Evidence map›Paper›PMID 37668981›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2023

Engineering of SH2 Domains for the Recognition of Protein Tyrosine O-Sulfation Sites.

Sean Paul Waldrop, Wei Niu, Jiantao Guo

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2023. 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, top 61% of its field
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, 0 citations in OpenAlex.

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

3 authors at 1 institution in 1 country.

Sean Paul WaldropDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE, USA.
Wei NiuDepartment of Chemical & Biomolecular Engineering, University of Nebraska-Lincoln, Lincoln, NE, USA.
Jiantao GuoDepartment of Chemistry, University of Nebraska-Lincoln, Lincoln, NE, USA. jguo4@unl.edu.
University of Nebraska–Lincoln · US

Funding

Development of proximity-induced fluorogenic reactions for imaging biomolecular interaction through noncanonical amino acid mutagenesis in response to quadruplet codon and recoding signalR01GM138623 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI GUO, JIANTAO · 2020 to 2021
$613k
Defining, studying, and targeting sulfated tyrosine residues of cell surface receptors for disease treatmentR01GM147785 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI GUO, JIANTAO · 2022 to 2022
$301k
NIGMS NIH HHS R01 GM138623NIGMS NIH HHS R01 GM147785
6 · The paper itself

Abstract

Protein engineering has brought advances to industrial processes, biomaterials, nanotechnology, biosensors, and biomedical applications. This chapter will focus on the engineering of Src Homology 2 domains (SH2) to act as an antibody mimetic for the recognition of sulfotyrosine-containing peptides or proteins. In comparison to anti-sulfotyrosine antibodies, SH2 mutants have much smaller size and can be heterologously expressed and purified in large quantity at low cost. This chapter will describe the use of phage display to identify a sulfotyrosine-binding SH2 mutant and the subsequent enrichment of sulfotyrosine-containing peptides in complex biological samples.

Indexed as

Bacteriophagessrc Homology DomainsAntibodiesBiocompatible MaterialsTyrosineAntibodiesBiocompatible MaterialsTyrosinePhage displayProtein engineeringProtein tyrosine O-sulfationSrc Homology 2 domainSulfotyrosine

Identifiers

PMID37668981
OpenAlexW4386438789

What OpenQuestion holds

Textmetadata
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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.