Evidence map›Paper›PMID 31034889›Full record

ArticleJournal of molecular biology2019

Alpha-Synuclein Is a Target of Fic-Mediated Adenylylation/AMPylation: Possible Implications for Parkinson's Disease.

Anwesha Sanyal, Sayan Dutta, Ali Camara, Aswathy Chandran, Antonius Koller, Ben G Watson, Ranjan Sengupta, Daniel Ysselstein, Paola Montenegro, Jason Cannon and 2 more

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

24 citing papers in PubMed, 45 citations in OpenAlex.

  1. bioRxiv : the preprint server for biology · 2026
    Article
  2. AMPylation: key roles in biological regulation across prokaryotes and eukaryotes.Frontiers in cellular and infection microbiology · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Peptide-based drugs in immunotherapy: current advances and future prospects.Medical oncology (Northwood, London, England) · 2025
    Review
  7. Review
  8. Article
  9. Article
  10. The Alarmone Diadenosine Tetraphosphate as a Cosubstrate for Protein AMPylation.Angewandte Chemie (International ed. in English) · 2023
    Article
  11. Anti-Cancer Peptides: Status and Future Prospects.Molecules (Basel, Switzerland) · 2023
    Review
  12. Review
  13. Article
  14. Article
  15. Production of an Active, Human Membrane Protein inInternational journal of molecular sciences · 2022
    Article
  16. Article
  17. Article
  18. Article
  19. Bio-protocol · 2020
    Article
  20. 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

12 authors at 2 institutions in 1 country.

Anwesha SanyalDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA; Department of Biochemistry, Purdue University, West Lafayette, IN 47907, USA.
Sayan DuttaDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA.
Ali CamaraDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Aswathy ChandranDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA.
Antonius KollerHerbert Irving Comprehensive Cancer Center, Columbia University Medical Center, New York, NY, USA.
Ben G WatsonDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Ranjan SenguptaDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA.
Daniel YsselsteinDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA.
Paola MontenegroDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA.
Jason CannonSchool of Health Sciences, Purdue University, 915 W State St., LILYG-227, West Lafayette, IN 47907, USA.
Jean-Christophe RochetDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA; Purdue Institute for Integrative Neuroscience, 915 W State St., LILYG-227, West Lafayette, IN 47907, USA.
Seema MattooDepartment of Biological Sciences, Purdue University, West Lafayette, IN 47907, USA; Purdue Institute for Inflammation, Immunology and Infectious Disease, Purdue University, 915 W State St., LILYG-227, West Lafayette, IN 47907, USA. Electronic address: smattoo@purdue.edu.
Purdue University West Lafayette · USColumbia University Irving Medical Center · US

Funding

Mechanisms of PhIP-induced dopaminergic neurotoxicityR01ES025750 · NIEHS · PURDUE UNIVERSITY · PI Jason R Cannon · 2016 to 2026
$4.2M
Role of Fic Proteins in Cellular SignalingR01GM100092 · NIGMS · PURDUE UNIVERSITY · PI MATTOO, SEEMA · 2015 to 2019
$1.7M
NIEHS NIH HHS R01 ES025750NIGMS NIH HHS R01 GM100092
6 · The paper itself

Abstract

During disease, cells experience various stresses that manifest as an accumulation of misfolded proteins and eventually lead to cell death. To combat this stress, cells activate a pathway called unfolded protein response that functions to maintain endoplasmic reticulum (ER) homeostasis and determines cell fate. We recently reported a hitherto unknown mechanism of regulating ER stress via a novel post-translational modification called Fic-mediatedadenylylation/AMPylation. Specifically, we showed that the human Fic (filamentation induced by cAMP) protein, HYPE/FicD, catalyzes the addition of an adenosine monophosphate (AMP) to the ER chaperone, BiP, to alter the cell's unfolded protein response-mediated response to misfolded proteins. Here, we report that we have now identified a second target for HYPE-alpha-synuclein (αSyn), a presynaptic protein involved in Parkinson's disease. Aggregated αSyn has been shown to induce ER stress and elicit neurotoxicity in Parkinson's disease models. We show that HYPE adenylylates αSyn and reduces phenotypes associated with αSyn aggregation invitro, suggesting a possible mechanism by which cells cope with αSyn toxicity.

Indexed as

Adenosine Monophosphatealpha-SynucleinAnimalsCell LineChemokine CCL7Endoplasmic ReticulumEndoplasmic Reticulum StressHEK293 CellsHumansMiceParkinson DiseaseProtein Processing, Post-TranslationalRatsUnfolded Protein ResponseAdenosine Monophosphatealpha-SynucleinCCL7 protein, humanChemokine CCL7adenylylationAMPylationFicParkinson's diseaseα-synuclein

Identifiers

PMID31034889
PMCPMC6554060
OpenAlexW2953355724

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.