ArticleMethods in molecular biology (Clifton, N.J.)2020
IDP-LZerD: Software for Modeling Disordered Protein Interactions.
Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Peptide-protein docking: from physics-based models to generative intelligence.Chemical communications (Cambridge, England) · 2026Review
- A deep learning method for predicting interactions for intrinsically disordered regions of proteins.bioRxiv : the preprint server for biology · 2025Article
- Evaluation of predictions of disordered binding regions in the CAID2 experiment.Computational and structural biotechnology journal · 2025Review
- Computational Methods to Investigate Intrinsically Disordered Proteins and their Complexes.ArXiv · 2024Article
- Predicting Protein-Peptide Interactions: Benchmarking Deep Learning Techniques and a Comparison with Focused Docking.Journal of chemical information and modeling · 2023Article
- Recent Advances in NMR Protein Structure Prediction with ROSETTA.International journal of molecular sciences · 2023Review
- Pairwise and Multi-chain Protein Docking Enhanced Using LZerD Web Server.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Computational prediction of disordered binding regions.Computational and structural biotechnology journal · 2023Review
- Multi-level analysis of intrinsically disordered protein docking methods.Methods (San Diego, Calif.) · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Modeling the tertiary structure of protein-protein interaction complex has been well studied over many years, especially in the case where the structures of both binding partners are roughly the same before and after binding. However, the assembly of complexes with less-ordered partners is a much harder problem, and modeling even small amounts of flexibility can pose a challenge. In an extreme case, where one of the binding partners is intrinsically disordered before binding, we have previously shown that by initially disregarding the coupling between windows of these intrinsically disordered proteins (IDPs), we can reliably assemble complexes involving IDPs up to at least 69 residues long. Here, we detail the use of the IDP-LZerD package and protocol.
Indexed as
Identifiers
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.