Elo Eriste
Karolinska Institutet
14 Papers
132 Citations
Elo Eriste is an academic researcher from Karolinska Institutet. The author has contributed to research in topics: Receptor & Peptide. The author has an hindex of 8, co-authored 14 publications. Previous affiliations of Elo Eriste include National Institute of Chemical Physics and Biophysics.
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Papers
INSL5 is a high affinity specific agonist for GPCR142 (GPR100).
Changlu Liu,Chester Kuei,Steven W. Sutton,Jingcai Chen,Pascal Bonaventure,Jiejun Wu,Diane Nepomuceno,Fredrik Kamme,Da-Thao Tran,Jessica Zhu,Tracey N. Wilkinson,Ross A. D. Bathgate,Elo Eriste,Rannar Sillard,Timothy W. Lovenberg +14 more
TL;DR: The high affinity interaction between InSL5 and GPCR142 coupled with their co-evolution and partially overlapping tissue expression patterns strongly suggest that INSL5 is an endogenous ligand for GPCr142.
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Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperatively.
TL;DR: The specific metal-binding properties of MT-3 could be functionally implemented for buffering of fluctuating concentrations of zinc in zincergic neurons and for transfer of zinc to synaptic vesicles.
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A novel form of neurotensin post-translationally modified by arginylation.
Elo Eriste,Åke Norberg,Diane Nepomuceno,Chester Kuei,Fredrik Kamme,Da-Thao Tran,Kerstin Strupat,Hans Jörnvall,Changlu Liu,Timothy W. Lovenberg,Rannar Sillard +10 more
TL;DR: A novel bioactive form of neurotensin post-translationally modified at a Glu residue was isolated from porcine intestine and named “arginylated neurotensIn” (R-NT, N-(neurotensin-C5–4-yl)arginine), and it is shown that SK-N-SH neuroblastoma cells express NTR1 and NTR3 but not NTR2, suggesting that the Ca2+ mobilization elicited
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Evidence for non-isostructural replacement of Zn2+ with Cd2+ in the β-domain of brain-specific metallothionein-3
TL;DR: In this paper, the authors used electrospray ionization mass spectrometry to probe conformational states of cadmium and zinc-substituted metalloforms of MT-3.
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•Journal Article
Metal binding to brain-specific metallothionein-3 studied by electrospray ionization mass spectrometry.
TL;DR: Higher structural plasticity, dynamics and metal binding capacity ofMT-3 than of MT-1 makes MT-3 suitable as a zinc buffer-transfer molecule in zinc-enriched neurons functioning at conditions of fluctuating zinc concentrations.
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