Screening a Molecular Fragment Library to Modulate the PED/PEA15-Phospholipase D1 Interaction in Cellular Lysate Environments-Reference-Cited by-同舟云学术

Screening a Molecular Fragment Library to Modulate the PED/PEA15-Phospholipase D1 Interaction in Cellular Lysate Environments

Published:2021-11-26 Issue:12 Volume:16 Page:2798-2807
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Farina Biancamaria¹,Pirone Luciano¹,D’Abrosca Gianluca²,Della Valle Maria²,Russo Luigi²,Isernia Carla²^ORCID,Sassano Marica²,Del Gatto Annarita¹,Di Gaetano Sonia¹,Zaccaro Laura¹^ORCID,Malgieri Gaetano²^ORCID,Pedone Emilia M.¹,Fattorusso Roberto²^ORCID

Affiliation:

1. Istituto di Biostrutture e Bioimmagini, CNR, via Mezzocannone 16, 80134 Napoli, Italy

2. Dipartimento di Scienze e Tecnologie Ambientali, Biologiche e Farmaceutiche, Università degli Studi della Campania─L. Vanvitelli, Via Vivaldi 43, 81100 Caserta, Italy

Funder

Ministero dell'Istruzione, dell'UniversitÃ e della Ricerca

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.1c00688

Reference46 articles.

1. Characterization of PEA-15, a major substrate for protein kinase C in astrocytes.

2. The Major Astrocytic Phosphoprotein PEA-15 Is Encoded by Two mRNAs Conserved on Their Full Length in Mouse and Human

3. Frontiers: PED/PEA-15, a multifunctional protein controlling cell survival and glucose metabolism

4. Recognition of ERK MAP kinase by PEA-15 reveals a common docking site within the death domain and death effector domain

5. High-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions

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