Evidence map›Paper›PMID 32539119›Full record

ReviewBiochemical Society transactions2020

Engineered peptide ligases for cell signaling and bioconjugation.

Clara L Frazier, Amy M Weeks

Open access · greenAbstract readReview
In one paragraph

Review in Biochemical Society transactions, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 8 citations in OpenAlex.

  1. Review
  2. Article
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 at 1 institution in 1 country.

Clara L FrazierDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, U.S.A.
Amy M WeeksDepartment of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, U.S.A.
University of Wisconsin–Madison · US

Funding

BIOTECHNOLOGY TRAINING PROGRAMT32GM008349 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI FOX, BRIAN G · 1989 to 2019
$22.5M
Biotechnology Training ProgramT32GM135066 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI SCOTT M. COYLE, BRIAN G FOX · 2020 to 2026
$7.0M
NIGMS NIH HHS T32 GM008349NIGMS NIH HHS T32 GM135066
6 · The paper itself

Abstract

Enzymes that catalyze peptide ligation are powerful tools for site-specific protein bioconjugation and the study of cellular signaling. Peptide ligases can be divided into two classes: proteases that have been engineered to favor peptide ligation, and protease-related enzymes with naturally evolved peptide ligation activity. Here, we provide a review of key natural peptide ligases and proteases engineered to favor peptide ligation activity. We cover the protein engineering approaches used to generate and improve these tools, along with recent biological applications, advantages, and limitations associated with each enzyme. Finally, we address future challenges and opportunities for further development of peptide ligases as tools for biological research.

Indexed as

Signal TransductionAnimalsAsparaginyl EndopeptidaseCatalysisCathepsin ACysteine EndopeptidasesGenetic VariationHumansLigasesPeptide HydrolasesPeptidesProtein EngineeringSubtilisinTrypsinAsparaginyl EndopeptidaseCathepsin ACysteine EndopeptidasesLigasesPeptide HydrolasesPeptidesSubtilisinTrypsinbioconjugationpeptide ligaseproteaseprotein engineeringprotein terminiproteomics

Identifiers

PMID32539119
PMCPMC8350744
OpenAlexW3034263621

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.