ArticleJournal of the American Chemical Society2017
The Michaelis Complex of Arginine Kinase Samples the Transition State at a Frequency That Matches the Catalytic Rate.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 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
11 citing papers in PubMed.
- Repurposing a supramolecular iridium catalystChemical science · 2024Article
- Binding of green tea epigallocatechin gallate to the arginine kinase active site from the brown recluse spider (Heliyon · 2024Article
- Arginine Kinase Activates Arginine for Phosphorylation by Pyramidalization and Polarization.ACS catalysis · 2024Article
- Excited-state observation of active K-Ras reveals differential structural dynamics of wild-type versus oncogenic G12D and G12C mutants.Nature structural & molecular biology · 2023Article
- Conserved conformational dynamics determine enzyme activity.Science advances · 2022Article
- Morphology Adjustment and Optimization of CuS as Enzyme Mimics for the High Efficient Colorimetric Determination of Cr(VI) in Water.Nanomaterials (Basel, Switzerland) · 2022Article
- Protein Dynamics revealed by NMR Relaxation Methods.Emerging topics in life sciences · 2020Article
- A Dynamic Switch in Inactive p38γ Leads to an Excited State on the Pathway to an Active Kinase.Biochemistry · 2019Article
- Transitions in DNA polymerase β μs-ms dynamics related to substrate binding and catalysis.Nucleic acids research · 2018Article
- Elevated μs-ms timescale backbone dynamics in the transition state analog form of arginine kinase.Journal of structural biology · 2017Article
- Defining the Structural Basis for Allosteric Product Release from E. coli Dihydrofolate Reductase Using NMR Relaxation Dispersion.Journal of the American Chemical Society · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
Abstract
Arginine kinase (AK), which is a member of the phosphagen kinase family, serves as a model system for studying the structural and dynamic determinants of biomolecular enzyme catalysis of all major states involved of the enzymatic cycle. These states are the apo state (substrate free), the Michaelis complex analogue AK:Arg:Mg·AMPPNP (MCA), a product complex analogue AK:pAIE:Mg·ADP (PCA), and the transition state analogue AK:Arg:Mg·ADP:NO
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.