Evidence map›Paper›PMID 31059184›Full record

ArticleChembiochem : a European journal of chemical biology2019

Exploring the Functional Consequences of Protein Backbone Alteration in Ubiquitin through Native Chemical Ligation.

Halina M Werner, Samuel K Estabrooks, G Michael Preston, Jeffrey L Brodsky, W Seth Horne

Abstract read
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Interplay between CChembiochem : a European journal of chemical biology · 2025
    Article
  6. Backbone Modification in a Protein Hydrophobic Core.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  7. Article
  8. Article
  9. 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

5 authors.

Halina M WernerDepartment of Chemistry, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.
Samuel K EstabrooksDepartment of Biological Sciences, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.
G Michael PrestonDepartment of Biological Sciences, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.
Jeffrey L BrodskyDepartment of Biological Sciences, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.
W Seth HorneDepartment of Chemistry, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, PA, 15260, USA.ORCID 0000-0003-2927-1739

Funding

ER Associated Degradation of Membrane Proteins in YeastR01GM075061 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BRODSKY, JEFFREY L. · 2006 to 2019
$3.2M
Renal and Epithelial Biology Training ProgramT32DK061296 · NIDDK · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI KLEYMAN, THOMAS R · 2002 to 2022
$3.1M
Molecular Mimics of Protein Tertiary Folding from Primary Sequence InformationR01GM107161 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HORNE, WILLIAM SETH · 2013 to 2022
$2.6M
Cystic Fibrosis Foundation BRODSK18G0Division of Chemistry 1625002NIDDK NIH HHS T32 DK061296NIGMS NIH HHS GM075061NIGMS NIH HHS GM107161NIGMS NIH HHS R01 GM075061NIGMS NIH HHS R01 GM107161
6 · The paper itself

Abstract

Ubiquitin (Ub) plays critical roles in myriad protein degradation and signaling networks in the cell. We report herein Ub mimetics based on backbones that blend natural and artificial amino acid units. The variants were prepared by a modular route based on native chemical ligation. Biological assays show that some are enzymatically polymerized onto protein substrates, and that the resulting Ub tags are recognized for downstream pathways. These results advance the size and complexity of folded proteins mimicked by artificial backbones and expand the functional scope of such agents.

Indexed as

Amino Acid SequenceBiological AssayProtein ConformationProtein FoldingUbiquitinsUbiquitinsfoldamersheterogeneous backbonesnative chemical ligationprotein mimeticsubiquitin

Identifiers

PMID31059184
PMCPMC6752966

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.