Evidence map›Paper›PMID 25560074›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2015

Phage selection assisted by Sfp phosphopantetheinyl transferase-catalyzed site-specific protein labeling.

Bo Zhao, Keya Zhang, Karan Bhuripanyo, Yiyang Wang, Han Zhou, Mengnan Zhang, Jun Yin

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2015. 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

7 authors.

Bo ZhaoDepartment of Chemistry, University of Chicago, 929 E57th Street, Chicago, IL, 60637, USA.
Keya Zhang
Karan Bhuripanyo
Yiyang Wang
Han Zhou
Mengnan Zhang
Jun Yin

Funding

Orthogonal Ubiquitin Transfer to Profile E3 Substrate Specificity.R01GM104498 · NIGMS · UNIVERSITY OF CHICAGO · PI KIYOKAWA, HIROAKI, YIN, JUN · 2013 to 2021
$3.2M
NIGMS NIH HHS 1R01GM104498NIGMS NIH HHS R01 GM104498
6 · The paper itself

Abstract

Phosphopantetheinyl transferases (PPTase) Sfp and AcpS catalyze a highly efficient reaction that conjugates chemical probes of diverse structures to proteins. PPTases have been widely used for site-specific protein labeling and live cell imaging of the target proteins. Here we describe the use of PPTase-catalyzed protein labeling in protein engineering by facilitating high-throughput phage selection.

Indexed as

Bacterial ProteinsBiotinBiotinylationEscherichia coliPeptide LibraryProtein EngineeringStaining and LabelingStreptavidinTransferases (Other Substituted Phosphate Groups)Bacterial ProteinsBiotinPeptide Libraryphosphopantetheinyl transferaseStreptavidinTransferases (Other Substituted Phosphate Groups)

Identifiers

PMID25560074
PMCPMC4648548

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.