Evidence map›Paper›PMID 10588706›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1999

Correlation of the structural and functional domains in the membrane protein Vpu from HIV-1.

F M Marassi, C Ma, H Gratkowski, S K Straus, K Strebel, M Oblatt-Montal, M Montal, S J Opella

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing 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

70 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
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  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015
    Review
  16. Review
  17. Article
  18. HIV-1 Vpu - an ion channel in search of a job.Biochimica et biophysica acta · 2014
    Review
  19. Review
  20. Article

10 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

8 authors.

F M MarassiDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104, USA.
C Ma
H Gratkowski
S K Straus
K Strebel
M Oblatt-Montal
M Montal
S J Opella

Funding

WORKSHOP ON BIOLOGICAL SOLID STATE NMR SPECTROSCOPYP41RR009793 · NCRR · UNIVERSITY OF PENNSYLVANIA · PI OPELLA, STANLEY J · 1994 to 2002
$2.0M
STRUCTURE DETERMINATION OF VPU FROM HIV 1P01GM056538 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI MONTAL, MAURICIO S · 1997 to 2002
$1.6M
Molecular Analysis Of Retroviral Genes &Their ProductsZ01AI000669 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI STREBEL, KLAUS · 1993 to 2008
$852k
NCRR NIH HHS P41RR09793NIGMS NIH HHS P01 GM56538
6 · The paper itself

Abstract

Vpu is an 81-residue membrane protein encoded by the HIV-1 genome. NMR experiments show that the protein folds into two distinct domains, a transmembrane hydrophobic helix and a cytoplasmic domain with two in-plane amphipathic alpha-helices separated by a linker region. Resonances in one-dimensional solid-state NMR spectra of uniformly (15)N labeled Vpu are clearly segregated into two bands at chemical shift frequencies associated with NH bonds in a transmembrane alpha-helix, perpendicular to the membrane surface, and with NH bonds in the cytoplasmic helices parallel to the membrane surface. Solid-state NMR spectra of truncated Vpu(2-51) (residues 2-51), which contains the transmembrane alpha-helix and the first amphipathic helix of the cytoplasmic domain, and of a construct Vpu(28-81) (residues 28-81), which contains only the cytoplasmic domain, support this structural model of Vpu in the membrane. Full-length Vpu (residues 2-81) forms discrete ion-conducting channels of heterogeneous conductance in lipid bilayers. The most frequent conductances were 22 +/- 3 pS and 12 +/- 3 pS in 0.5 M KCl and 29 +/- 3 pS and 12 +/- 3 pS in 0.5 M NaCl. In agreement with the structural model, truncated Vpu(2-51), which has the transmembrane helix, forms discrete channels in lipid bilayers, whereas the cytoplasmic domain Vpu(28-81), which lacks the transmembrane helix, does not. This finding shows that the channel activity is associated with the transmembrane helical domain. The pattern of channel activity is characteristic of the self-assembly of conductive oligomers in the membrane and is compatible with the structural and functional findings.

Indexed as

Amino Acid SequenceCD4 AntigensHIV-1Human Immunodeficiency Virus ProteinsIon ChannelsLipid BilayersMagnetic Resonance SpectroscopyMolecular Sequence DataViral Regulatory and Accessory ProteinsViroporin ProteinsCD4 AntigensHuman Immunodeficiency Virus ProteinsIon ChannelsLipid BilayersViral Regulatory and Accessory ProteinsViroporin Proteinsvpu protein, Human immunodeficiency virus 1

Identifiers

PMID10588706
PMCPMC24437

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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.