Evidence map›Paper›PMID 33914511›Full record

ArticleJournal of the American Chemical Society2021

Faster Surface Ligation Reactions Improve Immobilized Enzyme Structure and Activity.

Andres F Chaparro Sosa, Riley M Bednar, Ryan A Mehl, Daniel K Schwartz, Joel L Kaar

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

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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

5 authors.

Andres F Chaparro SosaDepartment of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States.
Riley M BednarDepartment of Biochemistry and Biophysics, Oregon State University, 2011 Agricultural and Life Sciences Building, Corvallis, Oregon 97331-7305, United States.ORCID 0000-0001-9452-825X
Ryan A MehlDepartment of Biochemistry and Biophysics, Oregon State University, 2011 Agricultural and Life Sciences Building, Corvallis, Oregon 97331-7305, United States.ORCID 0000-0003-2932-4941
Daniel K SchwartzDepartment of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States.ORCID 0000-0001-5397-7200
Joel L KaarDepartment of Chemical and Biological Engineering, University of Colorado, Boulder, Colorado 80309, United States.ORCID 0000-0002-0794-3955

Funding

Development of an improved core technology for efficient genetic code expansion in biomedical researchR01GM131168 · NIGMS · OREGON STATE UNIVERSITY · PI MEHL, RYAN A · 2019 to 2021
$1.1M
NIGMS NIH HHS R01 GM131168
6 · The paper itself

Abstract

During integration into materials, the inactivation of enzymes as a result of their interaction with nanometer size denaturing "hotspots" on surfaces represents a critical challenge. This challenge, which has received far less attention than improving the long-term stability of enzymes, may be overcome by limiting the exploration of surfaces by enzymes. One way this may be accomplished is through increasing the rate constant of the surface ligation reaction and thus the probability of immobilization with reactive surface sites (i.e., ligation efficiency). Here, the connection between ligation reaction efficiency and the retention of enzyme structure and activity was investigated by leveraging the extremely fast reaction of strained

Indexed as

Carbonic Anhydrase IIEnzymes, ImmobilizedHumansProtein ConformationProtein UnfoldingSurface PropertiesCarbonic Anhydrase IIEnzymes, Immobilized

Identifiers

PMID33914511
PMCPMC8574164

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.