Evidence map›Paper›PMID 30315172›Full record

ArticleNature communications2018

Precisely measured protein lifetimes in the mouse brain reveal differences across tissues and subcellular fractions.

Eugenio F Fornasiero, Sunit Mandad, Hanna Wildhagen, Mihai Alevra, Burkhard Rammner, Sarva Keihani, Felipe Opazo, Inga Urban, Till Ischebeck, M Sadman Sakib and 14 more

Abstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 208 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
208citing papers in PubMed, 1 pooled it
–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

208 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Shift of the insoluble content of the proteome in the aging mouse brain.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Pooled it
  2. Article
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  4. Article
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  7. Sex- and experience-dependent regulation of synaptic protein turnover.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  8. Mass spectrometry proteomics for studying mitostasis.Protein science : a publication of the Protein Society · 2026
    Review
  9. Article
  10. Article
  11. Review
  12. Age-based approach to characterize the dynamics of cellular processes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Disruption of a selective vesicle pool upon retrograde amnesia dissociates memory at presynaptic terminals.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  19. Ribosome Molecular Aging Shapes Translation Dynamics.bioRxiv : the preprint server for biology · 2026
    Article
  20. Review

148 more citing papers are in PubMed but not listed here.

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

24 authors.

Eugenio F FornasieroDepartment of Neuro- and Sensory Physiology, University Medical Center Göttingen, Cluster of Excellence Nanoscale Microscopy and Molecular Physiology of the Brain, 37073, Göttingen, Germany. efornas@gwdg.de.ORCID http://orcid.org/0000-0001-7643-4962
Sunit MandadDepartment of Neuro- and Sensory Physiology, University Medical Center Göttingen, Cluster of Excellence Nanoscale Microscopy and Molecular Physiology of the Brain, 37073, Göttingen, Germany.
Hanna WildhagenDepartment of Neuro- and Sensory Physiology, University Medical Center Göttingen, Cluster of Excellence Nanoscale Microscopy and Molecular Physiology of the Brain, 37073, Göttingen, Germany.
Mihai AlevraDepartment of Neuro- and Sensory Physiology, University Medical Center Göttingen, Cluster of Excellence Nanoscale Microscopy and Molecular Physiology of the Brain, 37073, Göttingen, Germany.
Burkhard RammnerDepartment of Neuro- and Sensory Physiology, University Medical Center Göttingen, Cluster of Excellence Nanoscale Microscopy and Molecular Physiology of the Brain, 37073, Göttingen, Germany.
Sarva KeihaniDepartment of Neuro- and Sensory Physiology, University Medical Center Göttingen, Cluster of Excellence Nanoscale Microscopy and Molecular Physiology of the Brain, 37073, Göttingen, Germany.
Felipe OpazoDepartment of Neuro- and Sensory Physiology, University Medical Center Göttingen, Cluster of Excellence Nanoscale Microscopy and Molecular Physiology of the Brain, 37073, Göttingen, Germany.ORCID http://orcid.org/0000-0002-4968-9713
Inga UrbanGenes and Behavior Department, Max Planck Institute of Biophysical Chemistry, 37073, Göttingen, Germany.
Till IschebeckDepartment of Plant Biochemistry, Albrecht-von-Haller-Institute, Georg-August-University, 37073, Göttingen, Germany.
M Sadman SakibLaboratory of Epigenetics in Neurodegenerative Diseases, German Center for Neurodegenerative Diseases (DZNE), 37075, Göttingen, Germany.
Maryam K FardGerman Center for Neurodegenerative Disease (DZNE), 81377, Munich, Germany.
Koray KirliDepartment of Cellular Logistics, Max Planck Institute for Biophysical Chemistry, 37077, Göttingen, Germany.ORCID http://orcid.org/0000-0002-2289-0652
Tonatiuh Pena CentenoLaboratory of Computational Systems Biology, German Center for Neurodegenerative Diseases (DZNE), 37075, Göttingen, Germany.ORCID http://orcid.org/0000-0002-9329-8912
Ramon O VidalLaboratory of Computational Systems Biology, German Center for Neurodegenerative Diseases (DZNE), 37075, Göttingen, Germany.
Raza-Ur RahmanLaboratory of Computational Systems Biology, German Center for Neurodegenerative Diseases (DZNE), 37075, Göttingen, Germany.
Eva BenitoLaboratory of Epigenetics in Neurodegenerative Diseases, German Center for Neurodegenerative Diseases (DZNE), 37075, Göttingen, Germany.
André FischerLaboratory of Epigenetics in Neurodegenerative Diseases, German Center for Neurodegenerative Diseases (DZNE), 37075, Göttingen, Germany.
Sven DennerleinDepartment of Cellular Biochemistry, University Medical Center Göttingen, 37077, Göttingen, Germany.
Peter RehlingDepartment of Cellular Biochemistry, University Medical Center Göttingen, 37077, Göttingen, Germany.ORCID http://orcid.org/0000-0001-5661-5272
Ivo FeussnerDepartment of Plant Biochemistry, Albrecht-von-Haller-Institute, Georg-August-University, 37073, Göttingen, Germany.ORCID http://orcid.org/0000-0002-9888-7003
Stefan BonnLaboratory of Computational Systems Biology, German Center for Neurodegenerative Diseases (DZNE), 37075, Göttingen, Germany.ORCID http://orcid.org/0000-0003-4366-5662
Mikael SimonsGerman Center for Neurodegenerative Disease (DZNE), 81377, Munich, Germany.
Henning UrlaubDepartment of Clinical Chemistry, University Medical Center Göttingen, 37077, Göttingen, Germany. henning.urlaub@med.uni-goettingen.de.
Silvio O RizzoliDepartment of Neuro- and Sensory Physiology, University Medical Center Göttingen, Cluster of Excellence Nanoscale Microscopy and Molecular Physiology of the Brain, 37073, Göttingen, Germany. srizzol@gwdg.de.

Funding

EC | European Research Council (ERC) ERC-2013-CoG
6 · The paper itself

Abstract

The turnover of brain proteins is critical for organism survival, and its perturbations are linked to pathology. Nevertheless, protein lifetimes have been difficult to obtain in vivo. They are readily measured in vitro by feeding cells with isotopically labeled amino acids, followed by mass spectrometry analyses. In vivo proteins are generated from at least two sources: labeled amino acids from the diet, and non-labeled amino acids from the degradation of pre-existing proteins. This renders measurements difficult. Here we solved this problem rigorously with a workflow that combines mouse in vivo isotopic labeling, mass spectrometry, and mathematical modeling. We also established several independent approaches to test and validate the results. This enabled us to measure the accurate lifetimes of ~3500 brain proteins. The high precision of our data provided a large set of biologically significant observations, including pathway-, organelle-, organ-, or cell-specific effects, along with a comprehensive catalog of extremely long-lived proteins (ELLPs).

Indexed as

Animalsbeta-GalactosidaseBrainComputational BiologyHippocampusMaleMass SpectrometryMiceModels, Theoreticalbeta-Galactosidase

Identifiers

PMID30315172
PMCPMC6185916

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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.