Evidence map›Paper›PMID 35278475›Full record

ArticleJournal of molecular biology2022

A Designed, Highly Efficient Pyrrolysyl-tRNA Synthetase Mutant Binds o-Chlorophenylalanine Using Two Halogen Bonds.

Erol C Vatansever, Kai S Yang, Zhi Zachary Geng, Yuchen Qiao, Pingwei Li, Shiqing Xu, Wenshe Ray Liu

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

8 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Update of the Pyrrolysyl-tRNA Synthetase/tRNAJournal of bacteriology · 2023
    Review
  8. 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

7 authors at 1 institution in 1 country.

Erol C VatanseverThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Kai S YangThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Zhi Zachary GengThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Yuchen QiaoThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Pingwei LiDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
Shiqing XuThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA.
Wenshe Ray LiuThe Texas A&M Drug Discovery Laboratory, Department of Chemistry, Texas A&M University, College Station, TX 77843, USA; Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA; Institute of Biosciences and Technology and Department of Translational Medical Sciences, College of Medicine, Texas A&M University, Houston, TX 77030, USA; Department of Molecular and Cellular Medicine, College of Medicine, Texas A&M University, College Station, TX 77843, USA. Electronic address: wsliu2007@tamu.edu.
Texas A&M University · US

Funding

Develop General Methods for the Synthesis of Proteins with Posttranslational Lysine ModificationsR01GM127575 · NIGMS · TEXAS A&M UNIVERSITY · PI LIU, WENSHE RAY · 2019 to 2022
$1.4M
Studying Reversible Histone Acylations in Nucleosome ContextsR01GM121584 · NIGMS · TEXAS A&M UNIVERSITY · PI LIU, WENSHE RAY · 2017 to 2020
$1.3M
NIGMS NIH HHS R01 GM121584NIGMS NIH HHS R01 GM127575
6 · The paper itself

Abstract

As one of the most valuable tools for genetic code expansion, pyrrolysyl-tRNA synthetase (PylRS) is structurally related to phenylalanyl-tRNA synthetase (PheRS). By introducing mutations that mimic ligand interactions in PheRS into PylRS, we designed a PylRS mutant. This mutant, designated as oClFRS, recognizes a number of o-substituted phenylalanines for their genetic incorporation at amber codon. Its efficiency in catalyzing genetic incorporation of o-chlorophenylalanine (o-ClF) is better than that for N

Indexed as

Amino Acyl-tRNA SynthetasesGenetic CodeMethanosarcinaPhenylalanineHalogensLysineMutationProtein BindingAmino Acyl-tRNA SynthetasesHalogensLysinePhenylalaninepyrrolysineamber suppressionhalogen bondnoncanonical amino acidO-chlorophenylalaninepyrrolysyl-tRNA synthetase

Identifiers

PMID35278475
PMCPMC9018553
OpenAlexW4220837588

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.