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Luba Krapivinsky

Researcher at Howard Hughes Medical Institute

Publications -  22
Citations -  4134

Luba Krapivinsky is an academic researcher from Howard Hughes Medical Institute. The author has contributed to research in topics: G protein & TRPC1. The author has an hindex of 21, co-authored 22 publications receiving 3898 citations. Previous affiliations of Luba Krapivinsky include Harvard University & University of Rochester.

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TRPC1 and TRPC5 form a novel cation channel in mammalian brain.

TL;DR: It is demonstrated here that TRPC1 and TRPC5 are subunits of a heteromeric neuronal channel, and proposed that many TRPC heteromers form diverse receptor-regulated nonselective cation channels in the mammalian brain.
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All four CatSper ion channel proteins are required for male fertility and sperm cell hyperactivated motility

TL;DR: Direct protein interactions among CatSpers, the sperm specificity of these proteins, and loss of ICatSper in each of the four CatSper−/− mice indicate that CatSper are highly specialized flagellar proteins.
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The NMDA Receptor Is Coupled to the ERK Pathway by a Direct Interaction between NR2B and RasGRF1

TL;DR: It is shown that NR2B, but not NR2A or NR1 subunits of the NMDAR, interacts in vivo and in vitro with RasGRF1, a Ca(2+)/calmodulin-dependent Ras-guanine-nucleotide-releasing factor, which serves as N MDAR-dependent regulator of the ERK kinase pathway.
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Formation of Novel TRPC Channels by Complex Subunit Interactions in Embryonic Brain

TL;DR: This complex assembly mechanism increases the diversity of TRPC channels in mammalian brain and may generate novel heteromers that have specific roles in the developing brain.
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SynGAP-MUPP1-CaMKII Synaptic Complexes Regulate p38 MAP Kinase Activity and NMDA Receptor- Dependent Synaptic AMPA Receptor Potentiation

TL;DR: Specific peptide-induced synGAP dissociation from the MUPP1-CaMKII complex results in SynGAP dephosphorylation accompanied by P38 MAPK inactivation, potentiation of synaptic AMPA responses, and an increase in the number of AMPAR-containing clusters in hippocampal neuron synapses, which implicate SynGap in NMDAR- and CaMKII-dependent regulation of AM PAR trafficking.