Evidence map›Paper›PMID 18687679›Full record

ArticleThe Journal of biological chemistry2008

NMR structure of the N-terminal coiled coil domain of the Andes hantavirus nucleocapsid protein.

Yu Wang, Daniel M Boudreaux, D Fernando Estrada, Chet W Egan, Stephen C St Jeor, Roberto N De Guzman

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Structural characterization of the self-association domain of swallow.Protein science : a publication of the Protein Society · 2021
    Article
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  5. Article
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  7. Article
  8. 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

6 authors.

Yu WangDepartment of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045, USA.
Daniel M Boudreaux
D Fernando Estrada
Chet W Egan
Stephen C St Jeor
Roberto N De Guzman

Funding

Vaccines and Diagnostics TrialsU54AI065359 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI BARBOUR, ALAN G. · 2005 to 2013
$88.8M
NIAID NIH HHS AI057160NIAID NIH HHS AI65359
6 · The paper itself

Abstract

The hantaviruses are emerging infectious viruses that in humans can cause a cardiopulmonary syndrome or a hemorrhagic fever with renal syndrome. The nucleocapsid (N) is the most abundant viral protein, and during viral assembly, the N protein forms trimers and packages the viral RNA genome. Here, we report the NMR structure of the N-terminal domain (residues 1-74, called N1-74) of the Andes hantavirus N protein. N1-74 forms two long helices (alpha1 and alpha2) that intertwine into a coiled coil domain. The conserved hydrophobic residues at the helix alpha1-alpha2 interface stabilize the coiled coil; however, there are many conserved surface residues whose function is not known. Site-directed mutagenesis, CD spectroscopy, and immunocytochemistry reveal that a point mutation in the conserved basic surface formed by Arg22 or Lys26 lead to antibody recognition based on the subcellular localization of the N protein. Thus, Arg22 and Lys26 are likely involved in a conformational change or molecular recognition when the N protein is trafficked from the cytoplasm to the Golgi, the site of viral assembly and maturation.

Indexed as

AnimalsArginineChlorocebus aethiopsCircular DichroismCOS CellsCytoplasmGolgi ApparatusLysineMagnetic Resonance SpectroscopyMutagenesis, Site-DirectedNucleocapsid ProteinsOrthohantavirusProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryArginineLysineNucleocapsid Proteins

Identifiers

PMID18687679
PMCPMC2568929

What Socratic holds

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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 Socratic graph.