Evidence map›Paper›PMID 32883800›Full record

ArticleMolecular & cellular proteomics : MCP2020

Stoichiometry of Nucleotide Binding to Proteasome AAA+ ATPase Hexamer Established by Native Mass Spectrometry.

Yadong Yu, Haichuan Liu, Zanlin Yu, H Ewa Witkowska, Yifan Cheng

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 59% 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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Review
  2. 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

5 authors at 2 institutions in 1 country.

Yadong YuDepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA.
Haichuan LiuDepartment of OBGYN & Reproductive Sci, Sandler-Moore MS Core Facility, University of California San Francisco, San Francisco, California, USA.
Zanlin YuDepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA.
H Ewa WitkowskaDepartment of OBGYN & Reproductive Sci, Sandler-Moore MS Core Facility, University of California San Francisco, San Francisco, California, USA. Electronic address: h_ewa_witkowska@yahoo.com.
Yifan ChengDepartment of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA; Howard Hughes Medical Institute, University of California San Francisco, San Francisco, California, USA. Electronic address: yifan.cheng@ucsf.edu.
University of California, San Francisco · USHoward Hughes Medical Institute · US

Funding

MOLECULAR CHAPERONES AND PROTEIN DEGRADATIONR01GM051923 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLDBERG, ALFRED L · 1995 to 2020
$10.1M
Mechanism of gate-opening in the 20S proteasome induced by the proteasomal ATPaseR01GM082893 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI CHENG, YIFAN · 2008 to 2017
$2.8M
Structural Characterization of Polypeptides, Protein Complexes, OligosaccharidesS10RR029446 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI WITKOWSKA, H. EWA · 2010 to 2010
$1.0M
Howard Hughes Medical InstituteNCRR NIH HHS S10 RR029446NIGMS NIH HHS R01 GM051923NIGMS NIH HHS R01 GM082893
6 · The paper itself

Abstract

AAA+ ATPases constitute a large family of proteins that are involved in a plethora of cellular processes including DNA disassembly, protein degradation and protein complex disassembly. They typically form a hexametric ring-shaped structure with six subunits in a (pseudo) 6-fold symmetry. In a subset of AAA+ ATPases that facilitate protein unfolding and degradation, six subunits cooperate to translocate protein substrates through a central pore in the ring. The number and type of nucleotides in an AAA+ ATPase hexamer is inherently linked to the mechanism that underlies cooperation among subunits and couples ATP hydrolysis with substrate translocation. We conducted a native MS study of a monodispersed form of PAN, an archaeal proteasome AAA+ ATPase, to determine the number of nucleotides bound to each hexamer of the WT protein. We utilized ADP and its analogs (TNP-ADP and mant-ADP), and a nonhydrolyzable ATP analog (AMP-PNP) to study nucleotide site occupancy within the PAN hexamer in ADP- and ATP-binding states, respectively. Throughout all experiments we used a Walker A mutant (PAN

Indexed as

Mass SpectrometryProtein MultimerizationAdenosine DiphosphateAdenylyl ImidodiphosphateArchaeal ProteinsATPases Associated with Diverse Cellular ActivitiesLigandsMethanocaldococcusMutant ProteinsNucleotidesProteasome Endopeptidase ComplexProtein BindingProtein SubunitsSpectrometry, Mass, Electrospray IonizationAdenosine DiphosphateAdenylyl ImidodiphosphateArchaeal ProteinsATPases Associated with Diverse Cellular ActivitiesLigandsMutant ProteinsNucleotidesProteasome Endopeptidase ComplexProtein SubunitsAAA+ ATPaseArchaebacteria*cooperativityelectron microscopymacromolecular complex analysismass spectrometrynative mass spectrometrynon-covalent interaction MS*nucleotide bindingproteasomestoichiometry

Identifiers

PMID32883800
PMCPMC7710143
OpenAlexW3083197451

What OpenQuestion holds

Textmetadata
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.