Abstract
Contact and support
Need help, have a question, or want to contact the ResearchHub team?
© 2026 ResearchHub. Built for responsible scholarly connection.
Ivan Mercurio, Gianluca D’Abrosca, Maria della Valle, Gaetano Malgieri, Carla Isernia, Emilia Maria Pedone, Domenico Alberga, Giuseppe Felice Mangiatordi
Abstract
Authors
Institutions
No ROR-resolved institution is linked to this work yet.
Provenance
crossref
Confidence 100%
pubmed
Confidence 98%
europepmc
Confidence 96%
unpaywall
Confidence 95%
doaj
Confidence 92%
datacite
Confidence 0%
No local reference links have been materialized yet.
No local citing links have been materialized yet.
10.1016/s0021-9258(18)53407-4
10.1016/s0021-9258(18)53407-4
10.1046/j.1471-4159.1995.64031016.x
10.1046/j.1471-4159.1995.64031016.x
The major astrocytic phosphoprotein PEA-15 is encoded by two mRNAs conserved on their full length in mouse and human*
10.1074/jbc.271.25.14800 · 1996
Frontiers: PED/PEA-15, a multifunctional protein controlling cell survival and glucose metabolism
10.1152/ajpendo.00228.2009 · 2009
The anti-apoptotic protein PEA-15 is a tight binding inhibitor of ERK1 and ERK2, which blocks docking interactions at the D-recruitment site
10.1021/bi700206u · 2007
10.1038/sj.onc.1202831
10.1038/sj.onc.1202831
10.1074/jbc.271.25.14800
10.1074/jbc.271.25.14800
PEA-15 mediates cytoplasmic sequestration of ERK MAP kinase biological outputs by phosphorylating nuclear and cyto-plasmic substrates. Nuclear substrates include tran-scription factors such as Elk-1, and cytoplasmic sub
2001
Knock-out of the neural death effector domain protein PEA-15 demonstrates that its expression protects astrocytes from TNF-induced apoptosis.
10.1523/jneurosci.19-19-08244.1999 · 1999
Endothelin induces a calcium-dependent phosphorylation of PEA-15 in intact astrocytes: identification of Ser104 and Ser116 phosphorylated, respectively, by protein kinase C and calcium/calmodulin kinase II in vitro
10.1046/j.1471-4159.1998.71031307.x · 1998
Structure of ERK2 bound to PEA-15 reveals a mechanism for rapid release of activated MAPK
2013
10.1091/mbc.11.9.2863
10.1091/mbc.11.9.2863
10.1128/mcb.23.13.4511-4521.2003
10.1128/mcb.23.13.4511-4521.2003
10.1074/jbc.m202946200
10.1074/jbc.m202946200
10.1093/emboj/cdf641
10.1093/emboj/cdf641
Profound conformational changes of PED/PEA-15 in ERK2 complex revealed by NMR backbone dynamics
10.1016/j.bbapap.2012.07.001 · 2012
High-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions
10.1016/j.bbrc.2012.06.091 · 2012
Targetting PED/PEA-15 for diabetes treatment
2017
The PEA15 gene is overexpressed and related to insulin resistance in healthy first-degree relatives of patients with type 2 diabetes
10.1007/s00125-006-0455-5 · 2006
PED/PEA-15 gene controls glucose transport and is overexpressed in type 2 diabetes mellitus
10.1093/emboj/17.14.3858 · 1998
10.1128/mcb.4.11.5005-5015.2004
10.1128/mcb.4.11.5005-5015.2004
10.2337/db06-1260
10.2337/db06-1260
Residues 762-801 of PLD1 mediate the interaction with PED/PEA15
10.1039/c005272h · 2010
Molecular basis of the PED/PEA15 interaction with the C-terminal fragment of phospholipase D1 revealed by NMR spectroscopy
10.1016/j.bbapap.2013.04.012 · 2013
10.1074/jbc.m803771200
10.1074/jbc.m803771200
Regulation of expression of phospholipase D1 and D2 by PEA-15, a novel protein that interacts with them
10.1074/jbc.m003329200 · 2000
Expression and purification of the D4 region of PLD1 and characterization of its interaction with PED-PEA15
10.1016/j.pep.2008.02.012 · 2008
Expression and purification of the D4 region of PLD1 and characterization of its interaction with PED-PEA15
10.1016/j.pep.2008.02.012 · 2008
Screening a molecular fragment library to modulate the PED/PEA15-phospholipase D1 interaction in cellular lysate environments
10.1021/acschembio.1c00688 · 2021
Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
10.1038/nrd1343 · 2004
Protein and ligand preparation: parameters, protocols, and influence on virtual screening enrichments
10.1007/s10822-013-9644-8 · 2013
Unresolved referenced work
Kept as external metadata until matched
OPLS4: improving force field accuracy on challenging regimes of chemical space
10.1021/acs.jctc.1c00302 · 2021
Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy
10.1021/jm0306430 · 2004
10.1021/jm051256o
10.1021/jm051256o
Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment Factors in Database Screening
10.1021/jm030644s · 2004
Unresolved referenced work
Kept as external metadata until matched
10.1021/acs.jctc.1c00810
10.1021/acs.jctc.1c00810
Unresolved referenced work
Kept as external metadata until matched
Novel procedure for modeling ligand/receptor induced fit effects
10.1021/jm050540c · 2006
PEA-15 engages in allosteric interactions using a common scaffold in a phosphorylation-dependent manner
10.1038/s41598-021-04099-6 · doi-reference
10.1016/j.pnmrs.2013.02.001
10.1016/j.pnmrs.2013.02.001 · doi-reference
NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy
10.1093/bioinformatics/btu830 · doi-reference
Protein interaction patterns in different cellular environments are revealed by in-cell NMR
10.1038/srep14456 · doi-reference
10.3390/ijms20020378
10.3390/ijms20020378 · doi-reference
Identifying and characterizing binding sites and assessing druggability
10.1021/ci800324m · doi-reference
New method for fast and accurate binding-site identification and analysis
10.1111/j.1747-0285.2007.00483.x · doi-reference
10.1126/science.1136800
10.1126/science.1136800 · doi-reference
Constant pressure molecular dynamics algorithms
10.1063/1.467468 · doi-reference
10.1063/1.447334
10.1063/1.447334 · doi-reference
Canonical dynamics: equilibrium phase-space distributions
10.1103/physreva.31.1695 · doi-reference
10.1021/jp003919d
10.1021/jp003919d · doi-reference
10.1517/17460441.2015.1032936
10.1517/17460441.2015.1032936 · doi-reference
10.1002/jcc.20222
10.1002/jcc.20222 · doi-reference