ReviewFrontiers in bioscience (Landmark edition)2009
Diversity of polyproline recognition by EVH1 domains.
Review in Frontiers in bioscience (Landmark edition), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 48 citations in OpenAlex.
- Insights into the Interaction Landscape of the EVH1 Domain of Mena.Biochemistry · 2024Article
- Elaboration of the Homer1 recognition landscape reveals incomplete divergence of paralogous EVH1 domains.Protein science : a publication of the Protein Society · 2024Article
- Elaboration of the Homer1 Recognition Landscape Reveals Incomplete Divergence of Paralogous EVH1 Domains.bioRxiv : the preprint server for biology · 2024Article
- Conserved proline residues prevent dimerization and aggregation in the β-lactamase BlaC.Protein science : a publication of the Protein Society · 2024Article
- Review
- Article
- Two cold shock domain containing proteins trigger the development of infectious Trypanosoma brucei.PLoS pathogens · 2023Article
- PRMT4-mediated arginine methylation promotes tyrosine phosphorylation of VEGFR-2 and regulates filopodia protrusions.iScience · 2022Article
- A proline-rich motif in the large intracellular loop of the glycine receptor α1 subunit interacts with the Pleckstrin homology domain of collybistin.Journal of advanced research · 2021Article
- Novel perspectives of target-binding by the evolutionarily conserved PP4 phosphatase.Open biology · 2020Article
- SPRED proteins and their roles in signal transduction, development, and malignancy.Genes & development · 2020Review
- Transfer of HTLV-1 p8 and Gag to target T-cells depends on VASP, a novel interaction partner of p8.PLoS pathogens · 2020Article
- The Disordered Cellular Multi-Tasker WIP and Its Protein-Protein Interactions: A Structural View.Biomolecules · 2020Review
- Structural Insights into the SPRED1-Neurofibromin-KRAS Complex and Disruption of SPRED1-Neurofibromin Interaction by Oncogenic EGFR.Cell reports · 2020Article
- Membrane-associated mucins of the ocular surface: New genes, new protein functions and new biological roles in human and mouse.Progress in retinal and eye research · 2020Review
- A Consensus Binding Motif for the PP4 Protein Phosphatase.Molecular cell · 2019Article
- P-Bodies: Composition, Properties, and Functions.Biochemistry · 2018Review
- NMR resonance assignments of the EVH1 domain of neurofibromin's recruitment factor Spred1.Biomolecular NMR assignments · 2017Article
- TANGO1/cTAGE5 receptor as a polyvalent template for assembly of large COPII coats.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The neurofibromin recruitment factor Spred1 binds to the GAP related domain without affecting Ras inactivation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Enabled/VASP Homology-1 (EVH1) domains function primarily as interaction modules that link signaling proteins by binding to proline-rich sequences. EVH1 domains are ~115 residues in length and adopt the pleckstrin homology (PH) fold. Four different protein families contain EVH1 domains: Ena/VASP, Homer, WASP and SPRED. Except for the SPRED domains, for which no binding partners are known, EVH1 domains use a conserved hydrophobic cleft to bind a four-residue motif containing 2-4 prolines. Conserved aromatic residues, including an invariant tryptophan, create a wedge-shaped groove on the EVH1 surface that matches the triangular profile of a polyproline type II helix. Hydrophobic residues adjacent to the polyproline motif dock into complementary sites on the EVH1 domain to enhance ligand binding specificity. Pseudosymmetry in the polyproline type II helix allows peptide ligands to bind in either of two N-to-C terminal orientations, depending on interactions between sequences flanking the prolines and the EVH1 domain. EVH1 domains also recognize non-proline motifs, as illustrated by the structure of an EVH1:LIM3 complex and the extended EVH1 ligands of the verprolin family.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.