{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Pinet L"],"funding":["University of Paris-Sud","Agence Nationale de la Recherche"],"pagination":["1690"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8615588"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(11)"],"pubmed_abstract":["ErbBs are receptor tyrosine kinases involved not only in development, but also in a wide variety of diseases, particularly cancer. Their extracellular, transmembrane, juxtamembrane, and kinase folded domains were described extensively over the past 20 years, structurally and functionally. However, their whole C-terminal tails (CTs) following the kinase domain were only described at atomic resolution in the last 4 years. They were shown to be intrinsically disordered. The CTs are known to be tyrosine-phosphorylated when the activated homo- or hetero-dimers of ErbBs are formed. Their phosphorylation triggers interaction with phosphotyrosine binding (PTB) or Src Homology 2 (SH2) domains and activates several signaling pathways controling cellular motility, proliferation, adhesion, and apoptos"],"journal":["Biomolecules"],"pubmed_title":["Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs."],"pmcid":["PMC8615588"],"funding_grant_id":["ANR-13-BSV8-0016","2019SACLS375"],"pubmed_authors":["Assrir N","van Heijenoort C","Pinet L"],"additional_accession":[]},"is_claimable":false,"name":"Expanding the Disorder-Function Paradigm in the C-Terminal Tails of Erbbs.","description":"ErbBs are receptor tyrosine kinases involved not only in development, but also in a wide variety of diseases, particularly cancer. Their extracellular, transmembrane, juxtamembrane, and kinase folded domains were described extensively over the past 20 years, structurally and functionally. However, their whole C-terminal tails (CTs) following the kinase domain were only described at atomic resolution in the last 4 years. They were shown to be intrinsically disordered. The CTs are known to be tyrosine-phosphorylated when the activated homo- or hetero-dimers of ErbBs are formed. Their phosphorylation triggers interaction with phosphotyrosine binding (PTB) or Src Homology 2 (SH2) domains and activates several signaling pathways controling cellular motility, proliferation, adhesion, and apoptos","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Nov","modification":"2025-04-04T21:10:59.179Z","creation":"2022-02-11T13:22:45.203Z"},"accession":"S-EPMC8615588","cross_references":{"pubmed":["34827688"],"doi":["10.3390/biom11111690"]}}