Evidence map›Paper›PMID 37549799›Full record

ArticleMethods (San Diego, Calif.)2023

Combining non-canonical amino acid mutagenesis and native chemical ligation for multiply modifying proteins: A case study of α-synuclein post-translational modifications.

Ana Galesic, Buyan Pan, Jennifer Ramirez, Elizabeth Rhoades, Matthew R Pratt, E James Petersson

Open access · greenAbstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2023. 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
0.4field-weighted citation impact, top 35% 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, 2 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

6 authors at 2 institutions in 1 country.

Ana GalesicDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.
Buyan PanDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104, USA.
Jennifer RamirezGraduate Group in Biochemistry and Molecular Biophysics, Perelman School of Medicine, University of Pennsylvania, 421 Curie Boulevard, Philadelphia, PA 19104, USA.
Elizabeth RhoadesDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104, USA; Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, 421 Curie Boulevard, Philadelphia, PA 19104, USA.
Matthew R PrattDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.
E James PeterssonDepartment of Chemistry, University of Pennsylvania, 231 South 34th Street, Philadelphia, PA 19104, USA; Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, 421 Curie Boulevard, Philadelphia, PA 19104, USA. Electronic address: ejpetersson@sas.upenn.edu.
University of Pennsylvania · USUniversity of Southern California · US

Funding

The GCE4All Center: Unleashing the Potential of Genetic Code Expansion for Biomedical ResearchRM1GM144227 · NIGMS · OREGON STATE UNIVERSITY · PI RYAN A MEHL · 2022 to 2026
$6.2M
Functional Analysis of O-GlcNAc using Synthetic Protein ChemistryR01GM114537 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI PRATT, MATTHEW ROBERT · 2015 to 2024
$3.1M
Predoctoral Training at the Chemistry-Biology InterfaceT32GM133398 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI Ronen Marmorstein, Ernest James Petersson · 2020 to 2026
$2.4M
Combinatorial effects of PTMs on a-Synuclein structure, function and aggregationRF1NS125770 · NINDS · UNIVERSITY OF PENNSYLVANIA · PI PETERSSON, ERNEST JAMES, RHOADES, ELIZABETH · 2022 to 2022
$1.7M
Bruker RapifleX MALDI TOF/TOF Mass SpectrometerS10OD030460 · OD · UNIVERSITY OF PENNSYLVANIA · PI PETERSSON, ERNEST JAMES · 2021 to 2021
$881k
NIGMS NIH HHS R01 GM114537NIGMS NIH HHS RM1 GM144227NIGMS NIH HHS T32 GM133398NIH HHS S10 OD030460NINDS NIH HHS RF1 NS125770
6 · The paper itself

Abstract

The Parkinson's disease associated protein α-synuclein (αS) has been found to contain numerous post-translational modifications (PTMs), in both physiological and pathological states. One PTM site of particular interest is serine 87, which is subject to both O-linked β-N-acetylglucosamine (gS) modification and phosphorylation (pS), with αS-pS

Indexed as

alpha-SynucleinParkinson DiseaseAmino AcidsHumansMutagenesisProtein Processing, Post-Translationalalpha-SynucleinAmino Acids

Identifiers

PMID37549799
PMCPMC10657485
OpenAlexW4385613096

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.