ArticleDatabase : the journal of biological databases and curation2014
PolyprOnline: polyproline helix II and secondary structure assignment database.
Article in Database : the journal of biological databases and curation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- PolyProline Predictor: A web server for empirical sequence-based prediction of polyproline II helices.Protein science : a publication of the Protein Society · 2026Article
- Label-free optical observation of disordered-to-ordered transitions in single intrinsically disordered proteins.Npj biosensing · 2026Article
- An Improved Diabatization Scheme for Computing the Electronic Circular Dichroism of Proteins.The journal of physical chemistry. B · 2024Article
- Exploring the Role of Globular Domain Locations on an Intrinsically Disordered Region of p53: A Molecular Dynamics Investigation.Journal of chemical theory and computation · 2024Article
- Cryo-EM reveals how the mastigoneme assembles and responds to environmental signal changes.The Journal of cell biology · 2023Article
- BERT-PPII: The Polyproline Type II Helix Structure Prediction Model Based on BERT and Multichannel CNN.BioMed research international · 2022Article
- Molecular dynamics simulations of the adsorption of an intrinsically disordered protein: Force field and water model evaluation in comparison with experiments.Frontiers in molecular biosciences · 2022Article
- Residue Folding Degree-Relationship to Secondary Structure Categories and Use as Collective Variable.International journal of molecular sciences · 2021Article
- Sequence features, structure, ligand interaction, and diseases in small leucine rich repeat proteoglycans.Journal of cell communication and signaling · 2021Review
- The Effect of Multisite Phosphorylation on the Conformational Properties of Intrinsically Disordered Proteins.International journal of molecular sciences · 2021Article
- Force Field Effects in Simulations of Flexible Peptides with Varying Polyproline II Propensity.Journal of chemical theory and computation · 2021Article
- Molecular Dynamics Simulations of Phosphorylated Intrinsically Disordered Proteins: A Force Field Comparison.International journal of molecular sciences · 2021Article
- A linker of the proline-threonine repeating motif sequence is bimodal.Journal of molecular modeling · 2020Article
- Physicochemical Characterisation of KEIF-The Intrinsically Disordered N-Terminal Region of Magnesium Transporter A.Biomolecules · 2020Article
- Prediction of polyproline II secondary structure propensity in proteins.Royal Society open science · 2020Article
- ccPDB 2.0: an updated version of datasets created and compiled from Protein Data Bank.Database : the journal of biological databases and curation · 2019Article
- Super Secondary Structure Consisting of a Polyproline II Helix and a β-Turn in Leucine Rich Repeats in Bacterial Type III Secretion System Effectors.The protein journal · 2018Article
- The BackMAP Python module: how a simpler Ramachandran number can simplify the life of a protein simulator.PeerJ · 2018Article
- Article
- Molecular insights into protein synthesis with proline residues.EMBO reports · 2016Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The polyproline helix type II (PPII) is a regular protein secondary structure with remarkable features. Many studies have highlighted different crucial biological roles supported by this local conformation, e.g. in the interactions between biological macromolecules. Although PPII is less frequently present than regular secondary structures such as canonical alpha helices and beta strands, it corresponds to 3-10% of residues. Up to now, PPII is not assigned by most popular assignment tools, and therefore, remains insufficiently studied. PolyprOnline database is, therefore, dedicated to PPII structure assignment and analysis to facilitate the study of PPII structure and functional roles. This database is freely accessible from www.dsimb.inserm.fr/dsimb_tools/polyproline.
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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.