L
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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Journal ArticleDOI
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
Huayu Qi,Magdalene M. Moran,Betsy Navarro,Jayhong A. Chong,Grigory Krapivinsky,Luba Krapivinsky,Yuriy Kirichok,I. Scott Ramsey,Timothy A. Quill,David E. Clapham +9 more
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
Grigory Krapivinsky,Luba Krapivinsky,Yunona Manasian,Anton Ivanov,Roman Tyzio,Christophe Pellegrino,Yehezkel Ben-Ari,David E. Clapham,Igor Medina +8 more
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.
Journal ArticleDOI
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.