Evidence map›Paper›PMID 35742970›Full record

ArticleInternational journal of molecular sciences2022

Integration of Adenylate Kinase 1 with Its Peptide Conformational Imprint.

Cheng-Hsin Wu, Chung-Yin Lin, Tzu-Chieh Lin, Dar-Fu Tai

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2022. 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

4 authors.

Cheng-Hsin WuDepartment of Chemistry, National Dong Hwa University, Hualien 97403, Taiwan.
Chung-Yin LinMedical Imaging Research Center, Institute for Radiological Research, Chang Gung University, Taoyuan 33302, Taiwan.
Tzu-Chieh LinDepartment of Chemistry, National Dong Hwa University, Hualien 97403, Taiwan.
Dar-Fu TaiDepartment of Chemistry, National Dong Hwa University, Hualien 97403, Taiwan.

Funding

The Ministry of Science and Technology (MOST) Taiwan 100-213-M-259-001-MY3The Ministry of Science and Technology (MOST) Taiwan 109-221-E-182-008-MY3
6 · The paper itself

Abstract

In the present study, molecularly imprinted polymers (MIPs) were used as a tool to grasp a targeted α-helix or β-sheet of protein. During the fabrication of the hinge-mediated MIPs, elegant cavities took shape in a special solvent on quartz crystal microbalance (QCM) chips. The cavities, which were complementary to the protein secondary structure, acted as a peptide conformational imprint (PCI) for adenylate kinase 1 (AK1). We established a promising strategy to examine the binding affinities of human AK1 in conformational dynamics using the peptide-imprinting method. Moreover, when bound to AK1, PCIs are able to gain stability and tend to maintain higher catalytic activities than free AK1. Such designed fixations not only act on hinges as accelerators; some are also inhibitors. One example of PCI inhibition of AK1 catalytic activity takes place when PCI integrates with an AK1

Indexed as

Molecular ImprintingAdenylate KinaseHumansPeptidesProteinsQuartz Crystal Microbalance TechniquesAdenylate Kinaseadenylate kinase 1PeptidesProteinsadenylate kinase 1conformationinhibitionmolecularly imprinted polymerssecondary structure

Identifiers

PMID35742970
PMCPMC9223553

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Registered trials

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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.