Evidence map›Paper›PMID 10906196›Full record

ArticleJournal of virology2000

Assembly of retrovirus capsid-nucleocapsid proteins in the presence of membranes or RNA.

G Zuber, J McDermott, S Karanjia, W Zhao, M F Schmid, E Barklis

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  4. HIV-1 matrix protein binding to RNA.Journal of molecular biology · 2011
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  17. RNA is a structural element in retrovirus particles.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  18. 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

6 authors at 4 institutions in 2 countries.

G ZuberLaboratoire de Chimie Genetique, Faculté de Pharmacie, University of Strasbourg, Strasbourg, France.
J McDermott
S Karanjia
W Zhao
M F Schmid
E Barklis
Oregon Health & Science University · USVollum Institute · USBaylor College of Medicine · USLaboratoire de Chimie · FR

Funding

RETROVIRUS STRUCTURAL PROTEIN INTERACTIONSR01GM052914 · NIGMS · OREGON HEALTH AND SCIENCE UNIVERSITY · PI BARKLIS, ERIC W · 1995 to 2001
$402k
TRANSMISSION ELECTRON MICROSCOPES10RR012935 · NCRR · OREGON HEALTH AND SCIENCE UNIVERSITY · PI BARKLIS, ERIC W · 1998 to 1998
–
NCRR NIH HHS 1 S10 RR12935NIGMS NIH HHS 5RO1 GM 52914
6 · The paper itself

Abstract

Retrovirus Gag precursor (PrGag) proteins direct the assembly of roughly spherical immature virus particles, while after proteolytic processing events, the Gag capsid (CA) and nucleocapsid (NC) domains condense on viral RNAs to form mature retrovirus core structures. To investigate the process of retroviral morphogenesis, we examined the properties of histidine-tagged (His-tagged) Moloney murine leukemia (M-MuLV) capsid plus nucleocapsid (CANC) (His-MoCANC) proteins in vitro. The His-MoCANC proteins bound RNA, possessed nucleic acid-annealing activities, and assembled into strand, circle (or sphere), and tube forms in the presence of RNA. Image analysis of electron micrographs revealed that tubes were formed by cage-like lattices of CANC proteins surrounding at least two different types of protein-free cage holes. By virtue of a His tag association with nickel-chelating lipids, His-MoCANC proteins also assembled into planar sheets on lipid monolayers, mimicking the membrane-associated immature PrGag protein forms. Membrane-bound His-MoCANC proteins organized into two-dimensional (2D) cage-like lattices that were closely related to the tube forms, and in the presence of both nickel-chelating lipids and RNAs, 2D lattice forms appeared similar to lattices assembled in the absence of RNA. Our observations are consistent with a M-MuLV morphogenesis model in which proteolytic processing of membrane-bound Gag proteins permits CA and NC domains to rearrange from an immature spherical structure to a condensed mature form while maintaining local protein-protein contacts.

Indexed as

Virus AssemblyAmino Acid SequenceAnimalsCapsidCell MembraneCrystallographyHistidineImage Processing, Computer-AssistedLipid BilayersMiceMicroscopy, ElectronMolecular Sequence DataMoloney murine leukemia virusNucleocapsidRNAHistidineLipid BilayersRNA

Identifiers

PMID10906196
PMCPMC112263
OpenAlexW1966880904

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.