Evidence map›Paper›PMID 26120904›Full record

ReviewBiomolecules2015

Synthetic Proteins and Peptides for the Direct Interrogation of α-Synuclein Posttranslational Modifications.

Matthew R Pratt, Tharindumala Abeywardana, Nicholas P Marotta

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biomolecules, 2015. 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
0.7field-weighted citation impact, top 28% 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, 13 citations in OpenAlex.

  1. Review
  2. Chemical Synthesis of Microtubule-Associated Protein Tau.Journal of the American Chemical Society · 2023
    Article
  3. Review
  4. Review
  5. Article
  6. Molecular Interrogation to Crack the Case of O-GlcNAc.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020
    Review
  7. Article
  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

3 authors at 1 institution in 1 country.

Matthew R PrattDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA. matthew.pratt@usc.edu.
Tharindumala AbeywardanaDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA. abeyward@usc.edu.
Nicholas P MarottaDepartment of Chemistry, University of Southern California, Los Angeles, CA 90089, USA. nmarotta@usc.edu.
University of Southern California · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

α-Synuclein is the aggregation-prone protein associated with Parkinson's disease (PD) and related neurodegenerative diseases. Complicating both its biological functions and toxic aggregation are a variety of posttranslational modifications. These modifications have the potential to either positively or negatively affect α-synuclein aggregation, raising the possibility that the enzymes that add or remove these modifications could be therapeutic targets in PD. Synthetic protein chemistry is uniquely positioned to generate site-specifically and homogeneously modified proteins for biochemical study. Here, we review the application of synthetic peptides and proteins towards understanding the effects of α-synuclein posttranslational modifications.

Indexed as

alpha-SynucleinAnimalsChemistry Techniques, SyntheticHumansPeptidesProtein Processing, Post-TranslationalProteinsalpha-SynucleinPeptidesProteinsposttranslational modificationssynthesisSynuclein

Identifiers

PMID26120904
PMCPMC4598748
OpenAlexW2109276441

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.