Evidence map›Paper›PMID 34585207›Full record

ArticleOrganic & biomolecular chemistry2021

A glutamic acid-based traceless linker to address challenging chemical protein syntheses.

Riley J Giesler, Paul Spaltenstein, Michael T Jacobsen, Weiliang Xu, Mercedes Maqueda, Michael S Kay

Open access · greenAbstract read
In one paragraph

Article in Organic & biomolecular chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed, 10 citations in OpenAlex.

  1. Review
  2. Article
  3. 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

6 authors at 3 institutions in 2 countries.

Riley J GieslerDepartment of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East, Room 4100, Salt Lake City, Utah 84112-5650, USA. kay@biochem.utah.edu.
Paul SpaltensteinDepartment of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East, Room 4100, Salt Lake City, Utah 84112-5650, USA. kay@biochem.utah.edu.ORCID 0000-0003-0476-7287
Michael T JacobsenDepartment of Pediatrics, Division of Diabetes and Endocrinology, Stanford University, Palo Alto, CA 94304, USA.
Weiliang XuDepartment of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East, Room 4100, Salt Lake City, Utah 84112-5650, USA. kay@biochem.utah.edu.
Mercedes MaquedaDepartamento de Microbiología, Universidad de Granada, Avda. Fuentenueva, s/n, 18071 Granada, Spain.
Michael S KayDepartment of Biochemistry, University of Utah School of Medicine, 15 North Medical Drive East, Room 4100, Salt Lake City, Utah 84112-5650, USA. kay@biochem.utah.edu.ORCID 0000-0003-3186-9684
University of Utah · USStanford University · USUniversidad de Granada · ES

Funding

Virus TransmissionP50AI150464 · NIAID · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2019 to 2021
$14.9M
D-peptide Inhibitors of HIV-1 EntryR01AI076168 · NIAID · UNIVERSITY OF UTAH · PI KAY, MICHAEL S · 2008 to 2017
$3.1M
Program for Interdisciplinary Training in CHemical BiologyT32GM122740 · NIGMS · UNIVERSITY OF UTAH · PI KAY, MICHAEL S · 2018 to 2022
$932k
NIAID NIH HHS P50 AI150464NIAID NIH HHS R01 AI076168NIGMS NIH HHS T32 GM122740
6 · The paper itself

Abstract

Native chemical ligation (NCL) enables the total chemical synthesis of proteins. However, poor peptide segment solubility remains a frequently encountered challenge. Here we introduce a traceless linker that can be temporarily attached to Glu side chains to overcome this problem. This strategy employs a new tool, Fmoc-Glu(AlHx)-OH, which can be directly installed using standard Fmoc-based solid-phase peptide synthesis. The incorporated residue, Glu(AlHx), is stable to a wide range of chemical protein synthesis conditions and is removed through palladium-catalyzed transfer under aqueous conditions. General handling characteristics, such as efficient incorporation, stability and rapid removal were demonstrated through a model peptide modified with Glu(AlHx) and a Lys

Indexed as

BacteriocinsChemistry Techniques, SyntheticGlutamic AcidPeptidesbacteriocin AS-48, Enterococcus faecalisBacteriocinsGlutamic AcidPeptides

Identifiers

PMID34585207
PMCPMC8604549
OpenAlexW3201029773

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.