Evidence map›Paper›PMID 37775659›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Metal-Mediated Ligand Affinity Chemistry (MLAC).

Sailajah Gukathasan, Samuel G Awuah

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. Review
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.

Sailajah GukathasanDepartment of Chemistry, University of Kentucky, Lexington, KY, USA.
Samuel G AwuahDepartment of Chemistry, University of Kentucky, Lexington, KY, USA. awuah@uky.edu.

Funding

Understanding the role of anti-apolipoprotein A-I antibodies in atherosclerotic cardiovascular diseaseP20GM130456 · NIGMS · UNIVERSITY OF KENTUCKY · PI M. Ashfaqul Alam · 2020 to 2026
$18.7M
Q Exactive HF Nanoflow LC Mass Spectrometry SystemS10OD025267 · OD · UNIVERSITY OF COLORADO · PI AHN, NATALIE G. · 2018 to 2018
$600k
NIH HHS S10 OD025267
6 · The paper itself

Abstract

Metal-mediated ligand affinity chemistry (MLAC) enables site-specific protein modification and represents a powerful bioorthogonal strategy. Conventional bioorthogonal methods often involve two steps: (i) incorporation of the bioorthogonal handle (e.g., non-canonical amino acid, enzyme domain, peptide sequences) and (ii) the binding of functional molecules such as drugs, affinity tags, and fluorophores. This two-step protocol often involves genetic manipulation, which makes it impossible to chemically modify endogenous proteins in living systems. Thus, we propose the development of a transition metal-based chemical strategy that is ligand-directed to the endogenous protein of interest in a single step, which we refer to as metal-mediated ligand affinity chemistry (MLAC).

Indexed as

MetalsHumansLigandsProtein BindingProteinsLigandsMetalsProteinsBioconjugationMetal-based covalent modificationMLACProtein modification

Identifiers

PMID37775659

What OpenQuestion holds

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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.