ArticleProceedings of the National Academy of Sciences of the United States of America2013
Diffusion modifies the connectivity of kinetic schemes for multisite binding and catalysis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed.
- Assembling a single active pocket from enzyme and metal modules for simultaneously catalyzing oxidation-reduction cascades.Nature communications · 2026Article
- Kinetics of diffusion-influenced multisite phosphorylation with enzyme reactivation.Biopolymers · 2024Article
- Vectorial channeling as a mechanism for translational control by functional prions and condensates.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cluster Channeling in Cascade Reactions.The journal of physical chemistry. B · 2021Article
- Multisite reversible association in membranes and solutions: From non-Markovian to Markovian kinetics.The Journal of chemical physics · 2020Article
- Diffusion-induced competitive two-site binding.The Journal of chemical physics · 2019Article
- Theory of Diffusion-Influenced Reaction Networks.The journal of physical chemistry. B · 2018Article
- Receptor recharge time drastically reduces the number of captured particles.PLoS computational biology · 2018Article
- A mechanism of T cell dependent selection of antigen engaged Germinal Center B cells.PloS one · 2018Article
- Allosteric Modulation of Grb2 Recruitment to the Intrinsically Disordered Scaffold Protein, LAT, by Remote Site Phosphorylation.Journal of the American Chemical Society · 2017Article
- Including Rebinding Reactions in Well-Mixed Models of Distributive Biochemical Reactions.Biophysical journal · 2016Article
- Reversible Stochastically Gated Diffusion-Influenced Reactions.The journal of physical chemistry. B · 2016Article
- Long-term dynamics of multisite phosphorylation.Molecular biology of the cell · 2016Article
- Influence of diffusion on the kinetics of multisite phosphorylation.Protein science : a publication of the Protein Society · 2016Article
- The robustness of proofreading to crowding-induced pseudo-processivity in the MAPK pathway.Biophysical journal · 2014Article
- The Berg-Purcell limit revisited.Biophysical journal · 2014Article
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.
Funding
Abstract
The simplest way to describe the influence of the relative diffusion of the reactants on the time course of bimolecular reactions is to modify or renormalize the phenomenological rate constants that enter into the rate equations of conventional chemical kinetics. However, for macromolecules with multiple inequivalent reactive sites, this is no longer sufficient, even in the low concentration limit. The physical reason is that an enzyme (or a ligand) that has just modified (or dissociated from) one site can bind to a neighboring site rather than diffuse away. This process is not described by the conventional chemical kinetics, which is only valid in the limit that diffusion is fast compared with reaction. Using an exactly solvable many-particle reaction-diffusion model, we show that the influence of diffusion on the kinetics of multisite binding and catalysis can be accounted for by not only scaling the rates, but also by introducing new connections into the kinetic scheme. The rate constants that describe these new transitions or reaction channels turn out to have a transparent physical interpretation: The chemical rates are scaled by the appropriate probabilities that a pair of reactants, which are initially in contact, bind rather than diffuse apart. The theory is illustrated by application to phosphorylation of a multisite substrate.
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.