Evidence map›Paper›PMID 38816130›Full record

ArticleMethods in enzymology2024

Stopped-flow measurement of CO

Liam R Marshall, Olga V Makhlynets

Abstract read
In one paragraph

Article in Methods in enzymology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Liam R MarshallDepartment of Chemistry and Biochemistry, Baylor University, Waco, TX, United States.
Olga V MakhlynetsDepartment of Chemistry and Biochemistry, Baylor University, Waco, TX, United States. Electronic address: olga_makhlynets@baylor.edu.

Funding

From Fundamental Studies of Metalloproteins to Practical ApplicationsR15GM148939 · NIGMS · SYRACUSE UNIVERSITY · PI MAKHLYNETS, OLGA · 2022 to 2022
$310k
NIGMS NIH HHS R15 GM148939
6 · The paper itself

Abstract

With the ever-increasing rates of catalysis shown by catalytic amyloids, the use of faster characterization techniques is required for proper kinetic studies. The same is true for inherently fast chemical reactions. Carbon dioxide hydration is of significant interest to the field of enzyme design, given both carbonic anhydrases' status as a "perfect enzyme" and the central role carbonic anhydrase plays in the respiration and existence of all carbon-based life. Carbon dioxide is an underexplored hydrolysis substrate within the literature, and a lack of a direct spectroscopic marker for reaction monitoring can make studies more complex and require specialist equipment. Within this article we present a method for measuring the carbon dioxide hydration activity of amyloid fibrils.

Indexed as

AmyloidCarbon DioxideCarbonic AnhydrasesCatalysisEnzyme AssaysHumansKineticsWaterAmyloidCarbon DioxideCarbonic AnhydrasesWaterAmyloidsCarbon dioxide hydrationCatalysisPeptidesStopped-flow

Identifiers

PMID38816130
PMCPMC13410719

What OpenQuestion holds

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Registered trials

None linked

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.