Evidence map›Paper›PMID 33618608›Full record

ArticleAutophagy2021

Mouse models for hereditary spastic paraplegia uncover a role of PI4K2A in autophagic lysosome reformation.

Mukhran Khundadze, Federico Ribaudo, Adeela Hussain, Henry Stahlberg, Nahal Brocke-Ahmadinejad, Patricia Franzka, Rita-Eva Varga, Milena Zarkovic, Thanakorn Pungsrinont, Miriam Kokal and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Autophagy, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 32 citations in OpenAlex.

  1. Review
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  4. Phosphatidylinositol 4-phosphate; A minor lipid with multiple personalities.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  5. Lysosomal Repair in Health and Disease.Journal of cellular physiology · 2025
    Review
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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

14 authors at 3 institutions in 2 countries.

Mukhran KhundadzeInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Federico RibaudoInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Adeela HussainInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Henry StahlbergInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Nahal Brocke-AhmadinejadCore Facility Mass Spectrometry, Institute of Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, Bonn, Germany.
Patricia FranzkaInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Rita-Eva VargaInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Milena ZarkovicInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Thanakorn PungsrinontInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Miriam KokalInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Ian G GanleyMRC Protein Phosphorylation and Ubiquitylation Unit, School of Life Sciences, University of Dundee, Dundee, Scotland.
Christian BeetzInstitute of Clinical Chemistry, University Hospital Jena, Friedrich-Schiller-University Jena, Germany; Current Affiliation: Centogene GmbH, Rostock, Germany.
Marc SylvesterCore Facility Mass Spectrometry, Institute of Biochemistry and Molecular Biology, Medical Faculty, University of Bonn, Bonn, Germany.
Christian A HübnerInstitute of Human Genetics, University Hospital Jena, Friedrich-Schiller-University Jena, Jena, Germany.
Friedrich Schiller University Jena · DEUniversity of Bonn · DEMRC Protein Phosphorylation and Ubiquitylation Unit · GB

Funding

Medical Research Council MC_UU_00018/2
6 · The paper itself

Abstract

Hereditary spastic paraplegia (HSP) denotes genetically heterogeneous disorders characterized by leg spasticity due to degeneration of corticospinal axons. SPG11 and SPG15 have a similar clinical course and together are the most prevalent autosomal recessive HSP entity. The respective proteins play a role for macroautophagy/autophagy and autophagic lysosome reformation (ALR). Here, we report that

Indexed as

AutophagyAnimalsBlotting, WesternDisease Models, AnimalFlow CytometryLysosomesMass SpectrometryMiceMice, Inbred C57BLMice, KnockoutMinor Histocompatibility AntigensPhosphotransferases (Alcohol Group Acceptor)ProteinsSpastic Paraplegia, HereditaryMinor Histocompatibility Antigensphosphatidylinositol phosphate 4-kinasePhosphotransferases (Alcohol Group Acceptor)ProteinsSPG11 protein, mouseAutophagylysosomeneurodegenerationPI4K2Aspg11spg15

Identifiers

PMID33618608
PMCPMC8632344
OpenAlexW3131259014

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.