ReviewFEBS open bio2021
Do polyproline II helix associations modulate biomolecular condensates?
Review in FEBS open bio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 26 citations in OpenAlex.
- PolyProline Predictor: A web server for empirical sequence-based prediction of polyproline II helices.Protein science : a publication of the Protein Society · 2026Article
- Orientation affects hydrogen bonding cooperativity in polyproline II helical bundles.Communications chemistry · 2025Article
- Evolutionary perspective of the CAG/CAA interplay coding for pure polyglutamine stretches in proteins.NAR genomics and bioinformatics · 2025Article
- Profilin Pfy1 is critical for cell wall integrity and virulence inMicrobiology spectrum · 2025Article
- Revealing an origin of temperature-dependent structural change in intrinsically disordered proteins.Biophysical journal · 2025Article
- Site-Specific Incorporation of Fluorinated Prolines into Proteins and Their Impact on Neighbouring Residues.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Hydrogen bonding patterns and cooperativity in polyproline II helical bundles.Communications chemistry · 2024Article
- Proline, a unique amino acid whose polymer, polyproline II helix, and its analogues are involved in many biological processes: a review.Amino acids · 2024Review
- Insight into polyproline II helical bundle stability in an antifreeze protein denatured state.Biophysical journal · 2022Article
- BERT-PPII: The Polyproline Type II Helix Structure Prediction Model Based on BERT and Multichannel CNN.BioMed research international · 2022Article
- AlphaFold 2 and NMR Spectroscopy: Partners to Understand Protein Structure, Dynamics and Function.Frontiers in molecular biosciences · 2022Review
- Entering the second decade: FEBS Open Bio in 2022.FEBS open bio · 2022Article
- Glycine-Rich Peptides from FUS Have an Intrinsic Ability to Self-Assemble into Fibers and Networked Fibrils.Biochemistry · 2021Article
- Membraneless organelles: a smart design for metabolic control.FEBS open bio · 2021Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biomolecular condensates are microdroplets that form inside cells and serve to selectively concentrate proteins, RNAs and other molecules for a variety of physiological functions, but can contribute to cancer, neurodegenerative diseases and viral infections. The formation of these condensates is driven by weak, transient interactions between molecules. These weak associations can operate at the level of whole protein domains, elements of secondary structure or even moieties composed of just a few atoms. Different types of condensates do not generally combine to form larger microdroplets, suggesting that each uses a distinct class of attractive interactions. Here, we address whether polyproline II (PPII) helices mediate condensate formation. By combining with PPII-binding elements such as GYF, WW, profilin, SH3 or OCRE domains, PPII helices help form lipid rafts, nuclear speckles, P-body-like neuronal granules, enhancer complexes and other condensates. The number of PPII helical tracts or tandem PPII-binding domains can strongly influence condensate stability. Many PPII helices have a low content of proline residues, which hinders their identification. Recently, we characterized the NMR spectral properties of a Gly-rich, Pro-poor protein composed of six PPII helices. Based on those results, we predicted that many Gly-rich segments may form PPII helices and interact with PPII-binding domains. This prediction is being tested and could join the palette of verified interactions contributing to biomolecular condensate formation.
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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.