuo Nishimoto,Michael P. Lisanti +7 more
TL;DR: Data suggest that caveolin could function to negatively regulate the activation state of heterotrimeric G proteins, apparently by inhibiting GDP/GTP exchange.
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Rac1 orientates epithelial apical polarity through effects on basolateral laminin assembly
Lucy Erin O'Brien,Tzuu-Shuh Jou,Tzuu-Shuh Jou,Anne L. Pollack,Qihang Zhang,Steen H. Hansen,Steen H. Hansen,Peter D. Yurchenco,Keith E. Mostov +8 more
TL;DR: It is reported that orientation of apical polarity in developing Madin–Darby canine kidney (MDCK) epithelial cysts requires the small GTPase Rac1 and the basement membrane component laminin and Rac1-mediated laminIn assembly in apical pole orientation.
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Retrograde transport of endocytosed Shiga toxin to the endoplasmic reticulum
TL;DR: It is shown that in butyric acid-treated A431 cells endocytosed Shiga toxin is not only transported to the trans-Golgi network, but also to all Golgi stacks, to the endoplasmic reticulum and to the nuclear envelope.
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Clathrin and HA2 Adaptors: Effects of Potassium Depletion, Hypertonic Medium, and Cytosol Acidification
TL;DR: Quantitative ultrastructural observations reveal that acidification of the cytosol results in formation of heterogeneously sized and in average smaller clathrin-coated pits at the plasma membrane and buds on the TGN, and raise the possibility that adaptor aggregates can form nucleation sites forclathrin lattices.
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ARNO is a guanine nucleotide exchange factor for ADP-ribosylation factor 6.
TL;DR: It is reported here that in vitro ARNO can stimulate nucleotide exchange on both ARF1 and ARF6, and it is found that ARNO is localized to the plasma membrane in mammalian cells rather than the Golgi, therefore likely thatARNO functions in plasma membrane events by modulating the activity of ARF 6 in vivo.