Evidence map›Paper›PMID 29967539›Full record

ArticleNature structural & molecular biology2018

Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4.

Nicholas O Bodnar, Kelly H Kim, Zhejian Ji, Thomas E Wales, Vladimir Svetlov, Evgeny Nudler, John R Engen, Thomas Walz, Tom A Rapoport

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
5.3field-weighted citation impact, top 3% 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

67 citing papers in PubMed, 102 citations in OpenAlex.

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7 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

9 authors at 3 institutions in 1 country.

Nicholas O BodnarHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA, USA.
Kelly H KimLaboratory of Molecular Electron Microscopy, the Rockefeller University, New York, NY, USA.
Zhejian JiHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA, USA.ORCID 0000-0002-6835-0854
Thomas E WalesDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, USA.
Vladimir SvetlovHoward Hughes Medical Institute and Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, USA.ORCID 0000-0002-1977-4271
Evgeny NudlerHoward Hughes Medical Institute and Department of Biochemistry and Molecular Pharmacology, New York University School of Medicine, New York, NY, USA.
John R EngenDepartment of Chemistry and Chemical Biology, Northeastern University, Boston, MA, USA.ORCID 0000-0002-6918-9476
Thomas WalzLaboratory of Molecular Electron Microscopy, the Rockefeller University, New York, NY, USA. twalz@mail.rockefeller.edu.ORCID 0000-0003-2606-2835
Tom A RapoportHoward Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA, USA. tom_rapoport@hms.harvard.edu.ORCID 0000-0001-9911-4216
Howard Hughes Medical Institute · USNortheastern University · USRockefeller University · US

Funding

Medical Scientist Training ProgramT32GM007753 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WALENSKY, LOREN DAVID · 1985 to 2021
$50.0M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
PROTEIN TRANSPORT INTO MAMMALIAN ENDOPLASMIC RETICULUMR01GM052586 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI Tom A Rapoport · 1995 to 2026
$11.9M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR029205NIGMS NIH HHS P41 GM103403NIGMS NIH HHS R01 GM052586NIGMS NIH HHS T32 GM007753
6 · The paper itself

Abstract

Many polyubiquitinated proteins are extracted from membranes or complexes by the conserved ATPase Cdc48 (in yeast; p97 or VCP in mammals) before proteasomal degradation. Each Cdc48 hexamer contains two stacked ATPase rings (D1 and D2) and six N-terminal (N) domains. Cdc48 binds various cofactors, including the Ufd1-Npl4 heterodimer. Here, we report structures of the Cdc48-Ufd1-Npl4 complex from Chaetomium thermophilum. Npl4 interacts through its UBX-like domain with a Cdc48 N domain, and it uses two Zn

Indexed as

ChaetomiumCoenzymesCryoelectron MicroscopyCrystallography, X-RayFungal ProteinsModels, MolecularMultiprotein ComplexesMutagenesis, Site-DirectedNucleocytoplasmic Transport ProteinsProtein BindingProtein Interaction Domains and MotifsProtein Structure, QuaternarySaccharomyces cerevisiae ProteinsUbiquitinUnfolded Protein ResponseValosin Containing ProteinCDC48 protein, S cerevisiaeCoenzymesFungal ProteinsMultiprotein ComplexesNPL4 protein, S cerevisiaeNucleocytoplasmic Transport ProteinsSaccharomyces cerevisiae ProteinsUbiquitinUFD1 protein, S cerevisiaeValosin Containing ProteinVesicular Transport Proteins

Identifiers

PMID29967539
PMCPMC6044470
OpenAlexW2810410577

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.