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Emily Kim

Researcher at Harvard University

Publications -  25
Citations -  3527

Emily Kim is an academic researcher from Harvard University. The author has contributed to research in topics: GTPase-activating protein & RGS Proteins. The author has an hindex of 19, co-authored 25 publications receiving 3395 citations. Previous affiliations of Emily Kim include University of Freiburg & Beth Israel Deaconess Medical Center.

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Journal ArticleDOI

RIP : a novel protein containing a death domain that interacts with Fas/APO-1 (CD95) in yeast and causes cell death

Ben Z. Stanger, +6 more
- 19 May 1995 - 
TL;DR: Transient overexpression of RIP causes transfected cells to undergo the morphological changes characteristic of apoptosis, and these properties indicate that RIP is a novel form of apoptotic-inducing protein.
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Homo- and heterodimeric interactions between the gene products of PKD1 and PKD2.

Leonidas Tsiokas, +4 more
- 24 Jun 1997 - 
TL;DR: In this paper, the C-terminal cytoplasmic tails of PKD1 and PKD2 were found to form homodimers through a coiled-coil domain distinct from the region required for interaction with PKD 1.
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Specific association of the gene product of PKD2 with the TRPC1 channel

Leonidas Tsiokas, +5 more
- 30 Mar 1999 - 
TL;DR: In this paper, sequence homology between PKD2 and various members of the mammalian transient receptor potential channel (TRPC) proteins, thought to be activated by G protein-coupled receptor activation and/or depletion of internal Ca2+ stores, was described.
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The Polycystic Kidney Disease 1 Gene Product Modulates Wnt Signaling

Emily Kim, +8 more
- 19 Feb 1999 - 
TL;DR: It is reported here that expression of the C-terminal cytoplasmic domain of polycystin stabilizes soluble endogenous β-catenin and stimulates TCF-dependent gene transcription in human embryonic kidney cells, and suggest that poly Cystin has the capacity to modulate Wnt signaling during renal development.
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Trafficking of TRPP2 by PACS proteins represents a novel mechanism of ion channel regulation.

Michael Köttgen, +15 more
- 23 Feb 2005 - 
TL;DR: The paradigm that polycystin‐2 is sorted to and active at both ER and plasma membrane reconciles the previously incongruent views of its localization and function is reconciled.