ReviewThe Journal of biological chemistry2016
Insights into Coupled Folding and Binding Mechanisms from Kinetic Studies.
Review in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 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
81 citing papers in PubMed.
- Dock-and-lock binding of SxIP ligands is required for stable and selective EB1 interactions.eLife · 2025Article
- Hierarchical folding-upon-binding of an intrinsically disordered protein.Nature communications · 2025Article
- Phosphorylation of the protamine-like protein from baculovirus affects its DNA binding and virus propagation.Nucleic acids research · 2025Article
- Anion Binding and Aggregation ofACS omega · 2025Article
- Mutations to transcription factor MAX allosterically increase DNA selectivity by altering folding and binding pathways.Nature communications · 2025Article
- The transition state for coupled folding and binding of a disordered DNA binding domain resembles the unbound state.Nucleic acids research · 2024Article
- Design of amyloidogenic peptide traps.Nature chemical biology · 2024Article
- The molecular basis for cellular function of intrinsically disordered protein regions.Nature reviews. Molecular cell biology · 2024Review
- Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Folding-upon-binding pathways of an intrinsically disordered protein from a deep Markov state model.bioRxiv : the preprint server for biology · 2023Article
- Functional regulation of an intrinsically disordered protein via a conformationally excited state.Science advances · 2023Article
- Folding of Staphylococcal Nuclease Induced by Binding of Chemically Modified Substrate Analogues Sheds Light on Mechanisms of Coupled Folding/Binding Reactions.Biochemistry · 2023Article
- A tile model of circuit topology for self-entangled biopolymers.Scientific reports · 2023Article
- Evolutionary fine-tuning of residual helix structure in disordered proteins manifests in complex structure and lifetime.Communications biology · 2023Article
- Leaderless secretory proteins of the neurodegenerative diseases via TNTs: a structure-function perspective.Frontiers in molecular neuroscience · 2023Review
- Coupled binding and folding of disordered SPIN N-terminal region in myeloperoxidase inhibition.Frontiers in molecular biosciences · 2023Article
- Portability of a Small-Molecule Binding Site between Disordered Proteins.Biomolecules · 2022Article
- A modular approach to map out the conformational landscapes of unbound intrinsically disordered proteins.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Dilute phase oligomerization can oppose phase separation and modulate material properties of a ribonucleoprotein condensate.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- The origin and impact of bound water around intrinsically disordered proteins.Biophysical journal · 2022Article
21 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
Abstract
Intrinsically disordered proteins (IDPs) are characterized by a lack of persistent structure. Since their identification more than a decade ago, many questions regarding their functional relevance and interaction mechanisms remain unanswered. Although most experiments have taken equilibrium and structural perspectives, fewer studies have investigated the kinetics of their interactions. Here we review and highlight the type of information that can be gained from kinetic studies. In particular, we show how kinetic studies of coupled folding and binding reactions, an important class of signaling event, are needed to determine mechanisms.
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.